|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
9.74e-148 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 410.21 E-value: 9.74e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
5.00e-124 |
|
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: 350.17 E-value: 5.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
2.23e-112 |
|
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: 320.73 E-value: 2.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGM 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
2.48e-99 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 288.10 E-value: 2.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RRE-IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMkKRVIAIEDGMIVRDEA 220
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARA-DRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
4.01e-94 |
|
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: 274.37 E-value: 4.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKE-IPYL 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVnSMKKRVIAIEDGMI 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
4.87e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 235.36 E-value: 4.87e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:COG1135 1 MIELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
3.06e-76 |
|
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: 229.78 E-value: 3.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
4.20e-73 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 222.24 E-value: 4.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENV--------AFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-218 |
4.85e-72 |
|
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: 218.74 E-value: 4.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRREI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQD-----FKLlptlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG1122 78 GLVFQNpddqlFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
1.68e-70 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 214.74 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
2.58e-69 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 215.82 E-value: 2.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:PRK11153 1 MIELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-218 |
4.78e-68 |
|
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: 208.96 E-value: 4.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFAL--------EVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
4.57e-67 |
|
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: 206.77 E-value: 4.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENV--------AFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
2.14e-66 |
|
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: 203.91 E-value: 2.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeiPYLRREI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
6.26e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 207.26 E-value: 6.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYlRRE 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 161 ADEPTGNLDP----DTSWEIMKTLEEInnrGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG3842 159 LDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
1.72e-65 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 203.01 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYP---NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsikekEIPYL 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK--------PVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHN 196
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
2.11e-64 |
|
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: 198.85 E-value: 2.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKL-LPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-220 |
4.87e-63 |
|
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: 196.12 E-value: 4.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RRE-IGVVFQDFKLLPTLTVFENVAFALEVIGEQPqiIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVnSMKKRVIAIEDGMIVRDEA 220
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTA 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
5.87e-63 |
|
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: 195.97 E-value: 5.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDLSeAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNkeiVNSMKK---RVIAIEDGMIV 216
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHD---LDSAFAiadRVAVLADGKII 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.39e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.21 E-value: 1.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGsIKEKEIPYLRRE 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFAL-EVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHN----KEIVNsmkkRVIAIEDGMIV 216
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREVAD----RVVFMDGGRIV 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
7.17e-62 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 192.72 E-value: 7.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQD--FKLLPTLTVFENVAFALEV--IGEQPQIIKKKVLDVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
5.91e-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: 5.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-196 |
6.01e-61 |
|
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: 190.38 E-value: 6.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsikekEIPYLR 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--------PVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHN 196
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHD 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
3.40e-60 |
|
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: 197.05 E-value: 3.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYP----NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPY 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQD-FK-LLPTLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSI 152
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-218 |
3.60e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.73 E-value: 3.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipyLRREI 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-195 |
4.40e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 192.21 E-value: 4.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylrRE 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATH 195
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTH 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
3.52e-59 |
|
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: 186.17 E-value: 3.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpnGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:cd03261 1 IELRGLTKSF--GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQ-IIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEeEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.78e-57 |
|
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: 180.08 E-value: 1.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkEKEIPYLRREI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFAlevigeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
2.98e-57 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 180.80 E-value: 2.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgSIKEKEIPYLRREI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFAL-EVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
7.19e-55 |
|
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: 174.75 E-value: 7.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNgVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylrREI 81
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
1.96e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 177.65 E-value: 1.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNgVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeIPYLRREI 81
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----LPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 162 DEPTGNLDPDTSWEI----MKTLEEInnrGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG1118 158 DEPFGALDAKVRKELrrwlRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-210 |
2.42e-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: 167.79 E-value: 2.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE-IG 82
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 163 EPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNsMKKRVIAI 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
3.46e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 175.86 E-value: 3.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPS---KGKILINNKDLGSIKEKEipy 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQDFKL-LPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-195 |
4.31e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 170.27 E-value: 4.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500859999 159 VIADEPTGNLDP-------DtswEIMKTLEEInnrGTTVVMATH 195
Cdd:COG1125 158 LLMDEPFGALDPitreqlqD---ELLRLQREL---GKTIVFVTH 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
2.72e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.42 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL--GSIKEKEIpylR 78
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLI---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
4.73e-51 |
|
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: 166.45 E-value: 4.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgSIKEKEIPYLRRE 80
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:TIGR04520 79 VGMVFQnpDNQFVGA-TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMATHN-KEIVNSmkKRVIAIEDGMIVRD 218
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDmEEAVLA--DRVIVMNKGKIVAE 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
9.77e-51 |
|
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: 164.82 E-value: 9.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNgVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylrREI 81
Cdd:cd03296 3 IEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEV--IGEQP--QIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkpRSERPpeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-218 |
1.17e-50 |
|
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: 165.22 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFaleviGEQPQII---------KKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARS 151
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVAL-----GRYPHLGlfgrpsaedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 152 IVNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
1.49e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 164.42 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGvKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILI-NNK-DLGS-IKEKEIPYLR 78
Cdd:PRK11124 3 IQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIaGNHfDFSKtPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
1.93e-50 |
|
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: 161.28 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRREIGVVFQDFKLLPTLTVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 98 ENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKA----RQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
4.71e-50 |
|
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: 163.24 E-value: 4.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQL--KHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
5.89e-50 |
|
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: 162.35 E-value: 5.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKiYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDLGSIKEKEIpY 76
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVL-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQDFKLLPtLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQL--KHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:cd03260 79 LRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLkEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
9.21e-50 |
|
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: 172.33 E-value: 9.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEV-YKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekEIPYLRRE 80
Cdd:COG2274 474 IELENVsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLG------DPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMkKRVIAIEDGMIVRD-------EARG 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDgtheellARKG 701
|
..
gi 500859999 223 EY 224
Cdd:COG2274 702 LY 703
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-216 |
1.92e-49 |
|
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: 162.43 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE-IGVVFQDFKLLPTLT 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWE 175
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500859999 176 IMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03294 199 MQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
4.32e-49 |
|
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: 160.74 E-value: 4.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyL 77
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFK--LLPTLTVFENVAFALEVIGEQPqiIKKKVLDVLDLVQLKHKAR-QFPDQLSGGEQQRVSIARSIVN 154
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSFLdRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
4.72e-49 |
|
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: 158.32 E-value: 4.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVafalevigeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMkKRVIAIEDG 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
8.01e-49 |
|
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: 157.56 E-value: 8.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGvKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipyLRREI 81
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE----VKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVafalevigeqpqiikkkvldvldlvqlkhkarqfpdQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-218 |
4.51e-48 |
|
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: 156.06 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQdfkllp 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LARKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 tltvfenvafalevigeqpqiikkkvldVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 173 SWEIMKTLEEINN-RGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03214 133 QIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
4.54e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 159.15 E-value: 4.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY----PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQdF--KLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-225 |
1.43e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 156.71 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLG---SIKEKEIPYLR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVrdeargEYG 225
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII------EQG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-218 |
1.66e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.50 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREI 81
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
1.15e-46 |
|
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: 154.63 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsiKEKEIPYLRRE 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-220 |
1.82e-46 |
|
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: 153.75 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPylRREIGVVFQDFKLLPT 93
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEVIGEQPQI----------IKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIA------IEDG---MIVRDEA 220
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVldqgrvIAEGtpdEVRNNPR 235
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
4.20e-46 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 161.82 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYL 77
Cdd:PRK10535 4 LLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RRE-IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmKKRVIAIEDGMIVRD 218
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
6.22e-46 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 159.92 E-value: 6.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDfkllPTL---TVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVS 147
Cdd:COG4988 414 AWVPQN----PYLfagTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMkKRVIAIEDGMIV 216
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQA-DRILVLDDGRIV 550
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-216 |
9.78e-46 |
|
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: 152.00 E-value: 9.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRREI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQlkhkarQFPDQ-----------LSGGEQQRVSIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRPDATDEEVIEAAKAAQIHDKIM------RFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKkrVIAIEDGMIV 216
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADK--IIVLKDGRIV 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-218 |
2.11e-45 |
|
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: 153.80 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 33 VVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQ 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 113 IIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVV 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180
....*....|....*....|....*..
gi 500859999 192 MATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQI 182
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
2.65e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.01 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSikekeipyLRRE 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPT--LTVFENVAFALevIGEQP------QIIKKKVLDVLDLVQLKHKA-RQFpDQLSGGEQQRVSIARS 151
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGR--YGRRGlfrrpsRADREAVDEALERVGLEDLAdRPI-GELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 152 IVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.10e-44 |
|
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: 156.85 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLA------RPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMkKRVIAIEDGMIV 216
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
1.11e-44 |
|
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: 146.62 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEVYKIYPNGvKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIG 82
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQdfkllptltvfenvafalevigeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 163 EPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-213 |
1.95e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 148.43 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLR-REIGVVFQDFKLLPTLTVFEN 99
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKT 179
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 500859999 180 LEEINNR-GTTVVMATHNKEIVNSMkKRVIAIEDG 213
Cdd:PRK11629 188 LGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-216 |
3.19e-44 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 151.34 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREIGVVFQDFKLLPTLTV 96
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI-----TRLPPQKRDYGIVFQSYALFPNLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTS--- 173
Cdd:TIGR03265 94 ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVRehl 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500859999 174 -WEIMKTLEEInnrGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:TIGR03265 174 rTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-216 |
3.95e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.32 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLpTLTVFENVAFALEVIGEQpqiikkKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYGRPDATDE------EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNkeiVNSMKK--RVIAIEDGMIV 216
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHR---LSTIRNadRILVLDDGRIV 553
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-216 |
6.69e-44 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 146.67 E-value: 6.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL-GSIKEKEIPYLRREIGVVFQDFKLLPTLTVFENVAFALE 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 106 VIGEQPQiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-N 184
Cdd:cd03297 102 RKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkK 179
|
170 180 190
....*....|....*....|....*....|..
gi 500859999 185 NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-217 |
1.20e-43 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 150.00 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRR-EIGVVFQDFKLLP 92
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 173 SWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:TIGR01186 165 RDSMQDELKKLQaTLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQ 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-215 |
1.86e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.46 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNgVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylrREI 81
Cdd:PRK10851 3 IEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIG--EQPQ--IIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVLPrrERPNaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-208 |
6.38e-43 |
|
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: 147.12 E-value: 6.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 8 YKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKP---SKGKILINNKDLGSIKEKEIPYLR-REIGV 83
Cdd:COG0444 11 FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQD-FKLL-PTLTVFENVAFALEV-IGEQPQIIKKKVLDVLDLVQL---KHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:COG0444 91 IFQDpMTSLnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMATHNKEIVNSMKKRVI 208
Cdd:COG0444 171 LLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-216 |
1.35e-42 |
|
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: 144.02 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREIGVVFQDFKLLPTLTVFEN 99
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKT 179
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 500859999 180 LEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03299 172 LKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
2.29e-42 |
|
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: 141.79 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKeKEIPYLRREIGVVFQ--DF 88
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-KGLLERRQRVGLVFQdpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 89 KLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|.
