|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-243 |
9.86e-146 |
|
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: 407.45 E-value: 9.86e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVLQH 240
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
...
gi 60390566 241 IYR 243
Cdd:TIGR02315 241 IYG 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-242 |
2.76e-136 |
|
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: 383.46 E-value: 2.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVLQHI 241
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 60390566 242 Y 242
Cdd:cd03256 241 Y 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-248 |
2.48e-133 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 375.93 E-value: 2.48e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVLQH 240
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLRE 241
|
....*...
gi 60390566 241 IYRQPDQS 248
Cdd:COG3638 242 IYGGEAEE 249
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
4.01e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 230.32 E-value: 4.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS---LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:COG1136 4 LLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 R-HHIGMIFQNYNLISPLTALENVLhgrlgakstVAGML-GLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVG 155
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVA---------LPLLLaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIV 225
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-233 |
5.37e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 230.27 E-value: 5.37e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAELRKVRHH 80
Cdd:COG1126 1 MIEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLgaksTVAGMlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPI----KVKKM----SKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVT-HEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-224 |
2.32e-74 |
|
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: 225.45 E-value: 2.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNK---HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVR 78
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 H-HIGMIFQNYNLISPLTALENVLhgrLGAKstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVE---LPLL-----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAI 224
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-243 |
6.25e-71 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 218.34 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD----SGQILLDDTDIRQANKA-ELR 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ-ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagSHIELLGRTVQREGRLArDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KVRHHIGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVG 155
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
....*...
gi 60390566 236 AVLQHIYR 243
Cdd:PRK09984 243 ERFDHLYR 250
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-224 |
7.84e-71 |
|
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: 216.24 E-value: 7.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAELRKVRHHI 81
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLhgrlGAKSTVAGMlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENIT----LAPIKVKGM----SKAEAEErALELLEKVGLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAI 224
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVT-HEMGFAREVADRVIFMDDGRI 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
1.19e-70 |
|
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: 217.22 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:COG1120 1 MLEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKstvaGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGRYPHL----GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV-DDAVLQ 239
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVlTPELLE 232
|
....*.
gi 60390566 240 HIYRQP 245
Cdd:COG1120 233 EVYGVE 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-233 |
3.34e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 211.09 E-value: 3.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK---HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENV---LhgrlgaksTVAGMlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQR 153
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpL--------EIAGV----PKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLtIVLIT-HEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
.
gi 60390566 233 V 233
Cdd:COG1135 228 V 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
3.83e-67 |
|
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: 207.43 E-value: 3.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK---HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENV-----LHGrlgakstvagmlglYSSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQ 151
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENValpleIAG--------------VPKAEiEERVLELLELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATN 231
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
..
gi 60390566 232 EV 233
Cdd:cd03258 227 EV 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
1.34e-65 |
|
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: 204.06 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHsLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVV-LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVL-----HGRLgakstvagmlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQRV 154
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAfplreHTDL-------------SEAEIRElVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 155 GIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV- 233
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELl 230
|
....*...
gi 60390566 234 --DDAVLQ 239
Cdd:COG1127 231 asDDPWVR 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-235 |
5.20e-65 |
|
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: 202.35 E-value: 5.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIFQ 86
Cdd:cd03261 6 LTKSFGG-RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISPLTALENVL-----HGRLgakstvagmlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:cd03261 85 SGALFDSLTVFENVAfplreHTRL-------------SEEEIREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-244 |
1.03e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.44 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqankAELRKVRHHI 81
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHgrlgakstVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRF--------FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEkQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVLQHI 241
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDV 226
|
...
gi 60390566 242 YRQ 244
Cdd:COG1131 227 FLE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
6.12e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 200.13 E-value: 6.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS----LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRK 76
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 VRHHIGMIFQN-YNLISP-LTALENVLHG-RLgakstvagmLGLYSSAE-KQEALQLLDEVGL-KEYAYQRCDQLSGGQQ 151
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPrMTVGDIIAEPlRL---------HGLLSRAErRERVAELLERVGLpPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHqvDIAMA--YTDHIVGINSGAIVFEGA 229
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH--DLAVVryIADRVAVMYDGRIVEDGP 488
|
250
....*....|....*
gi 60390566 230 TNEVDDAVlQHIYRQ 244
Cdd:COG1123 489 TEEVFANP-QHPYTR 502
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
8.01e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 191.84 E-value: 8.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnkaelrkvRHH 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLIS--PLTALENVLHGRLGAKstvaGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:COG1121 77 IGYVPQRAEVDWdfPITVRDVVLMGRYGRR----GLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSGaIVFEGATNEV-DDAV 237
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVV-THDLGAVREYFDRVLLLNRG-LVAHGPPEEVlTPEN 230
|
....*...
gi 60390566 238 LQHIYRQP 245
Cdd:COG1121 231 LSRAYGGP 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
6.29e-60 |
|
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: 189.08 E-value: 6.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaeLRKVRHHI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYN--LISPlTALENVLHG--RLGakstvagmlglYSSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:COG1122 78 GLVFQNPDdqLFAP-TVEEDVAFGpeNLG-----------LPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVT-HDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-239 |
3.02e-58 |
|
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: 185.63 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnkhsLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELrkV 77
Cdd:COG0411 4 LLEVRGLTKRFGG----LVAVDdvsLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENVL---HGRLGAkSTVAGMLGLYSSAEK-----QEALQLLDEVGLKEYAYQRCDQLSGG 149
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLvaaHARLGR-GLLAALLRLPRARREerearERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGItILLIE-HDMDLVMGLADRIVVLDFGRVIAEG 235
|
250
....*....|...
gi 60390566 229 ATNEV--DDAVLQ 239
Cdd:COG0411 236 TPAEVraDPRVIE 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-228 |
1.98e-57 |
|
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: 181.96 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdtdirqanKAELRKVRHHIGMIFQNYNL-- 90
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF--------GKPLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 ISPLTALENVLHGRLGAKstvaGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:cd03235 82 DFPISVRDVVLMGLYGHK----GLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSGaIVFEG 228
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVV-THDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-237 |
1.51e-56 |
|
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: 180.71 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSnkhsLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqANKAELRKVR 78
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDdvsFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSS--AEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREerEARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV--D 234
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVE-HDMDVVMSLADRVTVLDQGRVIAEGTPDEVrnN 233
|
...
gi 60390566 235 DAV 237
Cdd:cd03219 234 PRV 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-233 |
1.79e-56 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 183.85 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK---HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:PRK11153 1 MIELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENV---LhgrlgaksTVAGMlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQR 153
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNValpL--------ELAGT----PKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-191 |
1.90e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 179.86 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENV---LHgrlgakstVAGMlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENValpLR--------VTGK----SRKEiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRL 191
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEI 183
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.99e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 181.06 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKA---VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnkaelrkv 77
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTAlddVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLIsP-LTALENVlhgRLGAKstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:COG1116 79 GPDRGVVFQEPALL-PwLTVLDNV---ALGLE-----LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVD--IAMAytDHIV 217
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaVFLA--DRVV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-225 |
5.83e-56 |
|
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: 178.48 E-value: 5.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHsLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHI 81
Cdd:cd03259 1 LELKGLSKTYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHG-RLGAKSTvagmlglysSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGlKLRGVPK---------AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIV 225
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-222 |
6.12e-56 |
|
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: 176.99 E-value: 6.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKaELRKVRHHI 81
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED-ELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHGrlgakstvagmlglyssaekqealqlldevglkeyayqrcdqLSGGQQQRVGIARALM 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSG 222
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-241 |
1.87e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 175.43 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQankaELRKVRHH 80
Cdd:COG4555 1 MIEVENLSKKYGK-VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENV-LHGRLgakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIrYFAEL---------YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKqLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV------ 233
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELreeige 225
|
250
....*....|.
gi 60390566 234 ---DDAVLQHI 241
Cdd:COG4555 226 enlEDAFVALI 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-241 |
5.88e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.13 E-value: 5.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqANKAELRKVRHH 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-DPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKstvagmlGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPLRVR-------GASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDA---- 236
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT-HEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNppsq 230
|
....*....
gi 60390566 237 ----VLQHI 241
Cdd:PRK09493 231 rlqeFLQHV 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
8.88e-54 |
|
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: 173.04 E-value: 8.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKA---VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaelrkvr 78
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAledISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLhgrLGAKstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVA---LGLE-----LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 159 ALMQHPKMILCDEPIASLDPKsTTIVM--DILRRLAKEKQLIILINlHQVDIAMAYTDHIV 217
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAL-TREQLqeELLDIWRETGKTVLLVT-HDIDEAVFLADRVV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-228 |
9.89e-54 |
|
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: 173.08 E-value: 9.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKA---VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQN-YNLISPL----TALENVL--HGRLGAKstvagmlglysSAEKQEALQLLDEVGL-KEYAYQRCDQLSGG 149
Cdd:cd03257 81 RKEIQMVFQDpMSSLNPRmtigEQIAEPLriHGKLSKK-----------EARKEAVLLLLVGVGLpEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-228 |
5.09e-52 |
|
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: 167.23 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIf 85
Cdd:cd03214 4 NLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR---KIAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 qnynlispltalenvlhgrlgakstvagmlglyssaekqeaLQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:cd03214 79 -----------------------------------------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
1.37e-51 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 168.39 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQA-----NKAELR 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KVRHHIGMIFQNYNLISPLTALENVLHGRLGAKSTVAGmlglyssAEKQEALQLLDEVGL--KEYAYQRcdQLSGGQQQR 153
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKE-------EATARARELLAKVGLagKETSYPR--RLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
1.66e-51 |
|
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: 168.06 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS---LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqanKAELRKV 77
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNynlisPLTALenvlHGRLGAKSTVA-GMLGLYSSAEKQEALQLLDEVGL-KEYAYQRCDQLSGGQQQRVG 155
Cdd:COG1124 78 RRRVQMVFQD-----PYASL----HPRHTVDRILAePLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
....*..
gi 60390566 236 AVlQHIY 242
Cdd:COG1124 229 GP-KHPY 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-252 |
2.31e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 171.05 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI--RQANKaelrkvR 78
Cdd:COG3842 5 ALELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgLPPEK------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HhIGMIFQNYNLISPLTALENVlhgRLGAKstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:COG3842 78 N-VGMVFQDYALFPHLTVAENV---AFGLR-----MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvddavl 238
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE------ 222
|
250
....*....|....
gi 60390566 239 qhIYRQPdQSTAVA 252
Cdd:COG3842 223 --IYERP-ATRFVA 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
4.55e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 166.47 E-value: 4.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsnkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElRKVrhh 80
Cdd:COG3840 1 MLRLDDLTYRYG---DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RPV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 iGMIFQNYNLISPLTALENVLhgrlgakstvagmLGL-----YSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVG 155
Cdd:COG3840 74 -SMLFQENNLFPHLTVAQNIG-------------LGLrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-222 |
7.91e-51 |
|
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: 165.33 E-value: 7.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYN-- 89
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR---KVGLVFQNPDdq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPlTALENVLHGrlgakstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:cd03225 88 FFGP-TVEEEVAFG--------LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSG 222
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVT-HDLDLLLELADRVIVLEDG 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-228 |
6.09e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 164.03 E-value: 6.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQ--ILLDDTDIRQANKA-ELRKVR 78
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFSKTPSDkAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLHgrlgAKSTVagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIE----APCRV---LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAkEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-233 |
1.16e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 163.82 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQ----------AN 70
Cdd:COG4598 8 ALEVRDLHKSFGDL-EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvpAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 71 KAELRKVRHHIGMIFQNYNLISPLTALENVLHGRLgaksTVAGMlglySSAE-KQEALQLLDEVGLkeyaYQRCD----Q 145
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPV----HVLGR----PKAEaIERAEALLAKVGL----ADKRDaypaH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 146 LSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIV 225
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVT-HEMGFARDVSSHVVFLHQGRIE 233
|
....*...