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEI 199
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
18-215 |
2.60e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeIPYLRREIGVVFQDfkllPTL--- 94
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQE----PALwgg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALEVIGEQPQiiKKKVLDVLDLVQLKHKARQFP-DQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTS 173
Cdd:COG4619 89 TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500859999 174 WEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:COG4619 167 RRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-209 |
3.71e-42 |
|
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: 141.90 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGsikekeipYLRREIGVVFQDFKLLP 92
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 T--LTVFENVAFAL----EVIGEQPQIIKKKVLDVLDLVQLKHKA-RQFpDQLSGGEQQRVSIARSIVNSPEVVIADEPT 165
Cdd:cd03235 82 DfpISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELAdRQI-GELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 166 GNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVN-------SMKKRVIA 209
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLeyfdrvlLLNRTVVA 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
2.45e-41 |
|
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: 140.20 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYLRREI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 162 DEPTGNLDPDTS---WEIMKTLEEINnrGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:cd03265 156 DEPTIGLDPQTRahvWEYIEKLKEEF--GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
2.49e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.04 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIK-----EKEIP 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 YLRREIGVVFQDFKLLPTLTVFENVAfalevigEQPQIIKKKVLD--------VLDLVQLKHKARQFPDQLSGGEQQRVS 147
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENII-------EGPVIVKGEPKEeatarareLLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-196 |
2.56e-41 |
|
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: 139.95 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSikekEIPYLRRE 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHN 196
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHS 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
4.58e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 139.89 E-value: 4.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpnGVKAINgINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYlRRE 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PA-ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALE----VIGEQpqiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRpglkLTAEQ----RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-215 |
2.90e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 138.56 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL-------GSIK---EKEIPYLRREIGVVF 85
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 86 QDFKLLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-217 |
3.01e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 141.51 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYlRRE 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP----PY-QRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 161 ADEPTGNLDPD----TSWEIMKTLEEInnrGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
1.64e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 136.53 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikekEIPYL 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV------TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RReiGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500859999 158 VVIADEPTGNLDPDTSwEIMKT--LEEINNRGTTVVMATHNKE 198
Cdd:COG4525 155 FLLMDEPFGALDALTR-EQMQEllLDVWQRTGKGVFLITHSVE 196
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-216 |
1.76e-39 |
|
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: 137.91 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipyLRREIGVVFQDF 88
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 89 KLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-216 |
2.98e-39 |
|
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: 135.05 E-value: 2.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQ-----LKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA--DKILVLDDGKII 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
5.21e-39 |
|
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: 134.52 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnkdlgSIKEKEIPYLRREIGVVFQDFKLLPTLTVF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV--------ILEGKQITEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 ENVAFALEVI------GEQPQIIKkkvlDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:TIGR01184 73 ENIALAVDRVlpdlskSERRAIVE----EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500859999 172 TSWEIMKTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR01184 149 TRGNLQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-216 |
5.62e-39 |
|
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: 135.17 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYLRREIGVV--FQDFKLL 91
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP----PHRIARLGIArtFQNPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTLTVFENVAFALEV---------------IGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG0411 92 PELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.09e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.82 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgSIKEKEIPYLRRE 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK13639 80 VGIVFQnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-195 |
1.44e-38 |
|
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: 132.29 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIK--MMYREEKPSKGKILINNKDLGSIKekeipyLRREIGVVFQDFKLLPTLT 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLDKRS------FRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFALEVIGeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWE 175
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|
gi 500859999 176 IMKTLEEINNRGTTVVMATH 195
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.95e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.09 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpylRREI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDfkllP-----TLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:PRK13647 82 GLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-169 |
3.59e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.93 E-value: 3.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikeKEIPYLRREIGV 83
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
....*.
gi 500859999 164 PTGNLD 169
Cdd:PRK11000 160 PLSNLD 165
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
7.35e-38 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 131.40 E-value: 7.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYP----NGVK--AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK----DLGSIK 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 71 EKEIPYLRR-EIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRVSI 148
Cdd:COG4778 84 PREILALRRrTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 149 ARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
1.15e-37 |
|
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: 131.36 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVyKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKG---KILinNKDLG--SIKEkeip 75
Cdd:COG1119 3 LLELRNV-TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGgeDVWE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 yLRREIGVVFQDF--KLLPTLTVFENV---AFAleVIG--EQP-QIIKKKVLDVLDLVQLKHKA-RQFpDQLSGGEQQRV 146
Cdd:COG1119 76 -LRKRIGLVSPALqlRFPRDETVLDVVlsgFFD--SIGlyREPtDEQRERARELLELLGLAHLAdRPF-GTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRG-TTVVMATHNKE-IVNSMkKRVIAIEDGMIVRD 218
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAA 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-220 |
1.48e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 130.67 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLR-REIGVVFQDFKLLPTLTV 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEI 176
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500859999 177 MKTLEEINNR-GTTVVMATHNKEIVNSMKKRvIAIEDGMIvRDEA 220
Cdd:PRK10584 186 ADLLFSLNREhGTTLILVTHDLQLAARCDRR-LRLVNGQL-QEEA 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-216 |
1.75e-37 |
|
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: 130.25 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpyLRREIGVVFQDFKLLPT 93
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEVIGEQPqiiKKKVLD-VLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:cd03224 90 LTVEENLLLGAYARRRAK---RKARLErVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500859999 172 TSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-217 |
2.02e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.69 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL--GSIKEkeipylrR 79
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQ-------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
2.43e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.43 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylrRE 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 500859999 161 ADEPTGNLD 169
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
3.21e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 131.75 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY----PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKD------------ 65
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 66 -LGSI--------KEKEIPYLRREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQ- 133
Cdd:PRK13651 83 vLEKLviqktrfkKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 134 FPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*
gi 500859999 214 MIVRD 218
Cdd:PRK13651 242 KIIKD 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-169 |
4.86e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD-FKLL-P 92
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpYASLnP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQLK--HkARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:COG4608 111 RMTVGDIIAEPLRIHGLASkAERRERVAELLELVGLRpeH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
4.91e-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: 128.94 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNgVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREI 81
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GvvfqdfkLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03269 80 G-------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 162 DEPTGNLDPdTSWEIMKT-LEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03269 153 DEPFSGLDP-VNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
6.23e-37 |
|
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: 128.46 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGvKAINGINVSIHPGEFVyVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipyLRREI 81
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-198 |
7.11e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 128.37 E-value: 7.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVyKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKP---SKGKILINNKDLGsikekEIPYL 77
Cdd:COG4136 1 MLSLENL-TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT-----ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALevigeqPQIIKKK-----VLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFAL------PPTIGRAqrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 153 VNSPEVVIADEPTGNLDPDT-----SWeimkTLEEINNRGTTVVMATHNKE 198
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALraqfrEF----VFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-218 |
7.62e-37 |
|
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: 128.38 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 23 VSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeiPYLRREIGVVFQDFKLLPTLTVFENVAF 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-----PPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 103 A----LEVIGEQPQIIKKkvldVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMK 178
Cdd:cd03298 94 GlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500859999 179 TLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03298 170 LVLDLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-196 |
1.02e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.95 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDLGSiKEKEIPYLRREIGV 83
Cdd:TIGR00972 8 NLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRmndlvPGVRIEGKVLFDGQDIYD-KKIDVVELRRRVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPtLTVFENVAFALEVIGeqpqIIKKKVLDvlDLVQ-----------LKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:TIGR00972 87 VFQKPNPFP-MSIYDNIAYGPRLHG----IKDKKELD--EIVEeslkkaalwdeVKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHN 196
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHN 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-215 |
1.87e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.64 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEkeipylrrEIGVVFQDFKLLPTLTVF 97
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--------DTRLMFQDARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 ENVAFALEviGEQpqiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIM 177
Cdd:PRK11247 100 DNVGLGLK--GQW----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500859999 178 KTLEEI-NNRGTTVVMATHN-KEIVnSMKKRVIAIEDGMI 215
Cdd:PRK11247 174 DLIESLwQQHGFTVLLVTHDvSEAV-AMADRVLLIEEGKI 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-216 |
7.53e-36 |
|
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: 125.45 E-value: 7.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEipyLRREIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE---RRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQD--FKLLpTLTVFENVAFALEVIGEQPQIIKKkVLDVLDLVQLKHkarQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03226 75 YVMQDvdYQLF-TDSVREELLLGLKELDAGNEQAET-VLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
9.26e-36 |
|
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: 124.25 E-value: 9.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVafalevigeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMkKRVIAIEDGMI 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
1.25e-35 |
|
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: 125.56 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPN---GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYL 77
Cdd:cd03266 1 MITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
1.97e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 126.64 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEkeIPYLRRE 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKL-LPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmKKRVIAIEDGMIV 216
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-218 |
2.50e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVK-----AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILInnKDLGSIKEKEIP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 YLRREIGVVFQ--DFKLLPTLtVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATH-NKEIVNSmkKRVIAIEDGMIVRD 218
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHyMEEAVEA--DRIIVMDSGKVVME 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
2.56e-35 |
|
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: 124.13 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYLRRE 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-196 |
2.90e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 10 IYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR--EEKPS---KGKILINNKDLGSiKEKEIPYLRREIGVV 84
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGarvEGEILLDGEDIYD-PDVDVVELRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 85 FQdfklLPT---LTVFENVAFALEVIGeqpqIIKKKVLDvlDLVQ-----------LKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:COG1117 98 FQ----KPNpfpKSIYDNVAYGLRLHG----IKSKSELD--EIVEeslrkaalwdeVKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHN 196
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
3.11e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.51 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIK----MMYREEKP-SKGKILINNKDLGSIKEKEIP 75
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAgSHIELLGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 YLRREIGVVFQDFKLLPTLTVFENVAFAleVIGEQP----------QIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-216 |
3.43e-35 |
|
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: 124.65 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPN-GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRRE 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENA--DRIVVLEDGKIV 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-195 |
1.21e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.14 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIK---------- 70
Cdd:COG4598 8 ALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 71 EKEIPYLRREIGVVFQDFKLLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIA 149
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-223 |
1.52e-34 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 123.76 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG--------VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEK 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 73 EIPYLRREIGVVFQDF--KLLPTLTVFENVAFALE---VIGEQPQiiKKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRV 146
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRhltSLDESEQ--KARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-195 |
2.40e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.84 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK--DLGSIKEKeipyLR 78
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDA----IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFALEvigeqpqiikKKVLDVLDLVQLKHKARQF---------PD----QLSGGEQQR 145
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLE----------PTKGGRLDRKAARARIRELserygldvdPDakveDLSVGEQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
3.79e-34 |
|
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: 121.17 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkdlGSIKEKEIPYLRReI 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD----GKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENvafaLEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03268 75 GALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
3.79e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.42 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgSIKEKEIPYLRRE 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQD-FKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
5.51e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.30 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE 80
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGvvfqdfkLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:COG4152 80 RG-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV----RDEARGEYG 225
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsgsVDEIRRQFG 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
6.90e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.41 E-value: 6.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT---ISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDfkllPT-----LTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:PRK13632 84 KIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGT-TVVMATHN-KEIVNSmkKRVIAIEDGMIVR 217
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDmDEAILA--DKVIVFSEGKLIA 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
1.04e-33 |
|
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: 126.34 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEkPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD-F-KLLP 92
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFgSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFALEV--IGEQPQIIKKKVLDVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:COG4172 378 RMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 170 PDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG4172 458 VSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-216 |
1.45e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 122.08 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGV----KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSiKEKEIPYL 77
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.99e-33 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 119.62 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDfkllPTL---TVFENVAFALEVIGEQpqiikkKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRV 146
Cdd:cd03245 80 IGYVPQD----VTLfygTLRDNITLGAPLADDE------RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHnKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITH-RPSLLDLVDRIIVMDSGRIVAD 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
2.49e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.58 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIY----PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEkeipY 76
Cdd:COG1101 1 MLELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LR-REIGVVFQDFKL--LPTLTVFENVAFALE----------VIGEQPQIIKKKvLDVLDLvQLKHKARQFPDQLSGGEQ 143
Cdd:COG1101 77 KRaKYIGRVFQDPMMgtAPSMTIEENLALAYRrgkrrglrrgLTKKRRELFREL-LATLGL-GLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 144 QRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNkeivnsMKK------RVIAIEDGMIV 216
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN------MEQaldygnRLIMMHEGRII 228
|
....*..
gi 500859999 217 RDeARGE 223
Cdd:COG1101 229 LD-VSGE 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-196 |
2.50e-33 |
|
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: 119.96 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYLRREIGVVF--Q 86
Cdd:cd03218 8 KRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHKRARLGIGYlpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 DFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTG 166
Cdd:cd03218 83 EASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190
....*....|....*....|....*....|
gi 500859999 167 NLDPDTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHN 192
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-217 |
3.49e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.22 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 22 NVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRRE-IGVVFQDFKLLPTLTVFENV 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 101 AFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTL 180
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 500859999 181 EEINNRGT-TVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-216 |
5.11e-33 |
|
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: 119.18 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPN--GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRR 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFKLLPTlTVFENVAFALEViGEQPQIIK-KKVLDVLDLVqlkhkaRQFPD-----------QLSGGEQQRVS 147
Cdd:cd03249 78 QIGLVSQEPVLFDG-TIAENIRYGKPD-ATDEEVEEaAKKANIHDFI------MSLPDgydtlvgergsQLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNkeiVNSMKK--RVIAIEDGMIV 216
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHR---LSTIRNadLIAVLQNGQVV 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-218 |
7.22e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.53 E-value: 7.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 22 NVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsikEKEIPYLRREIGVVFQDFKLLPTLTVFENVA 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 102 F----ALEVIGEQpqiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIM 177
Cdd:PRK10771 94 LglnpGLKLNAAQ----REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500859999 178 KTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:PRK10771 170 TLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
7.76e-33 |
|
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: 123.94 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIAR 150
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLA------RPDASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMKKRV 207
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-216 |
1.20e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsiKEKEIPYLRRE 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQ--DFKLLPTlTVFENVAFALEVIG-EQPQIIKKkVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK13635 83 VGMVFQnpDNQFVGA-TVQDDVAFGLENIGvPREEMVER-VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGT-TVVMATHNKEIVNSmKKRVIAIEDGMIV 216
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
2.08e-32 |
|
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: 122.87 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKS-TFIKMM----YREEKPSkGKILINNKDLGSIKEKEIPYLR-REIGVVFQD- 87
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGLSERELRRIRgNRIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 88 -FKLLPTLTVFENVAfalEVI----GEQPQIIKKKVLDVLDLVQLKHKAR---QFPDQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:COG4172 102 mTSLNPLHTIGKQIA---EVLrlhrGLSGAAARARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
2.91e-32 |
|
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: 122.60 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM--YREEKPSKGKILIN----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 63 -------------NKDLGSIKEKEIPYLRREIGVVFQ-DFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLK 128
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 129 HKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEE-INNRGTTVVMATHNKEIVNSMKKRV 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 500859999 208 IAIEDGMIV 216
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
4.26e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.98 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgSIKEKEIPYLRRE 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK13652 80 VGLVFQnpDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-218 |
1.00e-31 |
|
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: 115.66 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY-PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekEIPYLRRE 80
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDfKLLPTLTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSmKKRVIAIEDGMIVRD 218
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-195 |
1.04e-31 |
|
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: 115.45 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTF---IKMMYREEKPSKGKILINNKdlgsikEKEIPYLRREIGVVFQDFKLL 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQ------PRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTLTVFENVAFALEVIG--EQPQIIKKKVLDVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGN 167
Cdd:cd03234 94 PGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 500859999 168 LDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
1.17e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.04 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY----PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL-GSIKEKEIPY 76
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQdfklLPTLTVFE-----NVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKAR-QFPDQLSGGEQQRVSIAR 150
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-195 |
1.80e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.60 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEV-YKIypNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRR 79
Cdd:COG4559 1 MLEAENLsVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE---LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKA-RQFPdQLSGGEQQRVSIAR-------S 151
Cdd:COG4559 76 RRAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAgRSYQ-TLSGGEQQRVQLARvlaqlweP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500859999 152 IVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-223 |
1.96e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.94 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQDF--KLLPTLT 95
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFALE---VIGEQPQIikKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:PRK10419 108 VREIIREPLRhllSLDKAERL--ARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500859999 172 TSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK10419 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-196 |
3.65e-31 |
|
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: 119.39 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDFKL 90
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 91 LPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIARSIVNSPEVV 159
Cdd:TIGR02868 421 FDT-TVRENLRLA------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHN 196
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-216 |
3.71e-31 |
|
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: 119.92 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 19 NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipYLRREIGVVFQDfkllpTL---- 94
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA---SLRAAIGIVPQD-----TVlfnd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:COG5265 447 TIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGTTVVMA----ThnkeIVNSmkKRVIAIEDGMIV 216
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAhrlsT----IVDA--DEILVLEAGRIV 571
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
4.23e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.41 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE---LAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVAFaleviGEQP-----------QIIkKKVLDVLDLVQLKHKarqFPDQLSGGEQQRVSIA 149
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAF-----GRFPyskgrltaedrEII-DEAIAYLDLEDLADR---YLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
4.37e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.80 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikekEIPYLRRe 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 iGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500859999 161 ADEPTGNLDPDTSwEIMKT--LEEINNRGTTVVMATHNKE 198
Cdd:PRK11248 152 LDEPFGALDAFTR-EQMQTllLKLWQETGKQVLLITHDIE 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
4.98e-31 |
|
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: 113.92 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpyLRRE 80
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENvafaLEvIGEQPQIIKKKVLDVLDLV-----QLKHKARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEEN----LL-LGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-216 |
7.99e-31 |
|
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: 118.67 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYP-NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFaleviGEQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKA--DRIVVMDDGRIV 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
1.53e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.00 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLkHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGL-EKLLEDDKglnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMkKRVIAIEDGMIV 216
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-196 |
1.96e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.95 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 10 IYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDLGSIKEKEIPyLRREIGVV 84
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnPEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 85 FQDFKLLPtLTVFENVAFALEVIGEQpqiiKKKVLDvlDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIV 153
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIK----DKQVLD--EAVEKSLKGASIWDEvkdrlhdsalgLSGGQQQRVCIARVLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRS 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
3.11e-30 |
|
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: 109.83 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL--GSIKEKeipyLRR 79
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfASPRDA----RRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFqdfkllptltvfenvafalevigeqpqiikkkvldvldlvqlkhkarqfpdQLSGGEQQRVSIARSIVNSPEVV 159
Cdd:cd03216 76 GIAMVY---------------------------------------------------QLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 160 IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-213 |
3.62e-30 |
|
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: 114.44 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 35 GPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEI-PYLRREIGVVFQDFKLLPTLTVFENVAFAL-EVIGEQPQ 112
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlPPEKRRIGYVFQEARLFPHLSVRGNLRYGMkRARPSERR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 113 IIKKKVLDVLDLvqlKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVV 191
Cdd:TIGR02142 110 ISFERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPIL 186
|
170 180
....*....|....*....|..
gi 500859999 192 MATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR02142 187 YVSHSLQEVLRLADRVVVLEDG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-195 |
5.90e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.54 E-value: 5.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDlgsIKEKEIPYLRREIGVVFQDFK 89
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQD---IFKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTLTVFENVAFALEV--IGEQPQIIKKKVLDVLDLVQLKHKARQFPD----QLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:PRK14247 93 PIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|..
gi 500859999 164 PTGNLDPDTSWEIMKTLEEInNRGTTVVMATH 195
Cdd:PRK14247 173 PTANLDPENTAKIESLFLEL-KKDMTIVLVTH 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-216 |
8.80e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.13 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIY----PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSI-KEKEIP 75
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 YLRREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
1.72e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 112.23 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILInnkdLGSIKEKEIPYLRREI 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-196 |
1.75e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.51 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKdlgSIKEKE--IPYLRREIGVVFQDF 88
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmneleSEVRVEGRVEFFNQ---NIYERRvnLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 89 KLLPtLTVFENVAFALEVIGEQPQI----IKKKVLDVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGT-TVVMATHN 196
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-216 |
1.84e-29 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 115.18 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPN--GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRR 79
Cdd:TIGR02204 338 IEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LRA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFKLLPTlTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSI 148
Cdd:TIGR02204 415 RMALVPQDPVLFAA-SVMENIRYG------RPDATDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 149 ARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKA--DRIVVMDQGRIV 553
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-216 |
2.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL--GSIKEKEIPYLRREIGVVFQ 86
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 --DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:PRK13645 98 fpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 164 PTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
2.85e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.05 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILInnkdLGSIKEKEIPYLRREI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL----CGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-195 |
7.32e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK--DLGSIKEKEipylR 78
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAQ----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAfalevIGEQPQ---IIKKKVL-----DVLDLVQLKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIF-----LGREPRrggLIDWRAMrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTS---WEIMKTLEEinnRGTTVVMATH 195
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVerlFRIIRRLKA---QGVAIIYISH 198
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-217 |
8.34e-29 |
|
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: 112.83 E-value: 8.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILInnkDLGSIKEKEIPYLRRE 80
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTlRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL---DGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQlkhkarQFPD-----------QLSGGEQQRVSIA 149
Cdd:TIGR01842 394 IGYLPQDVELFPG-TVAENIARFGENADPEKIIEAAKLAGVHELIL------RLPDgydtvigpggaTLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKrVIAIEDGMIVR 217
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDK-ILVLQDGRIAR 533
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-217 |
1.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.15 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGV----KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGS-IKEKEIPY 76
Cdd:PRK13641 3 IKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-217 |
1.25e-28 |
|
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: 110.19 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 33 VVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSiKEKEI---PYLRReIGVVFQDFKLLPTLTVFENVAFALEVIGE 109
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpPHRRR-IGYVFQEARLFPHLSVRGNLLYGRKRAPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 110 QPQIIKkkvLD-VLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNR-G 187
Cdd:COG4148 108 AERRIS---FDeVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElD 184
|
170 180 190
....*....|....*....|....*....|
gi 500859999 188 TTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:COG4148 185 IPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-218 |
9.42e-28 |
|
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: 105.49 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkdlGSIKEKEIPYLRREIGVVF-QDFKLLPT 93
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA----GLVPWKRRKKFLRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTS 173
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 174 WEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:cd03267 190 ENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-215 |
9.80e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEV-YKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsiKEKEIPYLR 78
Cdd:PRK13650 4 IIEVKNLtFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:PRK13650 81 HKIGMVFQnpDNQFVGA-TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVnSMKKRVIAIEDGMI 215
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-219 |
1.17e-27 |
|
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: 109.84 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDFKLLPTlTVF 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRHIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 ENVA-FAlEVIGEqpQIIK--KKVlDVLDLVQlkhkarQFPD-----------QLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:COG4618 424 ENIArFG-DADPE--KVVAaaKLA-GVHEMIL------RLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKrVIAIEDGMIV----RDE 219
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDK-LLVLRDGRVQafgpRDE 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-216 |
1.94e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREeKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD--FKLLPTL 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL-INSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALEVigEQPQIIKK----KVLDVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:PRK15134 380 NVLQIIEEGLRV--HQPTLSAAqreqQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 170 PDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK15134 458 KTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-169 |
2.11e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.59 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD--FKLLP 92
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVfenvafalEVIGEQPQII---------KKKVLDVLDLVQLK--HKARqFPDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:PRK11308 108 RKKV--------GQILEEPLLIntslsaaerREKALAMMAKVGLRpeHYDR-YPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 500859999 162 DEPTGNLD 169
Cdd:PRK11308 179 DEPVSALD 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-217 |
5.54e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.58 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIY---PNGV-KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPY 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LR----REIGVVFQDFKLLPTLTVFENVAfalEVIG-EQP-QIIKKKVLDVLDLVQL-KHKAR----QFPDQLSGGEQQR 145
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLT---EAIGlELPdELARMKAVITLKMVGFdEEKAEeildKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDP----DTSWEIMKTLEEINNrgtTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-216 |
6.01e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.74 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDfKLLPTLTVFENV------------------AFALEVIGEQPqiikkkvlDVLDLVqLKHKARqfpdQLSGGEQ 143
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNIrvgrpdatdeemraaaerAQAHDFIERKP--------DGYDTV-VGERGR----QLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 144 QRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA--DRILVFDNGRVV 548
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-225 |
7.30e-27 |
|
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: 102.57 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY-PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDfkllPTL---TVFENvafaLEVIGEQPQiikKKVLDVLDLVQLKHKARQFPDQL-----------SGGEQQRV 146
Cdd:cd03244 80 ISIIPQD----PVLfsgTIRSN----LDPFGEYSD---EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEiNNRGTTVVMATHNKE-IVNSmkKRVIAIEDGMIVrdeargEYG 225
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDtIIDS--DRILVLDKGRVV------EFD 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-170 |
8.15e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDFKLLPTLTVF 97
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARRRAVLPQHSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 ENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKA-RQFPdQLSGGEQQRVSIAR------SIVNSPEVVIADEPTGNLDP 170
Cdd:PRK13548 95 EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARvlaqlwEPDGPPRWLLLDEPTSALDL 173
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-196 |
9.95e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 102.74 E-value: 9.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeiP-YLRREIGVVF--QDFK 89
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL-----PmHERARLGIGYlpQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:TIGR04406 87 IFRKLTVEENIMAVLEIRKDLDrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180
....*....|....*....|....*...
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:TIGR04406 167 DPIAVGDIKKIIKHLKERGIGVLITDHN 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
1.69e-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: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYP-NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipyLRRE 80
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENvafalevIGEQpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNN-------LGRR---------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATHNKEIVNSMKKrVIAIEDGMIV 216
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDK-ILFLENGKII 175
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-209 |
1.75e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYkiYPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRR 79
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFKLLPTLTVFENVAFAL-EVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSM--------KKRVIA 209
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIadhayivaDKKIVA 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-217 |
2.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGV----KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSI-KEKEIPY 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKAR-QFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFeKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-196 |
9.56e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEV-YKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpylRR 79
Cdd:PRK13648 7 IIVFKNVsFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQ--DFKLLPTLTVFEnVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHN 196
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHD 202
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-228 |
3.69e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.55 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD--FK 89
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTLTVFENVAFALEVIgeQPQI----IKKKVLDVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEP 164
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTY--HPKLsrqeVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 165 TGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVrdeargEYGIYD 228
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV------ELGTYD 247
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-196 |
5.23e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.18 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeiP-YLRR 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-----PmHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGV--------VFQDfkllptLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARS 151
Cdd:COG1137 77 RLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500859999 152 IVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
5.97e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYpnGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsikekeipyLRreIG 82
Cdd:COG0488 1 LENLSKSF--GGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LR--IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQDFKLLPTLTVFENVafaLEVIGEQPQIIKKK----------------------VLDVLDLVQLKHKARQ------F 134
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTV---LDGDAELRALEAELeeleaklaepdedlerlaelqeEFEALGGWEAEARAEEilsglgF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 135 PD--------QLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT-SWeimktLEE-INNRGTTVVMATHNKEIVNSMK 204
Cdd:COG0488 142 PEedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiEW-----LEEfLKNYPGTVLVVSHDRYFLDRVA 216
|
250
....*....|...