gi 60390566 226 FEGATNEV 233
Cdd:COG4598 234 EQGPPAEV 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-233 |
1.84e-49 |
|
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: 162.86 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIF 85
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR---KIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 QNYNLISPLTALENVlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGL--KEYAYQRCDQLSGGQQQRVGIARALMQH 163
Cdd:cd03295 82 QQIGLFPHMTVEENI--------ALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
6.97e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.16 E-value: 6.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSN-KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDTDIRQANKAELRK 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 vrhHIGMIFQNynlisPLTALENVlhgRLGAKSTVAGMLGLYSSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVG 155
Cdd:COG1123 84 ---RIGMVFQD-----PMTQLNPV---TVGDQIAEALENLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-201 |
7.74e-49 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 163.30 E-value: 7.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRD---DSGQILLDDTDIRQANKAEL 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDgvsFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKVR-HHIGMIFQNynlisPLTALeN-------------VLHGRLGAKstvagmlglyssAEKQEALQLLDEVGLKEyAY 140
Cdd:COG0444 81 RKIRgREIQMIFQD-----PMTSL-NpvmtvgdqiaeplRIHGGLSKA------------EARERAIELLERVGLPD-PE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 141 QRCD----QLSGGQQQRVGIARALMQHPKMILCDEPIASLDPkstTI---VMDILRRLAKEKQL-IILI 201
Cdd:COG0444 142 RRLDryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV---TIqaqILNLLKDLQRELGLaILFI 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-237 |
9.34e-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: 161.66 E-value: 9.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVR-HHIGMIFQNYNLISPLTA 96
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGRlgaksTVAGMlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIAS 175
Cdd:cd03294 120 LENVAFGL-----EVQGV----PRAEREErAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 176 LDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGA-----TNEVDDAV 237
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTpeeilTNPANDYV 257
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-243 |
1.12e-48 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 161.05 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRhh 80
Cdd:COG4559 1 MLEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 iGMIFQNYNLISPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:COG4559 78 -AVLPQHSSLAFPFTVEEVVALGRAP--------HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQ-------HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG4559 149 AQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAV-LHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
250
....*....|.
gi 60390566 234 -DDAVLQHIYR 243
Cdd:COG4559 228 lTDELLERVYG 238
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.19e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.57 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVlhgrlgakSTVAGMLGlYSSAEKQE-ALQLLDEVGL--KEYAYQRCDQLSGGQQQRVGIA 157
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENI--------ATVPRLLG-WDKERIRArVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIV 225
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-228 |
1.29e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI---RQANKAELRKVR 78
Cdd:COG4161 3 IQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLHgrlgAKSTVagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIE----APCKV---LGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKE--KQLIIlinLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgiTQVIV---THEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-174 |
1.33e-48 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 157.42 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLISPLTAL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK---EIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCD----QLSGGQQQRVGIARALMQHPKMILCDEPI 173
Cdd:pfam00005 78 ENLRLGLL--------LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 60390566 174 A 174
Cdd:pfam00005 150 A 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-252 |
1.42e-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: 161.47 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 5 IQLDK---TYGSN----KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV 77
Cdd:TIGR04521 1 IKLKNvsyIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQN--YNLISpLTALENVLHGRLgakstvagMLGLySSAE-KQEALQLLDEVGLKE-YAYQRCDQLSGGQQQR 153
Cdd:TIGR04521 81 RKKVGLVFQFpeHQLFE-ETVYKDIAFGPK--------NLGL-SEEEaEERVKEALELVGLDEeYLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLtVILVT-HSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
250 260
....*....|....*....|..
gi 60390566 233 V--DDAVLQHIYRQPDQSTAVA 252
Cdd:TIGR04521 230 VfsDVDELEKIGLDVPEITELA 251
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-252 |
1.99e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.01 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnkaelRKVRH-H 80
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----LPPRErR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGrLGAKSTvagmlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFG-LRVRPP--------SKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVddavlq 239
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV------ 221
|
250
....*....|...
gi 60390566 240 hiYRQPdQSTAVA 252
Cdd:COG1118 222 --YDRP-ATPFVA 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-206 |
3.03e-48 |
|
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: 159.27 E-value: 3.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLI-----RDDSGQILLDDTDIRQANKAELRkVRHHI 81
Cdd:cd03260 6 LNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLE-LRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLIsPLTALENVlhgRLGAKstVAGMLGlySSAEKQEALQLLDEVGLKEYAYQRCD--QLSGGQQQRVGIARA 159
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNV---AYGLR--LHGIKL--KEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI-NLHQV 206
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThNMQQA 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-235 |
7.11e-48 |
|
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: 157.98 E-value: 7.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqANKAELRKVRHHI 81
Cdd:cd03224 1 LEVENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI--TGLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHG-RLGAKSTVAGMLglyssaekQEALQLLDEvgLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGaYARRRAKRKARL--------ERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVE-QNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
7.88e-48 |
|
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: 158.37 E-value: 7.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS---LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAN---KAEL 74
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RkvRHHIGMIFQNYNLISPLTALENV-----LHGRLGAKstvagmlglyssaekQEALQLLDEVGLKEYAYQRCDQLSGG 149
Cdd:COG4181 88 R--ARHVGFVFQSFQLLPTLTALENVmlpleLAGRRDAR---------------ARARALLERVGLGHRLDHYPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIV 225
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-242 |
1.26e-47 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 158.32 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:COG4604 1 MIEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVL-------HGRLGAKSTvagmlglyssAEKQEALQLLDevgLKEYAYQRCDQLSGGQQQR 153
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAfgrfpysKGRLTAEDR----------EIIDEAIAYLD---LEDLADRYLDELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
250
....*....|
gi 60390566 234 -DDAVLQHIY 242
Cdd:COG4604 224 iTPEVLSDIY 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-245 |
2.30e-47 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 157.63 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRhh 80
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 iGMIFQNYNLISPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK13548 79 -AVLPQHSSLSFPFTVEEVVAMGRAP--------HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQ------HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV- 233
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVl 229
|
250
....*....|..
gi 60390566 234 DDAVLQHIYRQP 245
Cdd:PRK13548 230 TPETLRRVYGAD 241
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-201 |
2.52e-47 |
|
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: 156.24 E-value: 2.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 4 VIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV-RHHIG 82
Cdd:TIGR03608 1 LKNISKKFG-DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 83 MIFQNYNLISPLTALENVLHGRLGAKSTVAgmlglyssaEKQEAL-QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKK---------EKREKKkEALEKVGLNLKLKQKIYELSGGEQQRVALARAIL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:TIGR03608 151 KPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIV 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-252 |
3.24e-47 |
|
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: 156.63 E-value: 3.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHI 81
Cdd:cd03300 1 IELENVSKFYGG-FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHGrlgakstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFG--------LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvddavlqhI 241
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE--------I 218
|
250
....*....|.
gi 60390566 242 YRQPdQSTAVA 252
Cdd:cd03300 219 YEEP-ANRFVA 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-205 |
2.05e-46 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 155.19 E-value: 2.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSIN---QLIRDD--SGQILLDDTDI--RQANKAEL 74
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmnDLIPGArvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKvrhHIGMIFQNYNLIsPLTALENVLHG-RLgakstvagmLGLYSSAEKQE----ALQ---LLDEVG--LKEYAYQrcd 144
Cdd:COG1117 91 RR---RVGMVFQKPNPF-PKSIYDNVAYGlRL---------HGIKSKSELDEiveeSLRkaaLWDEVKdrLKKSALG--- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 145 qLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILI--NLHQ 205
Cdd:COG1117 155 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVthNMQQ 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-233 |
2.12e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 156.42 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqankaelRKVRHH 80
Cdd:COG4152 1 MLELKGLTKRFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGmifqnY-----NLISPLTALENVLH-GRLgakstvAGMlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQR 153
Cdd:COG4152 73 IG-----YlpeerGLYPKMKVGEQLVYlARL------KGL----SKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSS-HQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-233 |
2.72e-46 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 155.13 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQ----------ANK 71
Cdd:PRK10619 6 LNVIDLHKRYGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 72 AELRKVRHHIGMIFQNYNLISPLTALENVLHGRLGakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCD-QLSGGQ 150
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQ-------VLGLSKQEARERAVKYLAKVGIDERAQGKYPvHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 151 QQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGAT 230
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT-HEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
...
gi 60390566 231 NEV 233
Cdd:PRK10619 237 EQL 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-239 |
8.31e-46 |
|
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: 153.21 E-value: 8.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnKAElRKVRHH 80
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPH-RIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVlhgrlgakstvagMLGLYSSAEKQEALQLLDEVG-----LKEYAYQRCDQLSGGQQQRVG 155
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENL-------------LLGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQvdiAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVeqNARF---ALEIADRAYVLERGRIVLEGTAAEL 223
|
....*...
gi 60390566 234 --DDAVLQ 239
Cdd:COG0410 224 laDPEVRE 231
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-233 |
8.88e-46 |
|
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: 156.55 E-value: 8.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV-RHHIGMIFQN 87
Cdd:TIGR01186 1 KKTGGKK-GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPLTALENVlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:TIGR01186 80 FALFPHMTILQNT--------SLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-178 |
1.90e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 153.72 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVR-HHIGMIFQNYNLISPLTALEN 99
Cdd:COG4175 46 ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTVLEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 100 VLHGrLgaksTVAGMlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDP 178
Cdd:COG4175 126 VAFG-L----EIQGV----PKAERRErAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-228 |
6.22e-44 |
|
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: 147.34 E-value: 6.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGeVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqANKAELRKvrhHI 81
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRR---RI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHgrlgakstVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDY--------IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKqlIILINLHQV-DIAMAYTDHIVgINSGAIVFEG 228
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVeDVESLCNQVAV-LNKGKLVFEG 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-197 |
1.01e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 150.27 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY-------GSNKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANK 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfGRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 72 AELRKVRHHIGMIFQNynlisPLTALenvlHGRLgaksTVAGML-------GLYSSAEKQE-ALQLLDEVGLKEYAYQRC 143
Cdd:COG4608 88 RELRPLRRRMQMVFQD-----PYASL----NPRM----TVGDIIaeplrihGLASKAERRErVAELLELVGLRPEHADRY 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 144 -DQLSGGQQQRVGIARALMQHPKMILCDEPIASLDpKSttI---VMDILRRLAKEKQL 197
Cdd:COG4608 155 pHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS--IqaqVLNLLEDLQDELGL 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-228 |
1.01e-43 |
|
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: 147.13 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK---HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQankaELRKV 77
Cdd:cd03266 1 MITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENVLHgrlgakstVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEY--------FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-193 |
9.23e-43 |
|
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: 144.70 E-value: 9.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENV---LHGRlGAKSTVAGmlglyssaekQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENValpLEVR-GKKEREIQ----------RRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIA 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAK 193
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK 185
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-237 |
1.01e-42 |
|
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: 147.15 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI-RQAnkaelRKVRHHIGMIFQN 87
Cdd:TIGR01188 1 KVYGDFK-AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREP-----RKVRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPLTALEN-VLHGRLgakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:TIGR01188 75 ASVDEDLTGRENlEMMGRL---------YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAV 237
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTT-HYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-222 |
1.70e-42 |
|
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: 142.54 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqanKAELRKVRHHI 81
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcdQLSGGQQQRVGIARALM 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSG 222
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSS-HILEEAERLCDRVAILNNG 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-232 |
1.76e-42 |
|
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: 144.05 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQankaELRKVRHHIGMIFQ 86
Cdd:cd03265 6 LVKKYGDFE-AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISPLTALENV-LHGRLgakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:cd03265 81 DLSVDDELTGWENLyIHARL---------YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-224 |
3.28e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 3.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHsLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHI 81
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR---QV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPlTALENVLHGRLGAKSTVagmlglyssaEKQEALQLLDEVGL-KEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF----------DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAI 224
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-253 |
7.05e-42 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 146.40 E-value: 7.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKViQLDKTYGSnkHSLkAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLD-----DTDIRQANKAELR 75
Cdd:COG4148 2 MLEV-DFRLRRGG--FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSARGIFLPPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 kvrhHIGMIFQNYNLISPLTALENVLHGRLGAKST--------VAGMLGLyssaekqEALqlLDevglkeyayQRCDQLS 147
Cdd:COG4148 78 ----RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAerrisfdeVVELLGI-------GHL--LD---------RRPATLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFE 227
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
250 260
....*....|....*....|....*..