gi 500859999 205 KRVIAIEDGMIVR 217
Cdd:COG0488 217 TRILELDRGKLTL 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
6.09e-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: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPN--GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipYLRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDfkllPTL---TVFENVAFAL-----EVIGEQPQiiKKKVLDVLDLVQLKH--KARQFPDQLSGGEQQRVSIA 149
Cdd:cd03248 89 KVSLVGQE----PVLfarSLQDNIAYGLqscsfECVKEAAQ--KAHAHSFISELASGYdtEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 150 RSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMI 215
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERA--DQILVLDGGRI 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
7.33e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYP-----NG---------------VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM----YreekPSK 56
Cdd:COG4586 1 IIEVENLSKTYRvyekePGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilV----PTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 57 GKILINNKDlgsIKEKEIPYLRReIGVVF-QDFKLLPTLTVFENvaFAL--EVIGEQPQIIKKKVLDVLDLVQLKHKARQ 133
Cdd:COG4586 77 GEVRVLGYV---PFKRRKEFARR-IGVVFgQRSQLWWDLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 134 FPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMATHNKEIVNSMKKRVIAIED 212
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDH 230
|
....*.
gi 500859999 213 GMIVRD 218
Cdd:COG4586 231 GRIIYD 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-216 |
9.19e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.72 E-value: 9.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPN--GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsiKEKEIPYLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDfKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQlkhkarQFPD-----------QLSGGEQQRVSI 148
Cdd:TIGR00958 556 QVALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM------EFPNgydtevgekgsQLSGGQKQRIAI 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 149 ARSIVNSPEVVIADEPTGNLDPdtswEIMKTLEEINNRGT-TVVMATHNKEIVNSMKKrVIAIEDGMIV 216
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASrTVLLIAHRLSTVERADQ-ILVLKKGSVV 692
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-195 |
2.20e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.51 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIK-MMYREEKPSK--GKILINNKDLGSikekeiPYLRREIGVVFQDFKLLPTL 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsGSVLLNGMPIDA------KEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALE------VIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQ---LSGGEQQRVSIARSIVNSPEVVIADEPT 165
Cdd:TIGR00955 115 TVREHLMFQAHlrmprrVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 500859999 166 GNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-218 |
2.46e-24 |
|
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: 100.58 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDfKLLPTLTVFENVafaleVIGEQPQIIKKKVLDVLDLVQLKHKARQFP-----------DQLSGGEQQRVSIAR 150
Cdd:TIGR01193 551 NYLPQE-PYIFSGSILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRgtTVVMATHNKEIVnSMKKRVIAIEDGMIVRD 218
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQ 689
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
4.10e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM-----YReekpskGKILINNKDLgsiKEKEIPY 76
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQ------GSLKINGIEL---RELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQDfKLLPTLTVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFP--------DQ---LSGGEQQR 145
Cdd:PRK11174 421 WRKHLSWVGQN-PQLPHGTLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigDQaagLSVGQAQR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEiNNRGTTVVMATHNKEIVNSMKKrVIAIEDGMIVrdeARGEY 224
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIV---QQGDY 567
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-223 |
4.17e-24 |
|
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: 95.67 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYLR--REIGVVFQDFKLLPTL 94
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHERarAGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALEVIGEQPQIIKKkvlDVLDL--VQLKHKARQFPDqLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPD---EIYELfpVLKEMLGRRGGD-LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 173 SWEIMKTLEEINNRGT-TVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-196 |
4.18e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.24 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQdfkLLPT---L 94
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARRLALLPQ---HHLTpegI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFA----LEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDP 170
Cdd:PRK11231 92 TVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180
....*....|....*....|....*.
gi 500859999 171 DTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:PRK11231 172 NHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-196 |
4.60e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDLGSIKEKEIPyLRREIGV 83
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLFGRNIYSPDVDPIE-VRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENVAFALEVIG------EQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGlvkskkELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHS 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-223 |
6.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSikeKEIPYLRREIGVVFQD-FKLLPT 93
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEVIG-EQPQIIKKKVLDVLDLVQLKHKARQfPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:PRK13642 97 ATVEDDVAFGMENQGiPREEMIKRVDEALLAVNMLDFKTRE-PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 173 SWEIMKTLEEINNR-GTTVVMATHNKEIVNSmKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-221 |
7.04e-24 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 99.18 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPS--KGKILINNKDLGSikekeiPYLRReIGVVFQDFKLLPTLT 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK------QILKR-TGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFAL-----EVIGEQPQI-IKKKVLDVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGN 167
Cdd:PLN03211 157 VRETLVFCSllrlpKSLTKQEKIlVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 168 LDPDTSWEIMKTLEEINNRGTTVVMATHNKEivnsmkKRVIAIEDGMIVRDEAR 221
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPS------SRVYQMFDSVLVLSEGR 284
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-196 |
7.13e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR-----EEKPSKGKILINNKDL--GSIKEKEIpylRREIGVVFQDFK 89
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndliPGFRVEGKVTFHGKNLyaPDVDPVEV---RRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTlTVFENVAFALEVIGEQ---PQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTG 166
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|
gi 500859999 167 NLDPDTSWEIMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQ-YTIIIVTHN 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-216 |
7.80e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGV----KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGS-IKEKEIPY 76
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQdfklLPTLTVFEN-----VAFALEVIGEQPQIIKKKVLDVL-DLVQLKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-195 |
9.65e-24 |
|
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: 94.39 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINN-----KDLgsikekeipy 76
Cdd:TIGR03740 1 LETKNLSKRFGKQT-AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGhpwtrKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 lrREIGVVFQDFKLLPTLTVFENVAFALEVIGeqpqIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:TIGR03740 70 --HKIGSLIESPPLYENLTARENLKVHTTLLG----LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 500859999 157 EVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-193 |
1.55e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 98.25 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKeipYLRREI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLLPTlTVFENVAFALEvIGEQpqiikkKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLGRD-ISEE------QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMA 193
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-216 |
1.62e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 10 IYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYR--EEKPSK----GKILINNKDLGSIKEKEipyLRREIGV 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRliEIYDSKikvdGKVLYFGKDIFQIDAIK---LRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENVAFALEVIG-EQPQIIKKKVLDVLDLV----QLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNRgTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-225 |
1.65e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.95 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNG-VKAINGINVSIHPGEFVYVVGPSGAGKS-TFIKMMYREEKPSK--GKILINNKDLGSIKEKEIPYLRRE-IGVVFQ 86
Cdd:PRK09473 25 PDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEKELNKLRAEqISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 D--FKLLPTLTVFENVafaLEVIGEQPQIIKK-------KVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK09473 105 DpmTSLNPYMRVGEQL---MEVLMLHKGMSKAeafeesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIVrdeargEYG 225
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTM------EYG 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-223 |
3.38e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDfkllP 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQT----P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TL---TVFENVAFALEVIGEQPQiiKKKVLDVLDLVQLKHKARQFP-DQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:PRK10247 91 TLfgdTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 169 DPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKrVIAIEDGMIVRDEARGE 223
Cdd:PRK10247 169 DESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHADK-VITLQPHAGEMQEARYE 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
12-216 |
3.59e-23 |
|
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: 92.48 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDfkll 91
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQD---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTL---TVFENvafaLEVIGEQPQiikKKVLDVLdlvqlkhKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:cd03369 91 PTLfsgTIRSN----LDPFDEYSD---EEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:cd03369 157 DYATDALIQKTIREEFTNSTILTIAHRLRTIIDY--DKILVMDAGEVK 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-213 |
3.90e-23 |
|
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: 97.39 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIY-PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYLRREIG 82
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 163 EPTGNLDPDTSWEIMKTLEEINNrGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-223 |
5.14e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.92 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKeKEIPYLRREIGVVFQDfkllPTLTVF 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 -----ENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHkARQFPDQ-LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 172 TSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-216 |
6.00e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKS-TFIKMMYREEKPS----KGKILINNKDLGSIKEKEIPYLR-REIGVVFQD--FK 89
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTLTVFENVAfalEVI----GEQPQIIKKKVLDVLDLVQLKHKARQ---FPDQLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:PRK15134 105 LNPLHTLEKQLY---EVLslhrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 163 EPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
1.16e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpyLRRE 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVA----FAlevigeQPQIIKKKVLDVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggfFA------ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-216 |
1.33e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKS-TFIKMMYREEKPSK---GKILINNKDLGSIKEKEipylRR-----EIGVVFQ 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKE----RRnlvgaEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 D--FKLLPTLTVFENVAFALEV-IGEQPQIIKKKVLDVLDLVQLKHKARQ---FPDQLSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK11022 97 DpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
1.80e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKP---SKGKILINNKDLGsikEKEIPYL 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT---AKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 RREIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:PRK13640 83 REKVGIVFQnpDNQFVGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNKEIVNsMKKRVIAIEDGMIV 216
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-216 |
2.75e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.70 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVK-AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsiKEKEIPYLRRE 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTlTVFENVAFALEVIGEQPQIIK-----------KKVLDVLDLVQLKHKArqfpdQLSGGEQQRVSIA 149
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQYSREQIEEaarmayamdfiNKMDNGLDTVIGENGV-----LLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 150 RSIV-NSPeVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:PRK11176 493 RALLrDSP-ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA--DEILVVEDGEIV 557
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-207 |
2.82e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 92.66 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNG-VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPS----KGKILINNKDLG--SIKE-KEIpyLRREIGV 83
Cdd:COG4170 16 PQGrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLklSPRErRKI--IGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFK--LLPTLTVFENVAFAL---EVIG---EQPQIIKKKVLDVLDLVQLK-HKA--RQFPDQLSGGEQQRVSIARSI 152
Cdd:COG4170 94 IFQEPSscLDPSAKIGDQLIEAIpswTFKGkwwQRFKWRKKRAIELLHRVGIKdHKDimNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRV 207
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTI 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-195 |
4.19e-22 |
|
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: 89.73 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKE---KEIPYLRREIGvvfqdfkLLPTLTV 96
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephENILYLGHLPG-------LKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQpqiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEI 176
Cdd:TIGR01189 91 LENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 500859999 177 MKTLEEINNRGTTVVMATH 195
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTH 185
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
4.74e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 90.66 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGvKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIP----- 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSeaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 76 -YLRREIGVVFQDFK--LLPTLTVFENVAFALEVIGEQPQ-IIKKKVLDVLDLVQL-KHKARQFPDQLSGGEQQRVSIAR 150
Cdd:TIGR02323 82 rLMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHYgNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEE-INNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-196 |
1.57e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipYLRREIGVVFQDFKLLPT 93
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEV----IGEQPQIIKKKVLDVLDLVQLKHKARQfpdQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:PRK10895 93 LSVYDNLMAVLQIrddlSAEQREDRANELMEEFHIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180
....*....|....*....|....*..
gi 500859999 170 PDTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-216 |
2.71e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQD--FKLLP 92
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFALEVIG-EQPQIIKKKVLDVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDP 170
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 171 DTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
3.45e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnkDLGSikekeipylRRE 80
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-----KLGE---------TVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLL-PTLTVFENVAfaleviGEQPQIIKKKVLDVL-------DlvqlkhKARQFPDQLSGGEQQRVSIARSI 152
Cdd:COG0488 380 IGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLgrflfsgD------DAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 153 VNSPEVVIADEPTGNLDPDtsweimkTLEEINN-----RGtTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIE-------TLEALEEalddfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-217 |
4.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLG-------------SIKEKEIPYLR 78
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpySKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQ--DFKLLPTlTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-199 |
5.48e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.45 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTfikMMyreekpskgKIL--INNKDLGSIKekeipYLR 78
Cdd:PRK10762 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKST---MM---------KVLtgIYTRDAGSIL-----YLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 RE-------------IGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLD----VLDLVQLKHKARQFPDQLSGG 141
Cdd:PRK10762 66 KEvtfngpkssqeagIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAeadkLLARLNLRFSSDKLVGELSIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 142 EQQRVSIARSIVNSPEVVIADEPTGNLDpDTSWE-IMKTLEEINNRGTTVVMATHN-KEI 199
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALT-DTETEsLFRVIRELKSQGRGIVYISHRlKEI 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-219 |
6.82e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkekeipylrrEIGVVFQdfkllPTL 94
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL----------GLGGGFN-----PEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKhkarQFPDQ----LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDP 170
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELG----DFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500859999 171 DTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDE 219
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-208 |
8.59e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkdlgsikekeipyLRREIGVVFQDFKL-- 90
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA--------------GGARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 91 -LPtLTVFENVAF-------ALEVIGEQPQIIKKKVLDVLDLVQLKHkaRQFpDQLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:NF040873 69 sLP-LTVRDLVAMgrwarrgLWRRLTRDDRAAVDDALERVGLADLAG--RQL-GELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 163 EPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVI 208
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
1.03e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYLRRE 80
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGV--VFQDFKLLPTLTVFENVAFALevigEQPQIIKKKVLDVLDL--VQLKhkarqfPDQLSG----GEQQRVSIARSI 152
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAAlgCQLD------LDSSAGslevADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGEY 224
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
1.14e-20 |
|
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: 85.98 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGV----KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsikekeipyl 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 rreIGVVFQDFKLLPTlTVFENVAFALEvigeqpqIIKKKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRV 146
Cdd:cd03250 68 ---IAYVSQEPWIQNG-TIRENILFGKP-------FDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLeeINN---RGTTVVMATHNKEIVnSMKKRVIAIEDG 213
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGlllNNKTRILVTHQLQLL-PHADQIVVLDNG 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-192 |
1.70e-20 |
|
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: 84.79 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpyLRREIGVVFQDFK---LLP 92
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFalevigeqpqiikkkvldvldlvqlkhkarqfPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180
....*....|....*....|
gi 500859999 173 SWEIMKTLEEINNRGTTVVM 192
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLL 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
1.77e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLrrE 80
Cdd:PRK09700 5 YISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDFKLLPTLTVFENVafaleVIGEQPqiiKKKVLDV---------------LDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENL-----YIGRHL---TKKVCGVniidwremrvraammLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-223 |
1.80e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.96 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPylrREIGVVFQDFKLLPTLTVFENV 100
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 101 AFALevIGEQPQIIKKK------VLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSW 174
Cdd:PRK10253 103 ARGR--YPHQPLFTRWRkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500859999 175 EIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK10253 181 DLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-195 |
2.79e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM-----YRE---EKPSKGKILInnkdlgsIKEKeiPYLrreigv 83
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYGSgriARPAGARVLF-------LPQR--PYL------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 vfqdfkllPTLTVFENVAFalevigeqPQIIKK----KVLDVLDLVQLKHKARQF------PDQLSGGEQQRVSIARSIV 153
Cdd:COG4178 438 --------PLGTLREALLY--------PATAEAfsdaELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500859999 154 NSPEVVIADEPTGNLDPDTSWEIMKTLEEiNNRGTTVVMATH 195
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-226 |
4.07e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPylrREIGVVFQDFKLLPTLTVFENVAfalev 106
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVAYLPQQLPAAEGMTVRELVA----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 107 IGEQP---------QIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIM 177
Cdd:PRK10575 108 IGRYPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 178 KTLEEINN-RGTTVVMATHNKEIVNSMKKRVIAIEDG-MIVRDEA----RGE-----YGI 226
Cdd:PRK10575 188 ALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGeMIAQGTPaelmRGEtleqiYGI 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
9.36e-20 |
|
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: 81.73 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILinnkdlgSIKEKEIPYLrrei 81
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------WGSTVKIGYF---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 gvvfqdfkllptltvfenvafalevigeqpqiikkkvldvldlvqlkhkarqfpDQLSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:cd03221 69 ------------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 162 DEPTGNLDPDTsweIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:cd03221 95 DEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-216 |
1.19e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.21 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK-----DLGSIKEKEIPYL-RREIGVVFQD 87
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLlRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 88 FK--LLPTLTVFENVAFALEVIGEQP-QIIKKKVLDVLDLVQLKhKAR--QFPDQLSGGEQQRVSIARSIVNSPEVVIAD 162
Cdd:PRK11701 98 PRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEID-AARidDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 163 EPTGNLDPDTSWEIMKTLEE-INNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-216 |
1.42e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 33 VVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIkEKEI---PYLRReIGVVFQDFKLLPTLTVFENVAFALEvige 109
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDA-EKGIclpPEKRR-IGYVFQDARLFPHYKVRGNLRYGMA---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 110 qpQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLE----EINn 185
Cdd:PRK11144 103 --KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLErlarEIN- 179
|
170 180 190
....*....|....*....|....*....|.
gi 500859999 186 rgTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11144 180 --IPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-218 |
5.90e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 33 VVGPSGAGKSTFIKMMYR-EEKPS----KGKILINNKDLgsIKEKEIPYLRREIGVVFQDFKLLPtLTVFENVAFALEVI 107
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 108 GEQPQ-----IIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEE 182
Cdd:PRK14271 129 KLVPRkefrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 500859999 183 INNRgTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:PRK14271 209 LADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-215 |
7.25e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVyKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPylrRE 80
Cdd:PRK09536 3 MIDVSDL-SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDfkllpTLTVFEnvaFALEVI---GEQPQIIKKKVLD-----VLDLVQLKHKARQFPDQ----LSGGEQQRVSI 148
Cdd:PRK09536 79 VASVPQD-----TSLSFE---FDVRQVvemGRTPHRSRFDTWTetdraAVERAMERTGVAQFADRpvtsLSGGERQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 149 ARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
7.27e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---------------------VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKI 59
Cdd:COG1134 4 MIEVENVSKSYRLYhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 60 LINnkdlGSIkekeIPYLrrEIGVVFQdfkllPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKhkarQFPDQ-- 137
Cdd:COG1134 84 EVN----GRV----SALL--ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELG----DFIDQpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 138 --LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:COG1134 145 ktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....
gi 500859999 216 VRDE 219
Cdd:COG1134 225 VMDG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-214 |
1.28e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLrreiGVV--FQDFKLL 91
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM----GVVrtFQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTLTVFENVAFAlevigeQPQIIKKKVLD---------------------VLDLVQLKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:PRK11300 93 REMTVIENLLVA------QHQQLKTGLFSgllktpafrraesealdraatWLERVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMATHNKEIVNSMKKRVIAIEDGM 214
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-200 |
1.59e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnkdlgsikeKEIPYLRreIGVVFQDFKLLPTLT 95
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR--IGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFALevigeQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWE 175
Cdd:PRK09544 84 LTVNRFLRL-----RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*.
gi 500859999 176 IMKTLEEINNR-GTTVVMATHNKEIV 200
Cdd:PRK09544 159 LYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-201 |
1.61e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEK--PSKGKilinnkdlgsikekeipylrreigVVFQDFKLLPTLT 95
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGC------------------------VDVPDNQFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAfalevigeqpqiikkKVLDVLDLVQLKHKA--------RQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGN 167
Cdd:COG2401 102 LIDAIG---------------RKGDFKDAVELLNAVglsdavlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....*
gi 500859999 168 LDPDTSWEIMKTLEEINNR-GTTVVMATHNKEIVN 201
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRaGITLVVATHHYDVID 201
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-196 |
2.14e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEkPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDFKLLPTLTVFEN 99
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAE---LARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVIGEQPQIIkKKVLDVLDLVQLKHK-ARQFpDQLSGGEQQRVSIARSI------VN-SPEVVIADEPTGNLDpd 171
Cdd:COG4138 90 LALHQPAGASSEAVE-QLLAQLAEALGLEDKlSRPL-TQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLD-- 165
|
170 180 190
....*....|....*....|....*....|.
gi 500859999 172 tsweIM------KTLEEINNRGTTVVMATHN 196
Cdd:COG4138 166 ----VAqqaaldRLLRELCQQGITVVMSSHD 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-216 |
8.59e-18 |
|
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: 78.07 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM--YREEKPS-KGKILINNKDLGSIKEkeipYLRREIGVVFQDFK 89
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanRTEGNVSvEGDIHYNGIPYKEFAE----KYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 LLPTLTVFENVAFALEVIGEQpqIIKKkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGNE--FVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500859999 170 PDTSWEIMKTLEEINN--RGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:cd03233 151 SSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-197 |
1.08e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKE-IPYLRReigvvfQDFkLLPTLTVFE 98
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEaCHYLGH------RNA-MKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 99 NVAFALEVIGEQPQIIkkkvLDVLDLVQLKHKA-RQFPDqLSGGEQQRVSIARSIV-NSPeVVIADEPTGNLDPDTSWEI 176
Cdd:PRK13539 93 NLEFWAAFLGGEELDI----AAALEAVGLAPLAhLPFGY-LSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|.
gi 500859999 177 MKTLEEINNRGTTVVMATHNK 197
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-195 |
1.10e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.92 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKekeiPYLRREIGVVFQDFKLLPTLTVFEN 99
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR----DSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFaLEVIGEQPQIikKKVLDVLDLVQLKHKArqfPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKT 179
Cdd:cd03231 94 LRF-WHADHSDEQV--EEALARVGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 500859999 180 LEEINNRGTTVVMATH 195
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
1.19e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM---YreekPS---KGKILINNKDL--GSIKEK 72
Cdd:PRK13549 5 LLEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvY----PHgtyEGEIIFEGEELqaSNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 73 EipylRREIGVVFQDFKLLPTLTVFENVAFALEvigeqpqIIKKKVLD----------VLDLVQLKHKARQFPDQLSGGE 142
Cdd:PRK13549 80 E----RAGIAIIHQELALVKELSVLENIFLGNE-------ITPGGIMDydamylraqkLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 143 QQRVSIARSIVNSPEVVIADEPTGNLdpdTSWEI---MKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASL---TESETavlLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-197 |
1.30e-17 |
|
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: 80.75 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILinnkdlgsikekeiPYLRREIGV 83
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------------PQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENV-------------------AFALE------VIGEQPQIIKKkvLDVLDLVQLKHK------AR 132
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVeegvaeikdaldrfneisaKYAEPdadfdkLAAEQAELQEI--IDAADAWDLDSQleiamdAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 133 QFPD------QLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT-SWeimktLEE--INNRGtTVVMATHNK 197
Cdd:TIGR03719 151 RCPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvAW-----LERhlQEYPG-TVVAVTHDR 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-217 |
7.55e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 9 KIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDL--GSIKEKeipyLRREIGVVFQ 86
Cdd:PRK11288 12 KTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAA----LAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 DFKLLPTLTVFENVafaleVIGEQPQ---IIKKKVLDVLDLVQLKHKARQF-PDQ----LSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK11288 87 ELHLVPEMTVAENL-----YLGQLPHkggIVNRRLLNYEAREQLEHLGVDIdPDTplkyLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVR 217
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-217 |
9.22e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIK--MMYREEKPSKGKILINNKDLGSIKEKEIPylRREIGVVFQdfkl 90
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKtiMGHPKYEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 91 lptltvfenvafalevigEQPQIIKKKVLDVLdlvqlkhkaRQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDP 170
Cdd:cd03217 85 ------------------YPPEIPGVKNADFL---------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500859999 171 DTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMK-KRVIAIEDGMIVR 217
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDYIKpDRVHVLYDGRIVK 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
1.02e-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: 78.33 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM--YREEKPSKGKILINNKDL--GSIKEKEipy 76
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSPLkaSNIRDTE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 lRREIGVVFQDFKLLPTLTVFENVAFALEV-----IGEQPQIIkKKVLDVLDLVQLKHKARQFP-DQLSGGEQQRVSIAR 150
Cdd:TIGR02633 77 -RAGIVIIHQELTLVPELSVAENIFLGNEItlpggRMAYNAMY-LRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 151 SIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-193 |
2.89e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkDLGSIKEKEIPYLRREIGVVFQDfKLLPTL 94
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQD-PLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFAL------EVIGEQP--------------------------------------------QIIK-KKVLDVLD 123
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlEALSNYYnedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKdSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 124 LVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI--NNRGTTV 190
Cdd:PTZ00265 555 KVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITI 634
|
...
gi 500859999 191 VMA 193
Cdd:PTZ00265 635 IIA 637
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-216 |
3.26e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKS-TFIKMMYREEKP----SKGKILINNK-----DLGSIKEKEIPYLR-REIGV 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRsrqviELSEQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQD--FKLLPTLTVFENVAFALE----VIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRlhqgASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 158 VVIADEPTGNLDPDTSWEIM---KTLEEINNRGttVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILqliKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-207 |
7.89e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.84 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKP----SKGKILINNKDLGSIKEKEipyLRREIG----VVFQ 86
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE---RRKLVGhnvsMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 DFK--LLPTltvfenvafalEVIGEQ-PQII----------------KKKVLDVLDLVQLK-HKA--RQFPDQLSGGEQQ 144
Cdd:PRK15093 97 EPQscLDPS-----------ERVGRQlMQNIpgwtykgrwwqrfgwrKRRAIELLHRVGIKdHKDamRSFPYELTEGECQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500859999 145 RVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEIN-NRGTTVVMATHNKEIVNSMKKRV 207
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-195 |
1.01e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 72.28 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMM-YREEKPS-KGKILINNKDLGsikekeiPYLRREIGVVFQDFKLLPTLT 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD-------KNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAFALEVIGeqpqiikkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWE 175
Cdd:cd03232 96 VREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
gi 500859999 176 IMKTLEEINNRGTTVVMATH 195
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-169 |
1.24e-15 |
|
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: 73.21 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAINGINVSIHPGEF-----VYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgSIKEKEIPylrreigvvf 85
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 86 QDFkllpTLTVFENVAFALEVIGEQPQiIKKKVLDVLDLVQLKHkaRQFPDqLSGGEQQRVSIARSIVNSPEVVIADEPT 165
Cdd:cd03237 72 ADY----EGTVRDLLSSITKDFYTHPY-FKTEIAKPLQIEQILD--REVPE-LSGGELQRVAIAACLSKDADIYLLDEPS 143
|
....