gi 60390566 228 GATNEV-DDAVLQHIYRQPDQSTAVAA 253
Cdd:COG4148 216 GPLAEVlSRPDLLPLAGGEEAGSVLEA 242
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
3.78e-41 |
|
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: 141.14 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkvRHHI 81
Cdd:cd03218 1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIF--QNYNLISPLTALENVLhgrlgaksTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:cd03218 76 GIGYlpQEASIFRKLTVEENIL--------AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
4.74e-41 |
|
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: 139.92 E-value: 4.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAelrkVRHH 80
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHgrlgakstVAGMLGLYSSAEkqEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRF--------WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIL 200
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-222 |
9.72e-41 |
|
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: 137.38 E-value: 9.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 3 KVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIG 82
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR---RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 83 MIFQnynlispltalenvlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcdqLSGGQQQRVGIARALMQ 162
Cdd:cd00267 77 YVPQ-----------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 163 HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSG 222
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIV-THDPELAELAADRVIVLKDG 156
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-225 |
1.86e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.46 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYN 89
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR---QIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISpLTALENVLHGRLGAkstvagmlglySSAEKQEALQL--LDEV------GLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:COG1132 425 LFS-GTIRENIRYGRPDA-----------TDEEVEEAAKAaqAHEFiealpdGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlI--NLHQVDIAmaytDHIVGINSGAIV 225
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIV-IahRLSTIRNA----DRILVLDDGRIV 553
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-252 |
2.79e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 142.13 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHsLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqaNKAELRKvRHh 80
Cdd:COG3839 3 SLELENVSKSYGGVEA-LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKD-RN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGrLgaksTVAGMlglySSAEK----QEALQLLdevGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFP-L----KLRKV----PKAEIdrrvREAAELL---GLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLH-QVDiAMAYTDHIVGINSGAIVFEGATNEvdd 235
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVE-AMTLADRIAVMNDGRIQQVGTPEE--- 220
|
250
....*....|....*..
gi 60390566 236 avlqhIYRQPdQSTAVA 252
Cdd:COG3839 221 -----LYDRP-ANLFVA 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
2.85e-40 |
|
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: 139.87 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqaNKAELRKVRHH 80
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNynlisPltalENVLHGrlgakSTVA-----GM--LGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQR 153
Cdd:TIGR04520 79 VGMVFQN-----P----DNQFVG-----ATVEddvafGLenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVD-IAMAytDHIVGINSGAIVFEGATN 231
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGItVISIT-HDMEeAVLA--DRVIVMNKGKIVAEGTPR 221
|
..
gi 60390566 232 EV 233
Cdd:TIGR04520 222 EI 223
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-233 |
3.21e-40 |
|
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: 138.97 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLirDD-------SGQILLDDTDI--RQANKA 72
Cdd:TIGR00972 2 IEIENLNLFYG-EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRM--NDlvpgvriEGKVLFDGQDIydKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 73 ELRKvrhHIGMIFQNYNLIsPLTALENVLHGrlgakstvAGMLGLYSSAEKQEALQ-------LLDEVG--LKEYAYQrc 143
Cdd:TIGR00972 79 ELRR---RVGMVFQKPNPF-PMSIYDNIAYG--------PRLHGIKDKKELDEIVEeslkkaaLWDEVKdrLHDSALG-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 144 dqLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAkeKQLIILINLHQVDIAMAYTDHIVGINSGA 223
Cdd:TIGR00972 145 --LSGGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELK--KKYTIVIVTHNMQQAARISDRTAFFYDGE 220
|
250
....*....|
gi 60390566 224 IVFEGATNEV 233
Cdd:TIGR00972 221 LVEYGPTEQI 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-232 |
6.86e-40 |
|
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: 137.25 E-value: 6.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSN-KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQankaELRKVRHH 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENV-LHGRLGakstvagmlGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLrFYARLK---------GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQliILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRS--IILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
8.52e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.85 E-value: 8.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI------RQAnkael 74
Cdd:COG1137 3 TLEAENLVKSYGK-RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhKRA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 rkvRHHIGM------IFQNynlispLTALENVLhgrlgaksTVAGMLGLySSAEKQEAL-QLLDEVGLKEYAYQRCDQLS 147
Cdd:COG1137 77 ---RLGIGYlpqeasIFRK------LTVEDNIL--------AVLELRKL-SKKEREERLeELLEEFGITHLRKSKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFE 227
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
....*.
gi 60390566 228 GATNEV 233
Cdd:COG1137 218 GTPEEI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-222 |
8.90e-40 |
|
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: 135.59 E-value: 8.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLI 91
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK---NIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SpLTALENVlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcdqLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:cd03228 89 S-GTIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKqLIILI--NLHQVDIAmaytDHIVGINSG 222
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGK-TVIVIahRLSTIRDA----DRIIVLDDG 170
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
9.88e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.67 E-value: 9.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAeLRKVRHH 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS-LLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYN--LISPlTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:PRK13639 80 VGIVFQNPDdqLFAP-TVEEDVAFGPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITII-ISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
1.54e-39 |
|
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: 137.09 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkvrHHI 81
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHG-RLGAKSTVAgmlglySSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGlRVKPRSERP------PEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDA 236
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-233 |
1.63e-39 |
|
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: 144.98 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLI 91
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR---QIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPlTALENVLHGRlgakstvagmlglySSAEKQEALQLLDEVGLKEYAYQRCD-----------QLSGGQQQRVGIARAL 160
Cdd:COG2274 562 SG-TIRENITLGD--------------PDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlinlhqvdIA-----MAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII--------IAhrlstIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-224 |
2.19e-39 |
|
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: 136.00 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 5 IQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMI 84
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 85 FQNYNLISPLTALENVlhgrlgakstvagMLGLYSSAEKQEALQ-----LLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:cd03292 84 FQDFRLLPDRNVYENV-------------AFALEVTGVPPREIRkrvpaALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKeKQLIILINLHQVDIAMAYTDHIVGINSGAI 224
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
4-228 |
2.42e-39 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 135.89 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 4 VIQLDKTYGSnkHSLKaVNFTAkPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDT---DIRQanKAELRKVRHH 80
Cdd:cd03297 3 CVDIEKRLPD--FTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRK--KINLPPQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGrlgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:cd03297 77 IGLVFQQYALFPHLNVRENLAFG----------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-228 |
3.01e-39 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 135.42 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdtdirQANKAELRKVRHHI 81
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-----GKSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVlhgRLGAKstvagMLGLyssaEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENL---RLLAR-----LLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKqLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-232 |
3.62e-39 |
|
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: 142.97 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYN 89
Cdd:COG4988 345 SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR---QIAWVPQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LIsPLTALENVLHGRLGAkstvagmlglySSAEKQEALQLldeVGLKEYAYQRCD-----------QLSGGQQQRVGIAR 158
Cdd:COG4988 422 LF-AGTIRENLRLGRPDA-----------SDEELEAALEA---AGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKqLIILI--NLHQVDIAmaytDHIVGINSGAIVFEGATNE 232
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR-TVILIthRLALLAQA----DRILVLDDGRIVEQGTHEE 557
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-246 |
4.73e-39 |
|
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: 139.02 E-value: 4.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHI 81
Cdd:TIGR03265 5 LSIDNIRKRFG-AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI-----TRLPPQKRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENV---LHGRLGAKSTVAgmlglyssaekQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIaygLKNRGMGRAEVA-----------ERVAELLDLVGLPGSERKYPGQLSGGQQQRVALAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPKMILCDEPIASLDPKsttiVMDILRRLAKE--KQLII--LINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvd 234
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALDAR----VREHLRTEIRQlqRRLGVttIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE-- 221
|
250
....*....|..
gi 60390566 235 davlqhIYRQPD 246
Cdd:TIGR03265 222 ------IYRHPA 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-238 |
9.27e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.93 E-value: 9.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDD--TDIRQANKAelrkVR 78
Cdd:COG3845 5 ALELRGITKRFGGV-VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA----IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLhgrLGAKSTVAGMLGLysSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIV---LGLEPTKGGRLDR--KAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPK-MILcDEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQVdiaMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:COG3845 155 ALYRGARiLIL-DEPTAVLTPQEADELFEILRRLAAEGKSIIFIthKLREV---MAIADRVTVLRRGKVVGTVDTAETSE 230
|
...
gi 60390566 236 AVL 238
Cdd:COG3845 231 EEL 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-245 |
4.69e-38 |
|
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: 133.29 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQ--ILLDdtdiRQANKAELRKVRHHIGmifqnynLISPlt 95
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFG----ERRGGEDVWELRKRIG-------LVSP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVLHGRLGAKSTVA----GMLGLY---SSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:COG1119 86 ALQLRFPRDETVLDVVLsgffDSIGLYrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV-DDAVLQHIYRQP 245
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEVlTSENLSEAFGLP 243
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-239 |
1.82e-37 |
|
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: 131.49 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAELRkVRHHI 81
Cdd:TIGR03410 1 LEVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-TKLPPHER-ARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLhgrlgaksTVAGMLGLYSSAEKQEALQLLDEvgLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLL--------TGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPkstTIVMDI---LRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVL 238
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQP---SIIKDIgrvIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
.
gi 60390566 239 Q 239
Cdd:TIGR03410 225 R 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
2.17e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 132.29 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSN---KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAElrkv 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RhhiGMIFQNYNLISPLTALENVlhgRLGAKstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:COG4525 78 R---GVVFQKDALLPWLNVLDNV---AFGLR-----LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIA--MAyTDHIV 217
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAlfLA-TRLVV 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-228 |
4.47e-37 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 130.42 E-value: 4.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNL 90
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS---MIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 ISPlTALENVLHGRLGAKSTVAgmlglyssAEKQEALQLLDEV-----GLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:cd03254 89 FSG-TIMENIRLGRPNATDEEV--------IEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVDIaMAYTDHIVGINSGAIVFEG 228
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA--HRLST-IKNADKILVLDDGKIIEEG 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-228 |
6.16e-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: 129.32 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdtdirqaNKAELRKVRHHI 81
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-------GKPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHgrlgakstVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVY--------LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILST-HQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-228 |
7.46e-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: 129.15 E-value: 7.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 5 IQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElRKVrhhiGMI 84
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RPV----SML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 85 FQNYNLISPLTALENVLHGRLGakstvagmlGLYSSAEKQEALQ-LLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQH 163
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSP---------GLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-234 |
8.82e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 8.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRkvRHH 80
Cdd:COG1129 4 LLEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ--AAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKStvagmlGLYS-SAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRG------GLIDwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILIN--LHQVdiaMAYTDHIVGINSGAIVFEGATNEVD 234
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIShrLDEV---FEIADRVTVLRDGRLVGTGPVAELT 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-233 |
9.92e-37 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 130.11 E-value: 9.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnkhsLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqANKAELRKV 77
Cdd:PRK11300 5 LLSVSGLMMRFGG----LLAVNnvnLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTALENVL---HGRLGAkSTVAGMLGL--YSSAEKQ---EALQLLDEVGLKEYAYQRCDQLSGG 149
Cdd:PRK11300 79 RMGVVRTFQHVRLFREMTVIENLLvaqHQQLKT-GLFSGLLKTpaFRRAESEaldRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGA 229
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
....
gi 60390566 230 TNEV 233
Cdd:PRK11300 238 PEEI 241
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-245 |
2.10e-36 |
|
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: 131.08 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 33 IIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnKAELRkvrhHIGMIFQNYNLISPLTALENVLHGrlgakstvA 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-PPHLR----HINMVFQSYALFPHMTVEENVAFG--------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 113 GMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLA 192
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 60390566 193 KEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvddavlqhIYRQP 245
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEE--------IYEEP 192
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-233 |
2.25e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 132.85 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH-IGMIFQNYNLISPLTA 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGrlgakstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:PRK10070 124 LDNTAFG--------MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-236 |
2.83e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 135.76 E-value: 2.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRkvrHHIGMIFQNYNLI 91
Cdd:TIGR03375 475 GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLR---RNIGYVPQDPRLF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPlTALENVLHGRLgakstvagmlglysSAEKQEALQLLDEVGLKEYAYQ-----------RCDQLSGGQQQRVGIARAL 160
Cdd:TIGR03375 552 YG-TLRDNIALGAP--------------YADDEEILRAAELAGVTEFVRRhpdgldmqigeRGRSLSGGQRQAVALARAL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLII------LINLhqvdiamayTDHIVGINSGAIVFEGATNEVD 234
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLvthrtsLLDL---------VDRIIVMDNGRIVADGPKDQVL 687
|
..
gi 60390566 235 DA 236
Cdd:TIGR03375 688 EA 689
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
3.31e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.58 E-value: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAeLRKVRHH 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNY-NLISPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:PRK13636 84 VGMVFQDPdNQLFSASVYQDVSFGAVN--------LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-242 |
4.45e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.04 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD----SGQILLDDTDIRQANKAELRKVR-HHIGM 83
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRRIRgNRIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 84 IFQNynlisPLTALeNVLHgRLGAKstVAGML----GLYSSAEKQEALQLLDEVGLKEyAYQRCD----QLSGGQQQRVG 155
Cdd:COG4172 97 IFQE-----PMTSL-NPLH-TIGKQ--IAEVLrlhrGLSGAAARARALELLERVGIPD-PERRLDayphQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDpksTTI---VMDILRRLAKEKQL-IILI--NLHQV-DIAmaytDHIVGINSGAIVFEG 228
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALD---VTVqaqILDLLKDLQRELGMaLLLIthDLGVVrRFA----DRVAVMRQGEIVEQG 239
|
250
....*....|....
gi 60390566 229 ATNEVDDAvLQHIY 242
Cdd:COG4172 240 PTAELFAA-PQHPY 252
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
4.89e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 134.12 E-value: 4.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR---R 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPlTALENVLHGRLGAkstvagmlglysSAEkqEALQLLDEVGLKEYAYQRCD-----------QLSGG 149
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLARPDA------------TDE--ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKqLIILINLHQVDIAMAytDHIVGINSGAIVFEGA 229
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAGLERM--DRILVLEDGRIVEQGT 552
|
...
gi 60390566 230 TNE 232
Cdd:COG4987 553 HEE 555
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-228 |
8.66e-36 |
|
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: 126.94 E-value: 8.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLI 91
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR---NIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPlTALENVLHGRLGAKST----VAGMLGLYSSAEKQEA-LQLldEVGlkeyayQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:cd03245 91 YG-TLRDNITLGAPLADDErilrAAELAGVTDFVNKHPNgLDL--QIG------ERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVDIaMAYTDHIVGINSGAIVFEG 228
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT--HRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-233 |
2.67e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGSN----KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAE--LRKVRH 79
Cdd:PRK13634 7 KVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGKKNkkLKPLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 80 HIGMIFQnynliSPltalENVLHGRLGAKSTVAGMLGLYSSAE--KQEALQLLDEVGLKEYAYQRCD-QLSGGQQQRVGI 156
Cdd:PRK13634 86 KVGIVFQ-----FP----EHQLFEETVEKDICFGPMNFGVSEEdaKQKAREMIELVGLPEELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-209 |
2.91e-35 |
|
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: 124.46 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAeLRKVRHHIGMIFQNYN--LISPlT 95
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKG-LLERRQRVGLVFQDPDdqLFAA-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVLHGRLGakstvagmLGLySSAEKQ----EALQLldeVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:TIGR01166 86 VDQDVAFGPLN--------LGL-SEAEVErrvrEALTA---VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQVDIA 209
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVV-ISTHDVDLA 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-225 |
3.11e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.54 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVR-HHIGMIFQNYNLISPLTA 96
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRrEHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:PRK10535 104 AQNV--------EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINlHQVDIAmAYTDHIVGINSGAIV 225
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVT-HDPQVA-AQAERVIEIRDGEIV 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-225 |
3.45e-35 |
|
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: 125.06 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHIGMIFQNY 88
Cdd:cd03301 8 KRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 89 NLISPLTALENVLHG---RLGAKSTVagmlglysSAEKQEALQLLdevGLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:cd03301 82 ALYPHMTVYDNIAFGlklRKVPKDEI--------DERVREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIV 225
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-233 |
9.09e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.03 E-value: 9.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIR-----DDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLIS 92
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRR---RVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PLTALENVLHGrLGAKSTVAGMLGLYSSA-EKQEALQLLDEVglKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:PRK14247 96 NLSIFENVALG-LKLNRLVKSKKELQERVrWALEKAQLWDEV--KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEkqLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
5-254 |
1.03e-34 |
|
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: 127.54 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 5 IQLDKTYGSnkHSLKaVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKA-ELRKVRHHIGM 83
Cdd:TIGR02142 3 ARFSKRLGD--FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 84 IFQNYNLISPLTALENVLHGRLGAKstvagmlGLYSSAEKQEALQLLdevGLKEYAYQRCDQLSGGQQQRVGIARALMQH 163
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMKRAR-------PSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV-DDAVLQHIY 242
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVwASPDLPWLA 229
|
250
....*....|..
gi 60390566 243 RqPDQSTAVAAN 254
Cdd:TIGR02142 230 R-EDQGSLIEGV 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-244 |
1.32e-34 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 129.80 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDdSGQILLDDTDIRQANKAELRKVRHHIGMIFQN-YNLISP 93
Cdd:COG4172 299 VKAVDgvsLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFGSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 ltalenvlhgRLgaksTVA-----GML----GLYSSAEKQEALQLLDEVGLKEYAYQRC-DQLSGGQQQRVGIARALMQH 163
Cdd:COG4172 378 ----------RM----TVGqiiaeGLRvhgpGLSAAERRARVAEALEEVGLDPAARHRYpHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 164 PKMILCDEPIASLDpksTTI---VMDILRRLAKEKQL-IILI--NLHQVDiAMAytDHIVGINSGAIVFEGATNEVDDAV 237
Cdd:COG4172 444 PKLLVLDEPTSALD---VSVqaqILDLLRDLQREHGLaYLFIshDLAVVR-ALA--HRVMVMKDGKVVEQGPTEQVFDAP 517
|
....*..
gi 60390566 238 lQHIYRQ 244
Cdd:COG4172 518 -QHPYTR 523
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-233 |
1.68e-34 |
|
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: 123.99 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhsLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHI 81
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLHG---RLGAKSTVagmlglyssaeKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGlkkRKVDKKEI-----------ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-222 |
2.39e-34 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 122.90 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKA---VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI---RQANKAEL 74
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVlnhLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RkvRHHIGMIFQNYNLISPLTALENV---LHGRlgakstvagmlGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQ 151
Cdd:NF038007 81 R--RELIGYIFQSFNLIPHLSIFDNValpLKYR-----------GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDiAMAYTDHIVGINSG 222
Cdd:NF038007 148 QRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVT-HSDE-ASTYGNRIINMKDG 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-225 |
3.19e-34 |
|
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: 122.37 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDtdiRQANKAELRKVrhhIGMIFQN-- 87
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKS---IGYVMQDvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPlTALENVlhgRLGAKSTvagmlglysSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:cd03226 82 YQLFTD-SVREEL---LLGLKEL---------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIV 225
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIT-HDYEFLAKVCDRVLLLANGAIV 205
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-232 |
4.26e-34 |
|
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: 129.05 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 17 SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLISPlTA 96
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRA---RMALVPQDPVLFAA-SV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGRLGAksTVAGMLGLYSSAEKQEALQLLDEvGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:TIGR02204 431 MENIRYGRPDA--TDEEVEAAARAAHAHEFISALPE-GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 177 DPKSTTIVMDILRRLAKEK-QLIILINLHQVDIAmaytDHIVGINSGAIVFEGATNE 232
Cdd:TIGR02204 508 DAESEQLVQQALETLMKGRtTLIIAHRLATVLKA----DRIVVMDQGRIVAQGTHAE 560
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-245 |
4.77e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.22 E-value: 4.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 4 VIQL---DKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnKAELRkvrhH 80
Cdd:PRK09452 14 LVELrgiSKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV-PAENR----H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGrLGAKSTvagmlglySSAEKQ----EALQLldeVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFG-LRMQKT--------PAAEITprvmEALRM---VQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvdda 236
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE---- 231
|
....*....
gi 60390566 237 vlqhIYRQP 245
Cdd:PRK09452 232 ----IYEEP 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-245 |
1.12e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.45 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQankaelRKVRHH-IGMIFQN 87
Cdd:PRK11432 14 KRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPLTALENVLHGrlgakstvAGMLGLYSSAEKQ---EALQLLDEVGLKEyayQRCDQLSGGQQQRVGIARALMQHP 164
Cdd:PRK11432 87 YALFPHMSLGENVGYG--------LKMLGVPKEERKQrvkEALELVDLAGFED---RYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 165 KMILCDEPIASLDPKsttivmdiLRRLAKEK------QLII--LINLHQVDIAMAYTDHIVGINSGAIVFEGATnevdda 236
Cdd:PRK11432 156 KVLLFDEPLSNLDAN--------LRRSMREKirelqqQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP------ 221
|
....*....