gi 500859999 166 GNLD 169
Cdd:cd03237 144 AYLD 147
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
5.91e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK-DLGSIKEKeipylrRE 80
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVDQS------RD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 igvvfqdfKLLPTLTVFENVAFALEVIgeqpQIIKKKVldvldlvqlkhKARQF--------PDQ------LSGGEQQRV 146
Cdd:TIGR03719 396 --------ALDPNKTVWEEISGGLDII----KLGKREI-----------PSRAYvgrfnfkgSDQqkkvgqLSGGERNRV 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTsweiMKTLEE--INNRGTTVV----------MATH 195
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEalLNFAGCAVVishdrwfldrIATH 509
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-195 |
7.07e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 24 SIHPGEFVYVVGPSGAGKSTFIKMMyREEKPSKGKILINNKDLGSIKEKEIPYLRreiGVVFQDFKLLPTLTVFENVAFA 103
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 104 LEViGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI-----VNSPE--VVIADEPTGNLDPDTSWEI 176
Cdd:PRK03695 94 QPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQAAL 172
|
170
....*....|....*....
gi 500859999 177 MKTLEEINNRGTTVVMATH 195
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSH 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-195 |
9.04e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.10 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM-----YRE---EKPSKGKILInnkdlgsIKEKeiPYLrreigv 83
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGSgriGMPEGEDLLF-------LPQR--PYL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 vfqdfkllPTLTVFENVAFALEvigeqpqiikkkvldvldlvqlkhkarqfpDQLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:cd03223 76 --------PLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 500859999 164 PTGNLDPDTSWEIMKTLEEinnRGTTVVMATH 195
Cdd:cd03223 118 ATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-216 |
1.54e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsiKEKEIPYLRREIGVVFQD--FKLLP 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---HFGDYSYRSQRIRMIFQDpsTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TLTVFENVAFALEVIGE-QPQIIKKKVLDVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDP 170
Cdd:PRK15112 103 RQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 171 DTSWEIMKTLEEINNR-GTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK15112 183 SMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-216 |
1.89e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 25 IHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPylRREIGVVFqDFkllptltVFENVAFAL 104
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPP--RNVEGTVY-DF-------VAEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 105 EVIGEQPQIIKK-----------------KVLDVLDLVQLKHKARQF-------PDQ----LSGGEQQRVSIARSIVNSP 156
Cdd:PRK11147 96 EYLKRYHDISHLvetdpseknlnelaklqEQLDHHNLWQLENRINEVlaqlgldPDAalssLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 157 EVVIADEPTGNLDPDT-SWeimktLEEI--NNRGtTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK11147 176 DVLLLDEPTNHLDIETiEW-----LEGFlkTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-214 |
2.45e-14 |
|
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: 69.28 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 8 YKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdLGSIKEKEIPYLRREIGVVFQD 87
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 88 FK-LLPTLTVFENVAFalevigEQPqIIKKKVLDVLDLVQLKHKARQFP--DQ---------LSGGEQQRVSIARSIVNS 155
Cdd:cd03290 86 QKpWLLNATVEENITF------GSP-FNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKT--LEEINNRGTTVVMATHNKEIVnSMKKRVIAIEDGM 214
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDGS 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-217 |
2.90e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIK-MMYREE-KPSKGKILINNKDLG--SIKEKEipylRREIGVVFQDFKLLPT 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILelSPDERA----RAGIFLAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 94 LTVFENVAFALEVIGEQPQII---KKKVLDVLDLVQLKHKA--RQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSArefLKLLKEKMKELGLDEDFldRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMK-KRVIAIEDGMIVR 217
Cdd:COG0396 172 DIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVK 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-195 |
4.27e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkdlgsikekeiPYLRreIGV 83
Cdd:PRK11819 9 MNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA------------PGIK--VGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENV-------------------AFAL------EVIGEQPQIIKKkvLDVLDLVQLKHK------AR 132
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVeegvaevkaaldrfneiyaAYAEpdadfdALAAEQGELQEI--IDAADAWDLDSQleiamdAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500859999 133 QFPD------QLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT-SWeimktLEE--INNRGtTVVMATH 195
Cdd:PRK11819 153 RCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvAW-----LEQflHDYPG-TVVAVTH 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-195 |
5.31e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEK---EIPYLRREIGVvfqdfKllPTLTV 96
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLYLGHQPGI-----K--TELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQPQiikKKVLDVLDLVQLkhkaRQFPD----QLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:PRK13538 92 LENLRFYQRLHGPGDD---EALWEALAQVGL----AGFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 500859999 173 SWEIMKTLEEINNRGTTVVMATH 195
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTH 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-198 |
8.17e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.94 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNG---------VKAING-------INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKpSKGKILINNK 64
Cdd:TIGR01271 1202 VIENPHAQKCWPSGgqmdvqgltAKYTEAgravlqdLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGV 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 65 DLGSIKEKEipyLRREIGVVFQDFKLLpTLTVFENvafalevIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQL------ 138
Cdd:TIGR01271 1281 SWNSVTLQT---WRKAFGVIPQKVFIF-SGTFRKN-------LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvd 1349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 139 -----SGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEiNNRGTTVVMATHNKE 198
Cdd:TIGR01271 1350 ggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVE 1413
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
1.01e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipYLRREIGVVFQDFK---LLPTL 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLANGIVYISEDRKrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAF-ALEVIGEQPQIIKKK-----VLDVLDLVQLKHKARqfpDQ----LSGGEQQRVSIARSIVNSPEVVIADEP 164
Cdd:PRK10762 346 SVKENMSLtALRYFSRAGGSLKHAdeqqaVSDFIRLFNIKTPSM---EQaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 165 TGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-194 |
1.72e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 16 KAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK--DLGSIKE---KEIPYL---RREIGvvfqd 87
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDairAGIAYVpedRKGEG----- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 88 fkLLPTLTVFENVAFALevigeQPQIIKKKVLD-------VLDLV-QLKHKARQfPDQ----LSGGEQQRVSIARSIVNS 155
Cdd:COG1129 341 --LVLDLSIRENITLAS-----LDRLSRGGLLDrrreralAEEYIkRLRIKTPS-PEQpvgnLSGGNQQKVVLAKWLATD 412
|
170 180 190
....*....|....*....|....*....|....*....
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMAT 194
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS 451
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-195 |
1.75e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 10 IYP-NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQdf 88
Cdd:PRK10789 322 TYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQ-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 89 klLPTL---TVFENVAFAlevigeQPQIIKKKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIARSIVN 154
Cdd:PRK10789 397 --TPFLfsdTVANNIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEInNRGTTVVMATH 195
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-215 |
2.62e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.19 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKST----FIKMMYreekpSKGKILINNKDLGSIKEKEipy 76
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDGVSWNSVPLQK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQDFKLLpTLTVFENvafaLEVIGEQPQiikKKVLDVLDLVQLKHKARQFPDQL-----------SGGEQQR 145
Cdd:cd03289 75 WRKAFGVIPQKVFIF-SGTFRKN----LDPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEiNNRGTTVVMATHNKEIVNSMkKRVIAIEDGMI 215
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLEC-QRFLVIEENKV 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-192 |
3.66e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 12 PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLG--SIKEkeipylRREIGVVF---- 85
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglSPRE------RRRLGVAYiped 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 86 -QDFKLLPTLTVFENvaFALEVIGeQPQIIKKKVLDvldlvqlKHKARQF--------------PDQ----LSGGEQQRV 146
Cdd:COG3845 342 rLGRGLVPDMSVAEN--LILGRYR-RPPFSRGGFLD-------RKAIRAFaeelieefdvrtpgPDTparsLSGGNQQKV 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVM 192
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
3.93e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 6 EVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKD------LGSIKeKEIPYL-- 77
Cdd:PRK09700 267 EVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspLDAVK-KGMAYIte 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 78 -RREIGvvfqdfkLLPTLTVFENVAF-----------ALEVIGEQPQiiKKKVLDVLDLVQLK-HKARQFPDQLSGGEQQ 144
Cdd:PRK09700 346 sRRDNG-------FFPNFSIAQNMAIsrslkdggykgAMGLFHEVDE--QRTAENQRELLALKcHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 145 RVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMathnkeiVNSMKKRVIAIEDGMIVRDEAR 221
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM-------VSSELPEIITVCDRIAVFCEGR 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-213 |
4.62e-13 |
|
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: 67.54 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYRE-EKPSKGKILINNKDLgSIKEKEiPYLRREIGVVFQDFK---L 90
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPV-DIRNPA-QAIRAGIAMVPEDRKrhgI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 91 LPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLD--LVQLKHKARQfPD----QLSGGEQQRVSIARSIVNSPEVVIADE 163
Cdd:TIGR02633 351 VPILGVGKNITLSvLKSFCFKMRIDAAAELQIIGsaIQRLKVKTAS-PFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500859999 164 PTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-196 |
6.83e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLG-SIKEKEIPYLRRE 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQdfklLPTLTvfENVAFA--------LEVIGEQPQIIKKKVLDVLDLVQLKHkaRQFpDQLSGGEQQRVSIARSI 152
Cdd:PRK15056 87 EEVDWS----FPVLV--EDVVMMgryghmgwLRRAKKRDRQIVTAALARVDMVEFRH--RQI-GELSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500859999 153 VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHN 196
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-217 |
8.52e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 13 NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM--YREEKPSKGKILINNKdlgSIKEKEiPYLRREIGV--VFQ-- 86
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGE---SILDLE-PEERAHLGIflAFQyp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 87 ---------DFKLLP--------TLTVFENVAFaLEVIGEQpqiikkkvldvLDLVQLKHK--ARQFPDQLSGGEQQRVS 147
Cdd:CHL00131 94 ieipgvsnaDFLRLAynskrkfqGLPELDPLEF-LEIINEK-----------LKLVGMDPSflSRNVNEGFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAI-EDGMIVR 217
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVmQNGKIIK 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-130 |
9.04e-13 |
|
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: 66.75 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMM---YReekPSKGKILINNKdlgSIKEKEIPYLRREIGVVFQDFKLlptltvF 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLtglYR---PESGEILLDGQ---PVTADNREAYRQLFSAVFSDFHL------F 418
|
90 100 110
....*....|....*....|....*....|...
gi 500859999 98 EnvafalEVIGEQPQIIKKKVLDVLDLVQLKHK 130
Cdd:COG4615 419 D------RLLGLDGEADPARARELLERLELDHK 445
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
9.79e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipylRREIGVVF-----QDFKLLPTLT 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VFENVAfALeVIGEQPQIIK-KKVLDVLDL------VQLKHkARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:PRK15439 358 LAWNVC-AL-THNRRGFWIKpARENAVLERyrralnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-213 |
1.50e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYP-NGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKD-LGSIKEkeipyLR 78
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD-----VH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-170 |
1.66e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLlptltvFENVafaLEVIGEQPQiiKKKVLDVLDLVQLKHKAR----QFPD-QLSGGEQQRVSIARSIVNSP 156
Cdd:PRK10522 400 SAVFTDFHL------FDQL---LGPEGKPAN--PALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEER 468
|
170
....*....|....
gi 500859999 157 EVVIADEPTGNLDP 170
Cdd:PRK10522 469 DILLLDEWAADQDP 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-200 |
1.83e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEV-YKIypNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsikeKEIPYL--RR 79
Cdd:PRK11147 321 EMENVnYQI--DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------LEVAYFdqHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIgvvfqdfkLLPTLTVFENVAfalevIGEQPQIIKKKVLDVLDLVQ--LKH--KARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:PRK11147 392 AE--------LDPEKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLFHpkRAMTPVKALSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500859999 156 PEVVIADEPTGNLDPDTsweiMKTLEE-INNRGTTVVMATHNKEIV 200
Cdd:PRK11147 459 SNLLILDEPTNDLDVET----LELLEElLDSYQGTVLLVSHDRQFV 500
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-195 |
2.17e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIL-----INNKDLGSikekeipylRREIGVVFQDFKLL 91
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT---------RRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTLTVFENVA-----FALEvigeqPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTG 166
Cdd:NF033858 352 GELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|..
gi 500859999 167 NLDP---DTSWEIMKTLEEinNRGTTVVMATH 195
Cdd:NF033858 427 GVDPvarDMFWRLLIELSR--EDGVTIFISTH 456
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-216 |
4.32e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIY-PNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRRE 80
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVVFQDfkllPTLtvFE-NVAFALEVIGEQPQIikkKVLDVLDLVQLKHKARQFP-----------DQLSGGEQQRVSI 148
Cdd:PLN03130 1315 LGIIPQA----PVL--FSgTVRFNLDPFNEHNDA---DLWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSL 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 149 ARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC--DRILVLDAGRVV 1451
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-195 |
6.93e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMyrEEKPSKGKI-----LINNKDLGSikekeipYLRREIGVVFQDFKLLPTLTVFENVA 101
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVL--AERVTTGVItggdrLVNGRPLDS-------SFQRSIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 102 FALEVigEQPQIIKKK-----VLDVLDLVQLkhkaRQFPDQLSG--GE------QQRVSIARSIVNSPEVVI-ADEPTGN 167
Cdd:TIGR00956 859 FSAYL--RQPKSVSKSekmeyVEEVIKLLEM----ESYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180
....*....|....*....|....*...
gi 500859999 168 LDPDTSWEIMKTLEEINNRGTTVVMATH 195
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-171 |
6.96e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 25 IHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSI-KEKEIPYLRREIGvvfqdfkLLPTLTVFENVAFA 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLGHLPG-------LKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 104 LEVIGEQPQIIKKkvlDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:PRK13543 107 CGLHGRRAKQMPG---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-193 |
7.54e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGInvsIHPGEFVYVVGPSGAGKSTFIKMM----YREEKPSKGKILINNKDLGSIKekeiPYLRREIGVVFQDFKL 90
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIK----KHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 91 LPTLTVFENVAFA-------LEVIGEQPQIIKKKVLDV-LDLVQLKHK-----ARQFPDQLSGGEQQRVSIARSIVNSPE 157
Cdd:TIGR00956 150 FPHLTVGETLDFAarcktpqNRPDGVSREEYAKHIADVyMATYGLSHTrntkvGNDFVRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190
....*....|....*....|....*....|....*..