gi 60390566 237 vlQHIYRQP 245
Cdd:PRK11432 222 --QELYRQP 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-228 |
1.15e-33 |
|
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: 121.61 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDtdirQANKAELrkVRHHIGMIFQNYNLISPL 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG----QPRKPDQ--FQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENV---LHGRLGAKStvagmlglySSAEKQE--ALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:cd03234 97 TVRETLtytAILRLPRKS---------SDAIRKKrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQlIILINLHQ--VDIaMAYTDHIVGINSGAIVFEG 228
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHQprSDL-FRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-246 |
1.21e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.99 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaeLRKVRHHIGMIFQ 86
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYN--LISPlTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHP 164
Cdd:PRK13652 86 NPDdqIFSP-TVEQDIAFGPIN--------LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEvddavlqhIYRQ 244
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE--------IFLQ 228
|
..
gi 60390566 245 PD 246
Cdd:PRK13652 229 PD 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-209 |
1.84e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.08 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS---LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQ---ANKAEL 74
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKvrHHIGMIFQNYNLISPLTALENVlhgrlgaksTVAGMLGLYSSAEKQE-ALQLLDEVGLKEYAYQRCDQLSGGQQQR 153
Cdd:PRK11629 85 RN--QKLGFIYQFHHLLPDFTALENV---------AMPLLIGKKKPAEINSrALEMLAAVGLEHRANHRPSELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIA 209
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-232 |
6.53e-33 |
|
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: 119.64 E-value: 6.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNynl 90
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR---AIGVVPQD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 iSPL---TALENVLHGRLGAkstvagmlglySSAEKQEAL---QLLDEVGLKEYAYQ-----RCDQLSGGQQQRVGIARA 159
Cdd:cd03253 84 -TVLfndTIGYNIRYGRPDA-----------TDEEVIEAAkaaQIHDKIMRFPDGYDtivgeRGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI-NLHQVDIAmaytDHIVGINSGAIVFEGATNE 232
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAhRLSTIVNA----DKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-233 |
6.74e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 6.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNynlisPl 94
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR---QVGMVFQN-----P- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 talENVLHGrlgakSTVAG--MLGLYSSA----EKQEALQ-LLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:PRK13635 91 ---DNQFVG-----ATVQDdvAFGLENIGvpreEMVERVDqALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
7.50e-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: 125.09 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD---QI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNyNLISPLTALENVLHGRLGAkstvagmlglySSAEKQEALQL--LDEV------GLKEYAYQRCDQLSGGQQQR 153
Cdd:TIGR02857 399 AWVPQH-PFLFAGTIAENIRLARPDA-----------SDAEIREALERagLDEFvaalpqGLDTPIGEGGAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVDIAMAYtDHIV 217
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT--HRLALAALA-DRIV 527
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-232 |
2.36e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYgsnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAelrkvRHH 80
Cdd:PRK10771 1 MLKLTDITWLY---HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENV---LHGrlgakstvagmlGLYSSAEKQEALQ-LLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIglgLNP------------GLKLNAAQREKLHaIARQMGIEDLLARLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-233 |
3.16e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.96 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkAELRKVrhhiGMIF 85
Cdd:PRK10851 7 NIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRKV----GFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 QNYNLISPLTALENVLHGRlgaksTVAGMLGLYSSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHP 164
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGL-----TVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-233 |
3.17e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.58 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:PRK11231 2 TLRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQnyNLISP--LTALENVLHGRlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:PRK11231 78 LALLPQ--HHLTPegITVRELVAYGR----SPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV-LHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-201 |
1.08e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLirDD-------SGQILLDDTDI--RQANKAELRKvrhHI 81
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM--NDlnpevtiTGSIVYNGHNIysPRTDTVDLRK---EI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLIsPLTALENVLHG-RLGAKSTVAGMLGLYSSAEKQEALqlLDEVglKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK14239 89 GMVFQQPNPF-PMSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGASI--WDEV--KDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILI 201
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLV 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-191 |
1.18e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 116.38 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTY------GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDD----TDIRQAN 70
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 71 KAE---LRkvRHHIGMIFQNYNLISPLTALENVlhgrlgAKSTVAgmLGLYSSAEKQEALQLLDEVGLKEyayqRCDQL- 146
Cdd:COG4778 84 PREilaLR--RRTIGYVSQFLRVIPRVSALDVV------AEPLLE--RGVDREEARARARELLARLNLPE----RLWDLp 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 60390566 147 ----SGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRL 191
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
5-230 |
1.44e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 115.73 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 5 IQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHHIGMI 84
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 85 FQNYNLISPLTALENVlhgRLGAKStvagmlGLYSSAEKQEAL-QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQH 163
Cdd:TIGR01277 76 FQENNLFAHLTVRQNI---GLGLHP------GLKLNAEQQEKVvDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGAT 230
Cdd:TIGR01277 147 NPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
2.52e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 116.34 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSN----KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqANKAELRK 76
Cdd:COG1101 1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV--TKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 VRhHIGMIFQNynlisP-------LTALENVL-----HGRLGAKSTVagmlglySSAEK---QEALQLLDeVGLKEYAYQ 141
Cdd:COG1101 79 AK-YIGRVFQD-----PmmgtapsMTIEENLAlayrrGKRRGLRRGL-------TKKRRelfRELLATLG-LGLENRLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 142 RCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI---NLHQvdiAMAYTDHIVG 218
Cdd:COG1101 145 KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMvthNMEQ---ALDYGNRLIM 221
|
....*....
gi 60390566 219 INSGAIVFE 227
Cdd:COG1101 222 MHEGRIILD 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-177 |
2.59e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 115.36 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSSAekqealqlLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA--------LDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170
....*....|....*..
gi 60390566 161 MQHPKMILCDEPIASLD 177
Cdd:PRK10908 153 VNKPAVLLADEPTGNLD 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-234 |
3.04e-31 |
|
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: 115.26 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELrkvrhhigMIFQNYNLISPLTAL 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLhgrLGAKSTVAGMlglySSAEKQEAL-QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:TIGR01184 73 ENIA---LAVDRVLPDL----SKSERRAIVeEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVD 234
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVP 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-232 |
3.06e-31 |
|
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: 115.33 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaeLRKVRHHIGMIFQNYNLISpLTAL 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGAKST----VAGMLGLYSSAEKqealqLLD----EVGlkeyayQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:cd03249 95 ENIRYGKPDATDEeveeAAKKANIHDFIMS-----LPDgydtLVG------ERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQ-LIILINLHQVDIAmaytDHIVGINSGAIVFEGATNE 232
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKGRTtIVIAHRLSTIRNA----DLIAVLQNGQVVEQGTHDE 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-242 |
6.38e-31 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 115.47 E-value: 6.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkVRHHIGMIF 85
Cdd:PRK10253 12 QLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 QNYNLISPLTALENVLHGRLGAKStvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQP----LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE-VDDAVLQHIY 242
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEiVTAELIERIY 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-233 |
2.79e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.48 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHGRLGAKSTVAGMlglySSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTW----TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAA-IHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-209 |
3.41e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.56 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHS---LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAN---KAEL 74
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKvrHHIGMIFQNYNLISPLTALENVlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRV 154
Cdd:PRK10584 86 RA--KHVGFVFQSFMLIPTLNALENV--------ELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 155 GIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIA 209
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-199 |
4.27e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 112.90 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqaNKAELRKVRHHIGMIFQNYNLISPLTAL 97
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLT--GLDEHEIARLGIGRKFQKPTVFEELTVF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:COG4674 104 ENLELALKGDRGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMT 183
|
170 180
....*....|....*....|..
gi 60390566 178 PKSTTIVMDILRRLAKEKQLII 199
Cdd:COG4674 184 DAETERTAELLKSLAGKHSVVV 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-245 |
4.48e-30 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 112.96 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAN-KAELRKVRHhigmIFQNYNLISPLTA 96
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSsKAFARKVAY----LPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGRLGAKstvaGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:PRK10575 103 RELVAIGRYPWH----GALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDA-VLQHIYRQP 245
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGeTLEQIYGIP 248
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-178 |
6.74e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDTDIRQANkAELRkv 77
Cdd:COG4136 1 MLSLENLTITLGG-RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP-AEQR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 rhHIGMIFQNYNLISPLTALENVLhgrLGAKSTVAGmlglysSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:COG4136 77 --RIGILFQDDLLFPHLSVGENLA---FALPPTIGR------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180
....*....|....*....|.
gi 60390566 158 RALMQHPKMILCDEPIASLDP 178
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDA 166
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-224 |
7.52e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.00 E-value: 7.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKH-SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhH 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD---H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPlTALENVlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcdqLSGGQQQRVGIARAL 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI---------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAytDHIVGINSGAI 224
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA--DRILVLEDGRV 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-201 |
1.15e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKV---IQLDKTYGSNKH-SLKAV---NFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAEL 74
Cdd:PRK15079 14 LKVhfdIKDGKQWFWQPPkTLKAVdgvTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKVRHHIGMIFQNynlisPLTALenvlHGRLGAKSTVAGMLGLY----SSAE-KQEALQLLDEVGLKEYAYQRC-DQLSG 148
Cdd:PRK15079 94 RAVRSDIQMIFQD-----PLASL----NPRMTIGEIIAEPLRTYhpklSRQEvKDRVKAMMLKVGLLPNLINRYpHEFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 60390566 149 GQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILI 201
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLsLIFI 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-235 |
1.33e-29 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 110.95 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdtdirqaNKAELRKVRHHI 81
Cdd:TIGR03740 1 LETKNLSKRFG-KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFD-------GHPWTRKDLHKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLhgrlgaksTVAGMLGLyssaEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLK--------VHTTLLGL----PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSEN 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-225 |
1.58e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.67 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRkvRHHI 81
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR--RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFqnynlispltalenvlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcdQLSGGQQQRVGIARALM 161
Cdd:cd03216 78 AMVY-----------------------------------------------------------QLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIV 225
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFIS-HRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-228 |
1.61e-29 |
|
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: 109.56 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSI-NQLIR-DDSGQILLDDTDIRqankaeLRKVRHHIGMIFQ 86
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGlGVSGEVLINGRPLD------KRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 nynlispltalENVLHGRLgaksTVagmlglyssaekQEALQlldevglkeYAYQrCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:cd03213 90 -----------DDILHPTL----TV------------RETLM---------FAAK-LRGLSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAYT-DHIVGINSGAIVFEG 228
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICS-IHQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-245 |
1.74e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYgSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRHH 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHG-------RLGAKSTVAGMLGLyssaekqealqlldeVGLKEYAYQRCDQLSGGQQQR 153
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGlkqdklpKAEIASRVNEMLGL---------------VHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPK----STTIVMDILRRLAkekqLIILINLHQVDIAMAYTDHIVGINSGAIVFEGA 229
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250
....*....|....*.
gi 60390566 230 TNEvddavlqhIYRQP 245
Cdd:PRK11607 234 PEE--------IYEHP 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-233 |
3.09e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 8 DKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaELRKVRHHIGMIFQN 87
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLWDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 Y-NLISPLTALENVLHGrlgakstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PRK13633 94 PdNQIVATIVEEDVAFG--------PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-224 |
4.25e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 110.15 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILlddtdirqANKAELRKVRHHIGMIFQ 86
Cdd:PRK11247 18 VSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISPLTALENVlhgrlgakstvagMLGLySSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PRK11247 89 DARLLPWKKVIDNV-------------GLGL-KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 167 ILCDEPIASLDpKSTTIVM-DILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAI 224
Cdd:PRK11247 155 LLLDEPLGALD-ALTRIEMqDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
6.50e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.21 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS---KV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYN-LISPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK13647 82 GLVFQDPDdQVFSSTVWDDVAFGPVN--------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQVDIAMAYTDHIVGINSGAIVFEGA 229
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVI-VATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-233 |
7.39e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.85 E-value: 7.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIFQNYNLISPLTALENV 100
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 101 L-----HGRLGA---KSTVagmlglyssaekqeaLQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEP 172
Cdd:PRK11831 106 AyplreHTQLPApllHSTV---------------MMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 173 IASLDPksttIVMDILRRLAKEKQ----LIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK11831 171 FVGQDP----ITMGVLVKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-239 |
1.06e-28 |
|
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: 113.69 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLI 91
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR---HIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 sPLTALENVlhGRLG----------AKstVAGM----LGL---YSSaekqealqLLDEVGLkeyayqrcdQLSGGQQQRV 154
Cdd:COG4618 419 -DGTIAENI--ARFGdadpekvvaaAK--LAGVhemiLRLpdgYDT--------RIGEGGA---------RLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 155 GIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIaMAYTDHIVGINSGAIVFEGATNEVD 234
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVIT-HRPSL-LAAVDKLLVLRDGRVQAFGPRDEVL 554
|
....*
gi 60390566 235 DAVLQ 239
Cdd:COG4618 555 ARLAR 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-236 |
1.76e-28 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 113.27 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaeLRKVRHHIGMIF 85
Cdd:TIGR02203 336 VTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 QNYNLISPlTALENVLHGRLGAkstvagmlglYSSAEKQEALQ---LLDEV-----GLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:TIGR02203 413 QDVVLFND-TIANNIAYGRTEQ----------ADRAEIERALAaayAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQ-LIILINLHQVDIAmaytDHIVGINSGAIVFEGATNEVDDA 236
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTtLVIAHRLSTIEKA----DRIVVMDDGRIVERGTHNELLAR 557
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-233 |
2.03e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQaNKAELRKVRHHIGMIFQ--NYNLIS 92
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 pltalENVlhgrlgAKSTVAGM--LGLYSSAEKQEALQLLDEVGLK--EYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:PRK13637 99 -----ETI------EKDIAFGPinLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-232 |
2.34e-28 |
|
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: 107.70 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLISPlTAL 97
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR---QIGLVSQDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGakstvAGMLGLYSSAEKQEALQLLDEV--GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIAS 175
Cdd:cd03251 94 ENIAYGRPG-----ATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 176 LDPKSTTIVMDILRRLAKEKQLIILInlHQVD-IAMAytDHIVGINSGAIVFEGATNE 232
Cdd:cd03251 169 LDTESERLVQAALERLMKNRTTFVIA--HRLStIENA--DRIVVLEDGKIVERGTHEE 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-245 |
3.16e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.02 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQI------------------LLDDTDIRQANKAELRKV-- 77
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTRFKKIKKIke 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 -RHHIGMIFQ--NYNLISPlTALENVLhgrLGAKStvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCD-QLSGGQQQR 153
Cdd:PRK13651 103 iRRRVGVVFQfaEYQLFEQ-TIEKDII---FGPVS-----MGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVT-HDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
250
....*....|....
gi 60390566 234 --DDAVLQHIYRQP 245
Cdd:PRK13651 253 lsDNKFLIENNMEP 266
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-244 |
3.26e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.09 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDD-----TDIRQANKAELR 75
Cdd:PRK11701 6 LLSVRGLTKLYG-PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KV-RHHIGMIFQN------------YNLISPLTALENVLHGRLgakstvagmlglyssaeKQEALQLLDEVglkEYAYQR 142
Cdd:PRK11701 85 RLlRTEWGFVHQHprdglrmqvsagGNIGERLMAVGARHYGDI-----------------RATAGDWLERV---EIDAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 143 CDQL----SGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVG 218
Cdd:PRK11701 145 IDDLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260
....*....|....*....|....*..
gi 60390566 219 INSGAIVFEGATNEV-DDAvlQHIYRQ 244
Cdd:PRK11701 225 MKQGRVVESGLTDQVlDDP--QHPYTQ 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-233 |
9.41e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 9.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD-----SGQILLDDTDIRQANKAELRk 76
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 VRHHIGMIFQNYNLISPLTALENV-----LHGRLGAKSTVAGMLglySSAEKQEALqlLDEVG--LKEYAyqrcDQLSGG 149
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVaigvkLNGLVKSKKELDERV---EWALKKAAL--WDEVKdrLNDYP----SNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEkqLIILINLHQVDIAMAYTDHIVGINSGAIVFEGA 229
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
....
gi 60390566 230 TNEV 233
Cdd:PRK14267 232 TRKV 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-205 |
1.35e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.40 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQL------IRDDsGQILLDDTDIrQANKAELR 75
Cdd:PRK14243 11 LRTENLNVYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNL-YAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KVRHHIGMIFQNYNLIsPLTALENVLHGrlgakSTVAGMLG----LYSSAEKQEALqlLDEVglKEYAYQRCDQLSGGQQ 151
Cdd:PRK14243 88 EVRRRIGMVFQKPNPF-PKSIYDNIAYG-----ARINGYKGdmdeLVERSLRQAAL--WDEV--KDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILI--NLHQ 205
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVthNMQQ 212
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-244 |
2.88e-27 |
|
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: 105.30 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTD-----IRQANKAELR 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KV-RHHIGMIFQNynlisPLTALENVLH--GRLGAKSTVAGMLglYSSAEKQEALQLLDEVglkEYAYQRCD----QLSG 148
Cdd:TIGR02323 82 RLmRTEWGFVHQN-----PRDGLRMRVSagANIGERLMAIGAR--HYGNIRATAQDWLEEV---EIDPTRIDdlprAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 149 GQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250
....*....|....*..
gi 60390566 229 ATNEV-DDAvlQHIYRQ 244
Cdd:TIGR02323 232 LTDQVlDDP--QHPYTQ 246
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
3.33e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrQANKAELrkvrhh 80
Cdd:PRK11248 1 MLQISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 iGMIFQNYNLISPLTALENVLHG-RLGakstvagmlGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGlQLA---------GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 60390566 160 LMQHPKMILCDEPIASLDP----KSTTIVMDILRRLAKEKQLI 198
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQVLLI 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-233 |
3.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 17 SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNynlisPlta 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK---HIGIVFQN-----P--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 lENVLHGRLgAKSTVAgmLGLYSSAEKQEAL-----QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:PRK13648 93 -DNQFVGSI-VKYDVA--FGLENHAVPYDEMhrrvsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAyTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-233 |
6.39e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANK-AELRKVRHHIGMIFQnynliSPLTAL-- 97
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIRKKVGLVFQ-----FPESQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLhgrlgaKSTVAGMLGLYSSAEKQEALQL--LDEVGLKEYAYQRCD-QLSGGQQQRVGIARALMQHPKMILCDEPIA 174
Cdd:PRK13649 101 ETVL------KDVAFGPQNFGVSQEEAEALARekLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 175 SLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVT-HLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-233 |
9.84e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.35 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDS-----GQILLDDTDIRQaNKAELRK 76
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 VRHHIGMIFQNYNLIsPLTALENVLHGR--LGAKSTVAgMLGLYSSAEKqeALQLLDEVglKEYAYQRCDQLSGGQQQRV 154
Cdd:PRK14258 86 LRRQVSMVHPKPNLF-PMSVYDNVAYGVkiVGWRPKLE-IDDIVESALK--DADLWDEI--KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 155 GIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI---NLHQVDIAMAYTDHIVGINS--GAIVFEGA 229
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIvshNLHQVSRLSDFTAFFKGNENriGQLVEFGL 239
|
....
gi 60390566 230 TNEV 233
Cdd:PRK14258 240 TKKI 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-228 |
1.22e-26 |
|
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: 107.98 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNynl 90
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA---AIGIVPQD--- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 isplTAL------ENVLHGRLGAkstvagmlglySSAEKQEALQL--LD---------------EVGLKeyayqrcdqLS 147
Cdd:COG5265 441 ----TVLfndtiaYNIAYGRPDA-----------SEEEVEAAARAaqIHdfieslpdgydtrvgERGLK---------LS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlinlhqvdIA-----MAYTDHIVGINSG 222
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV--------IAhrlstIVDADEILVLEAG 568
|
....*.
gi 60390566 223 AIVFEG 228
Cdd:COG5265 569 RIVERG 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-233 |
1.94e-26 |
|
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: 107.20 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTT---ILRSINQLiRDDSGQIL------------------ 60
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQY-EPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 61 ------------LDDTDIRQANKAELRKVRHHIGMIFQ-NYNLISPLTALENVLHG--RLGakstvagmlglYSSAEK-Q 124
Cdd:TIGR03269 79 gepcpvcggtlePEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEAleEIG-----------YEGKEAvG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 125 EALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLH 204
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
250 260
....*....|....*....|....*....
gi 60390566 205 QVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-233 |
2.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK----HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANK-AELR 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 KVRHHIGMIFQ-NYNLISPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGL-KEYAYQRCDQLSGGQQQR 153
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQN--------FGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVT-HLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-233 |
3.69e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANK-AELRKVRHHIGMIFQnynliSP 93
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRPVRKRIGMVFQ-----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTAL--ENVLHGRL-GAKStvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCD-QLSGGQQQRVGIARALMQHPKMILC 169
Cdd:PRK13646 95 ESQLfeDTVEREIIfGPKN-----FKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-177 |
4.02e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTIlrsINQLIR---DDSGQILLDDTDIRQANKAELrkvRHHIGMIFQN 87
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPlTALENVLHGRLGAksTVAGMlglYSSAEKQEALQLLD--EVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:PRK13657 418 AGLFNR-SIEDNIRVGRPDA--TDEEM---RAAAERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170
....*....|..
gi 60390566 166 MILCDEPIASLD 177
Cdd:PRK13657 492 ILILDEATSALD 503
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-228 |
4.03e-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: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAelrkVRHH 80
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPlTALENVlhGRlgakstvagmlglyssaekqealqlldevglkeyayqrcdQLSGGQQQRVGIARAL 160
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNNL--GR----------------------------------------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQVdiAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIW-ITHHLT--GIEHMDKILFLENGKIIMQG 178
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-233 |
4.14e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.61 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNK--------HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkae 73
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 74 lRKVR-HHIGMIFQNynlisPLTALEnvlhgrlgAKSTVAGMLGL-------YSSAEKQEAL-QLLDEVGL-KEYAYQRC 143
Cdd:COG4167 82 -YKYRcKHIRMIFQD-----PNTSLN--------PRLNIGQILEEplrlntdLTAEEREERIfATLRLVGLlPEHANFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 144 DQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQL-IILINlHQVDIAMAYTDHIVGINSG 222
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsYIYVS-QHLGIVKHISDKVLVMHQG 226
|
250
....*....|.
gi 60390566 223 AIVFEGATNEV 233
Cdd:COG4167 227 EVVEYGKTAEV 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-177 |
4.55e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY------GSNKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKA 72
Cdd:PRK11308 6 LQAIDLKKHYpvkrglFKPERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 73 ELRKVRHHIGMIFQN-YNLISPLTALENVLHGRLGAKSTVagmlglySSAEKQE-ALQLLDEVGLKEYAYQRCDQL-SGG 149
Cdd:PRK11308 86 AQKLLRQKIQIVFQNpYGSLNPRKKVGQILEEPLLINTSL-------SAAERREkALAMMAKVGLRPEHYDRYPHMfSGG 158
|
170 180
....*....|....*....|....*...