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINN-RGTTVVMA 193
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVA 266
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
7.76e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNkdlgSIKekeipylrreI 81
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TVK----------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQDFKLL-PTLTVFENVAFALEVIgeqpQIIKKKVldvldlvqlkhKARQF--------PDQ------LSGGEQQRV 146
Cdd:PRK11819 390 AYVDQSRDALdPNKTVWEEISGGLDII----KVGNREI-----------PSRAYvgrfnfkgGDQqkkvgvLSGGERNRL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTsweiMKTLEE--INNRGTTVV----------MATH 195
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEalLEFPGCAVVishdrwfldrIATH 511
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-216 |
1.51e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDfkllPTLtvFE-NVAFALEVIGEQPQiikKKVLDVLDLVQLKHKARQFP-----------DQLSGGEQQRVS 147
Cdd:PLN03232 1311 VLSIIPQS----PVL--FSgTVRFNIDPFSEHND---ADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLS 1381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSmkKRVIAIEDGMIV 216
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC--DKILVLSSGQVL 1448
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-215 |
1.62e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.43 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDFKLLP-----TLT 95
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFKITIIPQDPVLFSgslrmNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 96 VF-----ENVAFALEV------IGEQPQiikkkvldvldlvQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEP 164
Cdd:TIGR00957 1382 PFsqysdEEVWWALELahlktfVSALPD-------------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500859999 165 TGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMkkRVIAIEDGMI 215
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT--RVIVLDKGEV 1497
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-216 |
3.25e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYPNGVkAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPskgkilinnkDLGSIKEKEipylRREI 81
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP----------DSGTVKWSE----NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 82 GVVFQD----FKllPTLTVFENVA-FALEVIGEQ------------PQIIKKKVldvldlvqlkhkarqfpDQLSGGEQQ 144
Cdd:PRK15064 385 GYYAQDhaydFE--NDLTLFDWMSqWRQEGDDEQavrgtlgrllfsQDDIKKSV-----------------KVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 145 RVSIARSIVNSPEVVIADEPTGNLDpdtsweiMKTLEEINN-----RGtTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMalekyEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-215 |
4.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILInnkdlgsikekeipyLRREIGVVFQdFKLLPTLTVF 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV---------------IRGSVAYVPQ-VSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 98 ENVAFALEVIGEqpqiikkKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNSPEVVIADEPTG 166
Cdd:PLN03232 697 ENILFGSDFESE-------RYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500859999 167 NLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKrVIAIEDGMI 215
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR-IILVSEGMI 817
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
4.65e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 4 MKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIpyLRREIGV 83
Cdd:PRK10982 1 MSNISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 84 VFQDFKLLPTLTVFENVAfalevIGEQPQ----IIKKKVLD----VLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNS 155
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMW-----LGRYPTkgmfVDQDKMYRdtkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 156 PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-169 |
8.07e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 6 EVYKIYPNGVKAING--INVS---IHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKdlgsIKEKeiP-YLRR 79
Cdd:PRK13409 338 ETLVEYPDLTKKLGDfsLEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISYK--PqYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 80 EIGVVFQDFkllptltvFENVAFALEVIGEQPQIIKKKVLD-VLDlvqlkhkaRQFPDqLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK13409 412 DYDGTVEDL--------LRSITDDLGSSYYKSEIIKPLQLErLLD--------KNVKD-LSGGELQRVAIAACLSRDADL 474
|
170
....*....|.
gi 500859999 159 VIADEPTGNLD 169
Cdd:PRK13409 475 YLLDEPSAHLD 485
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-216 |
1.34e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPnGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMM--------YReekpskGKILINNK--DLGSIK 70
Cdd:NF040905 1 ILEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsYE------GEILFDGEvcRFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 71 EKEipylRREIGVVFQDFKLLPTLTVFENVAFALE-----VIGEQPQIIKKKVLdvLDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:NF040905 74 DSE----ALGIVIIHQELALIPYLSIAENIFLGNErakrgVIDWNETNRRAREL--LAKVGLDESPDTLVTDIGVGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 146 VSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIV 216
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-169 |
2.08e-10 |
|
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: 59.80 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEVYKIYPNGVKAINGINVS-----IHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinNKDLgSIKEKeiP-Y 76
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KISYK--PqY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREIGVVFQDFkllptltVFENVAFALEVIGEQPQIIKKkvldvldlVQLKHKARQFPDQLSGGEQQRVSIARSIVNSP 156
Cdd:COG1245 410 ISPDYDGTVEEF-------LRSANTDDFGSSYYKTEIIKP--------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170
....*....|...
gi 500859999 157 EVVIADEPTGNLD 169
Cdd:COG1245 475 DLYLLDEPSAHLD 487
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-216 |
2.20e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILinnkdlgsiKEKEIPYLRREIGVVfqdfkllpTLTVFENV 100
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYVPQQAWIM--------NATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 101 AFALEvigEQPQiikkKVLDVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:PTZ00243 742 LFFDE---EDAA----RLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 170 PDTSWEIMKTLEEINNRGTTVVMATHNKEIVnSMKKRVIAIEDGMIV 216
Cdd:PTZ00243 815 AHVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVE 860
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-215 |
3.59e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKP-SKGKILINnkdlGSIKEkeIPylrrEIGVVFQdfkllptLTVFEN 99
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIR----GTVAY--VP----QVSWIFN-------ATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVigEQPQIIKkkvldVLDLVQLKHKARQFP--DQ---------LSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:PLN03130 699 ILFGSPF--DPERYER-----AIDVTALQHDLDLLPggDLteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 169 DPDTSWEIMKTLEEINNRGTTVVMATHNKEIVnSMKKRVIAIEDGMI 215
Cdd:PLN03130 772 DAHVGRQVFDKCIKDELRGKTRVLVTNQLHFL-SQVDRIILVHEGMI 817
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-202 |
4.30e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.95 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 8 YKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKmmyreekpskgkilinnkdlgsikekeipylrrEIGVVFQD 87
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------------------EGLYASGK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 88 FKLLPTLTVFEnvafalevigEQPQIIKKKVLDVLDL----VQLKHKArqfpDQLSGGEQQRVSIARSIVNSPE--VVIA 161
Cdd:cd03238 48 ARLISFLPKFS----------RNKLIFIDQLQFLIDVglgyLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500859999 162 DEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNS 202
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-171 |
7.43e-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: 58.22 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMY--------REEKPSKGKILInnkdlgsIKEK 72
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY-------VPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 73 eiPYLRREigvvfqdfkllptlTVFENVAFALEVIGEQPQIIKKKVLD-VLDLVQLKH---------KARQFPDQLSGGE 142
Cdd:TIGR00954 524 --PYMTLG--------------TLRDQIIYPDSSEDMKRRGLSDKDLEqILDNVQLTHilereggwsAVQDWMDVLSGGE 587
|
170 180
....*....|....*....|....*....
gi 500859999 143 QQRVSIARSIVNSPEVVIADEPTGNLDPD 171
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-201 |
8.65e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 22 NVSIH--PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLgsikEKEIPYLRREIGVVFQDFKLLPTLTVFEN 99
Cdd:PRK13540 19 QISFHlpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVIGEQPQIIkkkvlDVLDLVQLKHKArQFP-DQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMK 178
Cdd:PRK13540 95 CLYDIHFSPGAVGIT-----ELCRLFSLEHLI-DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|...
gi 500859999 179 TLEEINNRGTTVVMATHNKEIVN 201
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSHQDLPLN 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-215 |
1.17e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKI-LINNKDLGSIKEKEIPYLRreigvvfQDFKLLPTLTV 96
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLR-------ADESPLQHLAR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FenvafalevigeQPQIIKKKVLDVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWE 175
Cdd:PRK10636 401 L------------APQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500859999 176 IMKTLeeINNRGTTVVMaTHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK10636 469 LTEAL--IDFEGALVVV-SHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-215 |
2.02e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYRE-EKPSKGKILINNKDLgSIK--EKEIpylRREIGVVFQDFK- 89
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPV-KIRnpQQAI---AQGIAMVPEDRKr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 --LLPTLTVFENVAFA-LEVIGEQPQIIKKKVLDVLD--LVQLKHKARQfPDQ----LSGGEQQRVSIARSIVNSPEVVI 160
Cdd:PRK13549 350 dgIVPVMGVGKNITLAaLDRFTGGSRIDDAAELKTILesIQRLKVKTAS-PELaiarLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 161 ADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
119-216 |
2.17e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 119 LDVLDLVQLKHKAR---QFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI-NNRGTTVVMAT 194
Cdd:PRK10418 119 TAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVT 198
|
90 100
....*....|....*....|..
gi 500859999 195 HNKEIVNSMKKRVIAIEDGMIV 216
Cdd:PRK10418 199 HDMGVVARLADDVAVMSHGRIV 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-199 |
2.44e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 3 EMKEvYKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMyrEEKPSKGKILINNKDLGSIKEKEIpyLRREIG 82
Cdd:PLN03140 882 EMKE-QGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIEGDIRISGFPKKQET--FARISG 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 83 VVFQDFKLLPTLTVFENVAFAL------EVIGEQPQIIKKKVLDVLDLVQLKHKARQFP--DQLSGGEQQRVSIARSIVN 154
Cdd:PLN03140 957 YCEQNDIHSPQVTVRESLIYSAflrlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEI 199
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-218 |
2.52e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 15 VKAINGINVSIHPGEFVYVVGPSGAGKStfikmmyREEKPSKgkilINNKDLGSIKEKEIPY------LRREIGVvFQDF 88
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**-------RGALPAH----V*GPDAGRRPWRF*TWcanrraLRRTIG*-HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 89 KL--LPTLTVFENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTG 166
Cdd:NF000106 94 R*grRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500859999 167 NLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRD 218
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
11-222 |
3.48e-09 |
|
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: 55.30 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAI-NGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsIKEKEIPYLRREIGVVFQDfk 89
Cdd:cd03288 29 YENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID---ISKLPLHTLRSRLSIILQD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 90 llPTLtvFE-NVAFALEvigEQPQIIKKKVLDVLDLVQLKHKARQFP-----------DQLSGGEQQRVSIARSIVNSPE 157
Cdd:cd03288 104 --PIL--FSgSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKtleeinnrgttVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARG 222
Cdd:cd03288 177 ILIMDEATASIDMATENILQK-----------VVMTAFADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-195 |
3.83e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 55 SKGKILINNKDLGSIKEKEipyLRREIGVVFQDfKLLPTLTVFENVAFALEvigeqpQIIKKKVLDVLDLVQLKHKARQF 134
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKD---LRNLFSIVSQE-PMLFNMSIYENIKFGKE------DATREDVKRACKFAAIDEFIESL 1344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 135 PDQ-----------LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRG-TTVVMATH 195
Cdd:PTZ00265 1345 PNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-179 |
3.92e-09 |
|
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: 55.25 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnKDLGSIKEKEipylrreigvvfQDFKLLPTlTVFENV 100
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KHSGRISFSS------------QFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 101 AFALEVIgeqpqiiKKKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:cd03291 119 IFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170
....*....|
gi 500859999 170 PDTSWEIMKT 179
Cdd:cd03291 192 VFTEKEIFES 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-179 |
4.20e-09 |
|
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: 56.07 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 14 GVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnKDLGSIK-EKEIPYLrreigvvfqdfklLP 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----KHSGRISfSPQTSWI-------------MP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 93 TlTVFENVAFALEVIgeqpqiiKKKVLDVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNSPEVVIA 161
Cdd:TIGR01271 501 G-TIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
170
....*....|....*...