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-236 |
7.48e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 101.41 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNyNLISPLTAL 97
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---QVGVVLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGAksTVAGMLGLYSSAEKQEALQLLDEvGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:cd03252 94 DNIALADPGM--SMERVIEAAKLAGAHDFISELPE-GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 178 PKSTTIVMDILRRLAKEKQLIILInlHQVDIAMAyTDHIVGINSGAIVFEGATNEVDDA 236
Cdd:cd03252 171 YESEHAIMRNMHDICAGRTVIIIA--HRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-205 |
1.29e-25 |
|
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: 99.74 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqankAELRKVRH-HIGMIFQNYNLISPLTA 96
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHeNILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENvLHgrlgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:TIGR01189 91 LEN-LH-----------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 60390566 177 DPKSTTIVMDILRRLAkEKQLIILINLHQ 205
Cdd:TIGR01189 159 DKAGVALLAGLLRAHL-ARGGIVLLTTHQ 186
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-179 |
1.40e-25 |
|
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: 104.75 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVrhhIGMIFQNYNL 90
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 ISPlTALENVLHGRlgakstvagmlglySSAEKQEALQLLDEVGLKEYAYQRCD-----------QLSGGQQQRVGIARA 159
Cdd:TIGR02868 421 FDT-TVRENLRLAR--------------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180
....*....|....*....|
gi 60390566 160 LMQHPKMILCDEPIASLDPK 179
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAE 505
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-233 |
1.58e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI--RQANKAeLRKVRHHIGMIFQ-NYNLI 91
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpETGNKN-LKKLRKKVSLVFQfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCD-QLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:PRK13641 99 FENTVLKDVEFGPKN--------FGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT-HNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-245 |
1.98e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.74 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDTdirqanKAELRKVRHHIGMIFQNYNLI 91
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM------PIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENVL---HGRLGAKstvagmlglYSSAEKQEAL-QLLDEVGLKEYAYQRCDQ------LSGGQQQRVGIARALM 161
Cdd:TIGR00955 112 PTLTVREHLMfqaHLRMPRR---------VTKKEKRERVdEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAkEKQLIILINLHQ--VDIaMAYTDHIVGINSGAIVFEGATNEVDDAVLQ 239
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpsSEL-FELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
....*.
gi 60390566 240 HIYRQP 245
Cdd:TIGR00955 261 LGHPCP 266
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-244 |
2.63e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 14 NKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDdSGQILLDDTDIRQANKAELRKVRHHIGMIFQNYNlisp 93
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPN---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 ltaleNVLHGRLGAKSTVAGMLGLYS---SAEKQEA--LQLLDEVGLKEYAYQRC-DQLSGGQQQRVGIARALMQHPKMI 167
Cdd:PRK15134 373 -----SSLNPRLNVLQIIEEGLRVHQptlSAAQREQqvIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVLQHIYRQ 244
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-237 |
3.04e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.71 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 16 HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQ---ANKAELrkvrhHIGMIFQNYNLIS 92
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhKLAAQL-----GIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PLTALENVLHGRLGAKStVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEP 172
Cdd:PRK09700 94 ELTVLENLYIGRHLTKK-VCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 173 IASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV--DDAV 237
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYIS-HKLAEIRRICDRYTVMKDGSSVCSGMVSDVsnDDIV 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-233 |
3.57e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.85 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 17 SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKA--ELRKVRHHIGMIFQ--NYNLIS 92
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PlTALENVLHGRLGakstvagmLGlyssAEKQEAL----QLLDEVGL-KEYAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:PRK13645 106 E-TIEKDIAFGPVN--------LG----ENKQEAYkkvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-224 |
4.92e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELrkvRHHIGMIFQNY-NLI 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI---RHKIGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENVLHGrLGAKstvagmlGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:PRK13650 95 VGATVEDDVAFG-LENK-------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDiAMAYTDHIVGINSGAI 224
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-233 |
1.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDS---GQILLDDTDIRQANKAElrkVRHHIGMIFQNY- 88
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWD---IREKVGIVFQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 89 NLISPLTALENVLHGRLGAKSTVAGMLGLYSsaekqealQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:PRK13640 95 NQFVGATVGDDVAFGLENRAVPRPEMIKIVR--------DVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-254 |
1.78e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKaeLRKVRHH 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNynlisPltalENVLHGRLGAKSTVAG--MLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIAR 158
Cdd:PRK13644 79 VGIVFQN-----P----ETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 159 ALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQVDIAmaytDHIVGINSGAIVFEGATNEV-DD 235
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYIthNLEELHDA----DRIIVMDRGKIVLEGEPENVlSD 225
|
250
....*....|....*....
gi 60390566 236 AVLQHIYRQPDQSTAVAAN 254
Cdd:PRK13644 226 VSLQTLGLTPPSLIELAEN 244
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-225 |
1.96e-24 |
|
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: 97.18 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqaNKAELRKVRHHIGMIFQNYNLISPlTAL 97
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLRSRISIIPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVlhgrlgakstvaGMLGLYSSAEKQEALQlldEVGLKEYAYQRCDQL-----------SGGQQQRVGIARALMQHPKM 166
Cdd:cd03244 96 SNL------------DPFGEYSDEELWQALE---RVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQlIILINlHQVDIAMAYtDHIVGINSGAIV 225
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCT-VLTIA-HRLDTIIDS-DRILVLDKGRVV 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-241 |
3.15e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.75 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSN-KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrh 79
Cdd:PRK13632 7 MIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 80 HIGMIFQNY-NLISPLTA-------LENVLHGRLGAKSTVagmlglYSSAEKqealqlldeVGLKEYAYQRCDQLSGGQQ 151
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVeddiafgLENKKVPPKKMKDII------DDLAKK---------VGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAyTDHIVGINSGAIVFEGATN 231
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
250
....*....|..
gi 60390566 232 EV--DDAVLQHI 241
Cdd:PRK13632 228 EIlnNKEILEKA 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-236 |
3.75e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaelRKVRHHI 81
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVL-HGRlgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLvFGR---------YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRL-AKEKQliILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDA 236
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKT--ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-235 |
3.80e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQI-LLDDTDIRQAnkaelRKVRHHIGMIFQN 87
Cdd:PRK13536 49 KSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARA-----RLARARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 YNLISPLTALENVL-HGRLgakstvAGMlglysSAEKQEAL--QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHP 164
Cdd:PRK13536 123 DNLDLEFTVRENLLvFGRY------FGM-----STREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRR-LAKEKQliILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSlLARGKT--ILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-233 |
4.98e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIR-DDS-----GQILLDDTDIRQANKAELRKvrhHIGMI 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSkikvdGKVLYFGKDIFQIDAIKLRK---EVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 85 FQNYNLISPLTALENVlhgrlgakstvAGMLGLYSSAEKQEALQLLDE----VGLKEYAYQRCD----QLSGGQQQRVGI 156
Cdd:PRK14246 96 FQQPNPFPHLSIYDNI-----------AYPLKSHGIKEKREIKKIVEEclrkVGLWKEVYDRLNspasQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEkqLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
5.15e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.00 E-value: 5.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNK-HSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI-------RQA 69
Cdd:PRK13631 21 ILRVKNLYCVFDEKQeNELVALNnisYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 70 NKAELRKV------RHHIGMIFQ--NYNLISPlTALENVLHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQ 141
Cdd:PRK13631 101 TNPYSKKIknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVA--------LGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 142 RCD-QLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGIN 220
Cdd:PRK13631 172 RSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVIT-HTMEHVLEVADEVIVMD 250
|
250 260
....*....|....*....|..
gi 60390566 221 SGAIVFEGATNEV--DDAVLQH 240
Cdd:PRK13631 251 KGKILKTGTPYEIftDQHIINS 272
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-252 |
6.05e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkvrHH 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVLHgrlGAKstVAGMlglySSAEK----QEALQLLdevGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAY---GLK--IRGM----PKAEIeervAEAARIL---ELEPLLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKsTTIVMDI-LRRLAKEKQLIILINLH-QVDiAMAYTDHIVGINSGAIVFEGATNEVd 234
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAK-LRVQMRLeIQRLHRRLKTTSLYVTHdQVE-AMTLADRVVVMNGGVAEQIGTPVEV- 222
|
250
....*....|....*...
gi 60390566 235 davlqhiYRQPdQSTAVA 252
Cdd:PRK11650 223 -------YEKP-ASTFVA 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-232 |
8.07e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILrsiNQLI-----RddsGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLIS 92
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLgflpyQ---GSLKINGIELRELDPESWRK---HLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PlTALENVLHGRlgakstvagmlglySSAEKQEALQLLDEVGLKEY--------AYQRCDQ---LSGGQQQRVGIARALM 161
Cdd:PRK11174 437 G-TLRDNVLLGN--------------PDASDEQLQQALENAWVSEFlpllpqglDTPIGDQaagLSVGQAQRLALARALL 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRlAKEKQLIILINlHQVDIAMAYtDHIVGINSGAIVFEGATNE 232
Cdd:PRK11174 502 QPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVT-HQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-243 |
2.33e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.91 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDdSGQILLDDTDIRQANKAELRKVRhhiGMIFQNynlISPLTAL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHR---AYLSQQ---QSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 EnVLHgrlgakstvagMLGLYSSAE------KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQ-------HP 164
Cdd:COG4138 85 P-VFQ-----------YLALHQPAGasseavEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAkEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV-DDAVLQHIYR 243
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVmTPENLSEVFG 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-217 |
2.34e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGqillddtdirqankaELRKVRH-HIGMIFQNYNLIS--PL 94
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGaRVAYVPQRSEVPDslPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVLHGRLGAKstvaGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIA 174
Cdd:NF040873 73 TVRDLVAMGRWARR----GLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 60390566 175 SLDPKSTTIVMDILRRLAKEKQLIILInLHQVDIAMAyTDHIV 217
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVV-THDLELVRR-ADPCV 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-233 |
2.45e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKvIQLDKTYGSnkHSLKaVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDT---DIRQanKAELRKV 77
Cdd:PRK11144 1 MLE-LNFKQQLGD--LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNynlispltalenvlhGRLGAKSTVAGMLgLYSSAEKQEAL-----QLLD-EVGLKEYAYQrcdqLSGGQQ 151
Cdd:PRK11144 75 KRRIGYVFQD---------------ARLFPHYKVRGNL-RYGMAKSMVAQfdkivALLGiEPLLDRYPGS----LSGGEK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATN 231
Cdd:PRK11144 135 QRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
..