gi 500859999 162 DEPTGNLDPDTSWEIMKT 179
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFES 590
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-202 |
6.92e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.72 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEIPYLRREIGVVFQdfkllptLTVFENV 100
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-------MTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 101 AFALEVIGE----QPQIIKKKVLDVLDLVQLKhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEI 176
Cdd:PRK13541 92 KFWSEIYNSaetlYAAIHYFKLHDLLDEKCYS---------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|....*.
gi 500859999 177 MKTLEEINNRGTTVVMATHNKEIVNS 202
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSHLESSIKS 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-196 |
7.90e-09 |
|
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: 54.29 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKiLINNKDLGSIkekeIPYLRreiGVVFQD-FKLLPTLTVfeNVAFALE 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI----LDEFR---GSELQNyFTKLLEGDV--KVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 106 VIGEQPQIIKKKVLDVL-------------DLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDT 172
Cdd:cd03236 95 YVDLIPKAVKGKVGELLkkkdergkldelvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....
gi 500859999 173 SWEIMKTLEEINNRGTTVVMATHN 196
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-223 |
1.73e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK--DLGSIKEKeI-------PYLRREIGVVfqdfkll 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDA-IragimlcPEDRKAEGII------- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 92 PTLTVFENVAfalevIGEQPQIIKKKVLdvLDLVQLKHKARQF----------PDQ----LSGGEQQRVSIARSIVNSPE 157
Cdd:PRK11288 344 PVHSVADNIN-----ISARRHHLRAGCL--INNRWEAENADRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 158 VVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMIVRDEARGE 223
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-180 |
6.15e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 18 INGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDLGSIKEKEipyLRREIGVVFQDfkllPTL--- 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSMIPQD----PVLfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 95 TVFENVAFALEVIGEQpqiikkkVLDVLDLVQLKHKARQFPDQL-----------SGGEQQRVSIARSIVNSPEVVI-AD 162
Cdd:PTZ00243 1399 TVRQNVDPFLEASSAE-------VWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSGFIlMD 1471
|
170
....*....|....*...
gi 500859999 163 EPTGNLDPDTSWEIMKTL 180
Cdd:PTZ00243 1472 EATANIDPALDRQIQATV 1489
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-204 |
7.16e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 1 MIEMKEVyKIYPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMY-REE-KPSKGKILINNKDLGSIKEKEipylr 78
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREDyEVTGGTVEFKGKDLLELSPED----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIGVVFQDFKLLPTLTVFENVAF---ALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQL---------SGGEQQRV 146
Cdd:PRK09580 75 RAGEGIFMAFQYPVEIPGVSNQFFlqtALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 147 SIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNSMK 204
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIK 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-200 |
1.61e-07 |
|
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: 50.69 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKSTFI----------KMMYREEKPSKGK-----------ILINNKDLG------------ 67
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDrieglehidkvIVIDQSPIGrtprsnpatytg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 68 ---SIKEK---------------EIPYLRREIGVVFQdfkllptLTVFEnvafALEVIGEQPQIIKK-KVL-DV-LDLVQ 126
Cdd:cd03271 94 vfdEIRELfcevckgkrynretlEVRYKGKSIADVLD-------MTVEE----ALEFFENIPKIARKlQTLcDVgLGYIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500859999 127 LKHKArqfpDQLSGGEQQRVSIARSIVN---SPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIV 200
Cdd:cd03271 163 LGQPA----TTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-201 |
3.24e-07 |
|
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: 48.51 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 20 GINVSIHPGEFVYVVGPSGAGKSTFIkmmyreekpskgkilinnkdlgsikekeipylrREIGVVfqdfkllptltVFEN 99
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTIL---------------------------------DAIGLA-----------LGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 100 VAFALEVIGEQPQIIKkkVLDVLDLVQLKHkarqfpdQLSGGEQQRVSIA-----RSIVNSPEVVIaDEPTGNLDPDTSW 174
Cdd:cd03227 49 QSATRRRSGVKAGCIV--AAVSAELIFTRL-------QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQ 118
|
170 180
....*....|....*....|....*..
gi 500859999 175 EIMKTLEEINNRGTTVVMATHNKEIVN 201
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-211 |
6.02e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAINGINVSIHPGEF-----VYVVGPSGAGKSTFIKMMYREEKPSKGKIlinnkdlgsikekEIPYLRreigvvf 85
Cdd:cd03222 3 YPDCVKRYGVFFLLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGIT------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 86 qdfkllptltvfenvafalevIGEQPQIIKkkvldvldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNSPEVVIADEPT 165
Cdd:cd03222 63 ---------------------PVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500859999 166 GNLDPDTSWEIMKTLEEINNRGT-TVVMATHNKEIVNSMKKRVIAIE 211
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
6.11e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNKDlgsikekeipylrreigvvfqdfkllptltvfenvafalev 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 107 igeqpqiikkKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLE----- 181
Cdd:smart00382 40 ----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|...
gi 500859999 182 -EINNRGTTVVMATHNKEIVNSM 203
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-213 |
1.66e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNkdlgsikekeipylrrEIGVVFQDFKLLPTLTV 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEI 176
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 500859999 177 MKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDG 213
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-214 |
1.93e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 33 VVGPSGAGKSTFI---KMMYREEKPSKGKILINNKDLGSIKEKeipylRREIGVVFQ-----DFKLLPTLTVFENVAFAL 104
Cdd:cd03240 27 IVGQNGAGKTTIIealKYALTGELPPNSKGGAHDPKLIREGEV-----RAQVKLAFEnangkKYTITRSLAILENVIFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 105 EviGEqpqiIKKKVLDVldlvqlkhkarqfPDQLSGGEQQ------RVSIARSIVNSPEVVIADEPTGNLDPDTSW---- 174
Cdd:cd03240 102 Q--GE----SNWPLLDM-------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEesla 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500859999 175 EIMKTLEEINNRGTTVVmaTHNKEIVNSMKK--RVIAIEDGM 214
Cdd:cd03240 163 EIIEERKSQKNFQLIVI--THDEELVDAADHiyRVEKDGRQK 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-200 |
2.58e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 21 INVSIHPGEFVYVVGPSGAGKST------------------------FIKMMyreEKPSKGKIlinnKDLG---SIKEKE 73
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsayarqFLGQM---DKPDVDSI----EGLSpaiAIDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 74 I-PYLRREIGVVFQDFKLLPTLtvfenvaFALEVIGEQPQIIKKKVLDVLDLvqlkhkARQFPdQLSGGEQQRVSIARSI 152
Cdd:cd03270 87 TsRNPRSTVGTVTEIYDYLRLL-------FARVGIRERLGFLVDVGLGYLTL------SRSAP-TLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500859999 153 VNSPEVV--IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIV 200
Cdd:cd03270 153 GSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-213 |
6.15e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 136 DQLSGGEQQRVSIARSIvnSPEVV----IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVnSMKKRVIAIE 211
Cdd:PRK00635 475 ATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIG 551
|
..
gi 500859999 212 DG 213
Cdd:PRK00635 552 PG 553
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-215 |
1.53e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 11 YPNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINNK--------------DLGSikeKEIPY 76
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmavfsqhhvdglDLSS---NPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREI-GVVFQDFKL-LPTLTVFENVAFalevigeQPQIikkkvldvldlvqlkhkarqfpdQLSGGEQQRVSIARSIVN 154
Cdd:PLN03073 595 MMRCFpGVPEQKLRAhLGSFGVTGNLAL-------QPMY-----------------------TLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500859999 155 SPEVVIADEPTGNLDPDTSWEIMKTLEEINNrgtTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQG---GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-192 |
2.67e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 138 LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVM 192
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-169 |
2.84e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPSKGkiliNNKDLGSIKE-------KEI-PYLRR----EIGVVF--QDFKLLP 92
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG----DYDEEPSWDEvlkrfrgTELqDYFKKlangEIKVAHkpQYVDLIP 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500859999 93 TltVFE-NVAFALEVIGEqpqiiKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLD 169
Cdd:COG1245 174 K--VFKgTVRELLEKVDE-----RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
73-202 |
3.47e-05 |
|
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: 44.23 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 73 EIPYLRREIGVVFQdfkllptLTVFEnvafALEVIGEQPQIIKKkvLDVLDLVQLKH-KARQFPDQLSGGEQQRVSIARS 151
Cdd:TIGR00630 777 EVKYKGKNIADVLD-------MTVEE----AYEFFEAVPSISRK--LQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKE 843
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 500859999 152 I---VNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVNS 202
Cdd:TIGR00630 844 LskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT 897
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
145-202 |
5.32e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 5.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 145 RVSIARSIVNSPEVVIADEPTGNLDPDT-SWeimktLEEI-NNRGTTVVMATHNKEIVNS 202
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTiRW-----LEDVlNERNSTMIIISHDRHFLNS 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-169 |
1.19e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 27 PGEFVYVVGPSGAGKSTFIKMMYREEKPskgkilinnkDLGSIKEK----EIpyLRREIGVVFQD-FKLLPTLTVfeNVA 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIP----------NLGDYEEEpswdEV--LKRFRGTELQNyFKKLYNGEI--KVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 102 FALEVIGEQPQIIKKKVLDVL-------------DLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNL 168
Cdd:PRK13409 164 HKPQYVDLIPKVFKGKVRELLkkvdergkldevvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 500859999 169 D 169
Cdd:PRK13409 244 D 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-215 |
1.34e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 17 AINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKILINnkdlGSIKEKEIpylrreigvvfqDFKLLPTLTV 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK----GSAALIAI------------SSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 97 FENVAFALEVIGEQPQIIKKKVLDVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEI 176
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 500859999 177 MKTLEEINNRGTTVVMATHNKEIVNSMKKRVIAIEDGMI 215
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-192 |
1.43e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 22 NVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPSKGKI-----------------LI------NNKDLGSIKEKEIPYLR 78
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitrlsfeqlqkLVsdewqrNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 79 REIgvvFQDFKLLPTLTvfenvafalEVIGEQPQIikKKVLDvldlvqlkhkaRQFpDQLSGGEQQRVSIARSIVNSPEV 158
Cdd:PRK10938 103 AEI---IQDEVKDPARC---------EQLAQQFGI--TALLD-----------RRF-KYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190
....*....|....*....|....*....|....
gi 500859999 159 VIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVM 192
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-192 |
1.59e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 500859999 138 LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVM 192
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
31-88 |
2.12e-04 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 40.82 E-value: 2.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 31 VYVVGPSGAGKSTFIKMMYR---EEKPSKGKIlINNKD-----LGSIKEKEIPYLRREIGVVFQDF 88
Cdd:cd19516 14 VYVAGATGSGKSTLLAAIYRyilENDPPDRKI-ITYEDpiefvYDGIKSKHSIIVQSQIPRHFKSF 78
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-200 |
3.47e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500859999 138 LSGGEQQRVSIARSIVNS---PEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIV 200
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV 875
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
5.20e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 2 IEMKEVYKIYpNGVKAINGINVSIHPGEFVYVVGPSGAGKSTFIKMMYREEKPS-KGKILINNKDLGSikEKEIPYLRRE 80
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRRRGS--GETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 81 IGVV----FQDFKLLPTLtvfENVAFA--LEVIG------EQPQIIKKKVLDVLDLVQLKHKArqfPDQ-LSGGEQQRVS 147
Cdd:PRK10938 338 IGYVssslHLDYRVSTSV---RNVILSgfFDSIGiyqavsDRQQKLAQQWLDILGIDKRTADA---PFHsLSWGQQRLAL 411
|
170 180
....*....|....*....|...
gi 500859999 148 IARSIVNSPEVVIADEPTGNLDP 170
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDP 434
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
26-45 |
1.33e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 1.33e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-201 |
1.43e-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: 38.91 E-value: 1.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 135 PDQLSGGEQQ---RVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKEIVN 201
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
77-198 |
1.86e-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: 38.84 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 77 LRREI------GVVFQDFKLLPtltVFENVAF--ALEVIGEQPQIIKKKV----------LDV-LDLVQLKHKArqfpDQ 137
Cdd:TIGR00630 416 LKPEAlavtvgGKSIADVSELS---IREAHEFfnQLTLTPEEKKIAEEVLkeirerlgflIDVgLDYLSLSRAA----GT 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500859999 138 LSGGEQQRVSIARSIVNSPEVV--IADEPTGNLDPDTSWEIMKTLEEINNRGTTVVMATHNKE 198
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
126-211 |
1.91e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500859999 126 QLKHKARQFpdqlSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTS-WeimktLEE-INNRGTTVVMATHNKEIVNSM 203
Cdd:PRK10636 142 QLERPVSDF----SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAViW-----LEKwLKSYQGTLILISHDRDFLDPI 212
|
....*...
gi 500859999 204 KKRVIAIE 211
Cdd:PRK10636 213 VDKIIHIE 220
|
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
28-45 |
4.79e-03 |
|
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274078 Cd Length: 179 Bit Score: 36.57 E-value: 4.79e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
138-183 |
5.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.52 E-value: 5.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 500859999 138 LSGGEQQRVSIARSIVNSPEVVIADEPTGNLDPDTSWEIMKTLEEI 183
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| |