gi 60390566 232 EV 233
Cdd:PRK11144 215 EV 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-233 |
2.49e-23 |
|
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: 98.19 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLI 91
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK---HIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 sPLTALENVlhGRLGAKSTVAGMLGLYSSAEKQEALQLLdEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:TIGR01842 405 -PGTVAENI--ARFGENADPEKIIEAAKLAGVHELILRL-PDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDiAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVIT-HRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-233 |
2.67e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.55 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 30 VTAIIGPSGAGKTTILRSINQLirDD-------SGQILLDDTDIrqANKAELRKVRHHIGMIFQNYNLIsPLTALENVLH 102
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRM--NDkvsgyrySGDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF-PMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 103 GRLGAKstvagmlgLYSSAEKQEALQL-LDEVGLKEYAYQRCD----QLSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:PRK14271 124 GVRAHK--------LVPRKEFRGVAQArLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 178 PKSTTIVMDILRRLAkeKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK14271 196 PTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-233 |
4.19e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrKVRHHI 81
Cdd:PRK10895 4 LTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNLISPLTALENVLhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLM-------AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-228 |
5.31e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.49 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQnynlis 92
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR---QVALVGQ------ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 pltalENVLHGRlGAKSTVAGMLGLYSSAEKQEALQLL---DEVGLKEYAY-----QRCDQLSGGQQQRVGIARALMQHP 164
Cdd:TIGR00958 563 -----EPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAAnahDFIMEFPNGYdtevgEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDiLRRLAKEKQLIILINLHQVDIAmaytDHIVGINSGAIVFEG 228
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQE-SRSRASRTVLLIAHRLSTVERA----DQILVLKKGSVVEMG 695
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-224 |
8.34e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 92.92 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVrhhIGMIFQNYNLISPlTAL 97
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK---VSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGrLGAKSTVAGMlglySSAEKQEALQLLDEV--GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIAS 175
Cdd:cd03248 106 DNIAYG-LQSCSFECVK----EAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 60390566 176 LDPKSTTIVMDILRRlAKEKQLIILINLHQVDIAMAytDHIVGINSGAI 224
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERA--DQILVLDGGRI 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-207 |
8.95e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrKVRHHIGMIFQNYNLISPLTAL 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGAKstvAGMLGlySSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:PRK11288 98 ENLYLGQLPHK---GGIVN--RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|
gi 60390566 178 PKSTTIVMDILRRLAKEKQLIILINlHQVD 207
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVS-HRME 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-232 |
1.13e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIFQNynliSPltal 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQD----SI---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhGRLGAKSTVAG--------MLGLYSSAEKQEALQLLDEVGLK-EYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:PRK10419 100 -----SAVNPRKTVREiireplrhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-244 |
1.15e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.32 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTY--------GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDtdiRQANKA 72
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 73 ELRKVRHHIGMIFQNynlisPLTALENvlHGRLGAKSTVAGML--GLYSSAEKQEALQLLDEVGLK-EYAYQRCDQLSGG 149
Cdd:PRK15112 81 DYSYRSQRIRMIFQD-----PSTSLNP--RQRISQILDFPLRLntDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 150 QQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLaKEKQLIILINLHQVDIAMAY-TDHIVGINSGAIVFEG 228
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
250
....*....|....*.
gi 60390566 229 ATNEVDDAVLQHIYRQ 244
Cdd:PRK15112 233 STADVLASPLHELTKR 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
3.47e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILrsinQLI-RD---DSGQILLDDTDIRQANKAELRK 76
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLtRAwdpQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 77 V------RHHI--GMIFQNYNLISPlTALENVLhgrlgakSTVAGMLGLYSSAEKQEALQL-LDEVGlkeyayqRcdQLS 147
Cdd:PRK11160 415 AisvvsqRVHLfsATLRDNLLLAAP-NASDEAL-------IEVLQQVGLEKLLEDDKGLNAwLGEGG-------R--QLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVdIAMAYTDHIVGINSGAIVFE 227
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT--HRL-TGLEQFDRICVMDNGQIIEQ 554
|
.
gi 60390566 228 G 228
Cdd:PRK11160 555 G 555
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-237 |
3.64e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAelRKVRHH 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVlhgrlgakstvaGMLGLYssAEKQEALQLLDEV-----GLKEYAYQRCDQLSGGQQQRVG 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENL------------AMGGFF--AERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQvdiAMAYTDHIVGINSGAIVFE--GATN 231
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVeqNANQ---ALKLADRGYVLENGHVVLEdtGDAL 224
|
....*.
gi 60390566 232 EVDDAV 237
Cdd:PRK11614 225 LANEAV 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-224 |
4.05e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKHSlKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDT---DIRQANKAelrkvrhhIGMIF 85
Cdd:PRK11000 11 KAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG--------VGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 QNYNLISPLTALENVLHGrlgakstvagmLGLySSAEKQEALQLLDEVG----LKEYAYQRCDQLSGGQQQRVGIARALM 161
Cdd:PRK11000 82 QSYALYPHLSVAENMSFG-----------LKL-AGAKKEEINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 162 QHPKMILCDEPIASLDpKSTTIVMDI-LRRLAKE-KQLIILINLHQVDiAMAYTDHIVGINSGAI 224
Cdd:PRK11000 150 AEPSVFLLDEPLSNLD-AALRVQMRIeISRLHKRlGRTMIYVTHDQVE-AMTLADKIVVLDAGRV 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-208 |
5.08e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRD--DSGQILLDDTDIrqankaelrkvrhhigmiFQNYNLIs 92
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDVPDNQF------------------GREASLI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 pltalENVlhGRLGAKStvagmlglyssaekqEALQLLDEVGLKE-YAYQRC-DQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:COG2401 104 -----DAI--GRKGDFK---------------DAVELLNAVGLSDaVLWLRRfKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDI 208
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-244 |
1.89e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD-----SGQILLDDTDIRQANKAELRKVR-HHIGMIFQNYNL-ISP 93
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPMVsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTALENVLHGRLgakSTVAGMLGlysSAEKQEALQLLDEVGLKEYAYQRCD---QLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:PRK15134 108 LHTLEKQLYEVL---SLHRGMRR---EAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVlQHIYRQ 244
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP-THPYTQ 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-222 |
2.09e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIR--DDSGQILLDDTDIRQANKAELRkvRHHIGMIFQ 86
Cdd:PRK13549 13 KTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTE--RAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISPLTALENVLhgrLGAKSTVAGML---GLYSSAEKqealqLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQH 163
Cdd:PRK13549 90 ELALVKELSVLENIF---LGNEITPGGIMdydAMYLRAQK-----LLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSG 222
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYIS-HKLNEVKAISDTICVIRDG 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-205 |
2.38e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.32 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 20 AVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRK---VRHHIGmifqnynlISP-LT 95
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLGHQPG--------IKTeLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENV-----LHGRLGAkstvagmlglyssaekQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:PRK13538 91 ALENLrfyqrLHGPGDD----------------EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 60390566 171 EPIASLDPKSttiVMDILRRLAK--EKQLIILINLHQ 205
Cdd:PRK13538 155 EPFTAIDKQG---VARLEALLAQhaEQGGMVILTTHQ 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-227 |
2.83e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 16 HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIFQN-------- 87
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyasldpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 ----YNLISPLTaLENVLHGRlGAKSTVAgmlglyssaekqealQLLDEVGLK-EYAYQRCDQLSGGQQQRVGIARALMQ 162
Cdd:PRK10261 418 qtvgDSIMEPLR-VHGLLPGK-AAAARVA---------------WLLERVGLLpEHAWRYPHEFSGGQRQRICIARALAL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 163 HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQV--------DIAMAYTDHIVGINSGAIVFE 227
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMavverishRVAVMYLGQIVEIGPRRAVFE 553
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-233 |
5.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNynlis 92
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR---KIGMVFQN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 pltaLENVLHGRLGAKSTVAGMLGlySSAEKQEALQLLDE----VGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:PRK13642 90 ----PDNQFVGATVEDDVAFGMEN--QGIPREEMIKRVDEallaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAmAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-245 |
1.44e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.01 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDTDIRQANKAEL 74
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNdlnFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 75 RKVR-HHIGMIFQNynlisPLTALENVLhgRLGAKSTVAGML--GLYSSAEKQEALQLLDEVGLKEyAYQRCD----QLS 147
Cdd:PRK09473 92 NKLRaEQISMIFQD-----PMTSLNPYM--RVGEQLMEVLMLhkGMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKE-KQLIILINlHQVDIAMAYTDHIVginsgaIVF 226
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMIT-HDLGVVAGICDKVL------VMY 236
|
250
....*....|....*....
gi 60390566 227 EGATNEVDDAvlQHIYRQP 245
Cdd:PRK09473 237 AGRTMEYGNA--RDVFYQP 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-244 |
1.54e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 88.65 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLI----RDDSGQILLDDTDIRQANKAE 73
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 74 LRK-VRHHIGMIFQNynlisPLTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAyQRCD----QLSG 148
Cdd:PRK11022 83 RRNlVGAEVAMIFQD-----PMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPA-SRLDvyphQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 149 GQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
250
....*....|....*.
gi 60390566 229 ATNEVDDAVLqHIYRQ 244
Cdd:PRK11022 237 KAHDIFRAPR-HPYTQ 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-233 |
1.66e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 90.25 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGS-NKHSLKAVN---FTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQI-------LLDDTDIRQA 69
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 70 NKAelrKVRHHIGMIFQNYNLISPLTALENVlhgrlgaksTVAGMLGLYSSAEKQEALQLLDEVGLKE-YAY----QRCD 144
Cdd:TIGR03269 359 GRG---RAKRYIGILHQEYDLYPHRTVLDNL---------TEAIGLELPDELARMKAVITLKMVGFDEeKAEeildKYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 145 QLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAI 224
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*....
gi 60390566 225 VFEGATNEV 233
Cdd:TIGR03269 507 VKIGDPEEI 515
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-200 |
1.73e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.01 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQAnKAELRKVRHHIGmiFQNyNLISPLTAL 97
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLG--HAP-GIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENV-LHGRLGAKSTVagmlglyssaekqeaLQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:cd03231 92 ENLrFWHADHSDEQV---------------EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIIL 200
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVL 180
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-233 |
1.73e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAeLRKVRHHIGMIFQNYNlispltal 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRG-LLALRQQVATVFQDPE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLgaKSTVAGMLGLYSSAEKQ------EALQLLDEVGLKEYAYQrCdqLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:PRK13638 88 QQIFYTDI--DSDIAFSLRNLGVPEAEitrrvdEALTLVDAQHFRHQPIQ-C--LSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-230 |
3.71e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELrkvrhhI 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYNL--ISPLTALENVLHGRLGAkstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:PRK15056 81 AYVPQSEEVdwSFPVLVEDVVMMGRYGH----MGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQlIILINLHQVDIAMAYTDHIVGINsGAIVFEGAT 230
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPT 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-232 |
4.25e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqanKAELRKVRHHIGMIFQNY 88
Cdd:PRK11176 350 TYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 89 NLISPLTAlENVLHGRLGAkstvagmlglYSSAEKQEALQL---LD-----EVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK11176 427 HLFNDTIA-NNIAYARTEQ----------YSREQIEEAARMayaMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 161 MQH-PKMILcDEPIASLDPKSTTIVMDILRRLAKEKQ-LIILINLHQVDIAmaytDHIVGINSGAIVFEGATNE 232
Cdd:PRK11176 496 LRDsPILIL-DEATSALDTESERAIQAALDELQKNRTsLVIAHRLSTIEKA----DEILVVEDGEIVERGTHAE 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-207 |
8.57e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNLISPlTAL 97
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVLHGRLGAKSTVagmlglyssaEKQEALQLLDEVGLKEYAYQ-RCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:PRK10247 99 DNLIFPWQIRNQQP----------DPAIFLDDLERFALPDTILTkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|.
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINLHQVD 207
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-172 |
1.43e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 4 VIQLDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdTDIRqankaelrkvrhhIGM 83
Cdd:COG0488 1 LENLSKSFGG-RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-------------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 84 IFQNYNLISPLTALENVLHGRLGAKSTVAGMLGLYSS-----------AEKQEAL-------------QLLDEVGLK-EY 138
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKlaepdedlerlAELQEEFealggweaearaeEILSGLGFPeED 145
|
170 180 190
....*....|....*....|....*....|....
gi 60390566 139 AYQRCDQLSGGQQQRVGIARALMQHPKMILCDEP 172
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-228 |
1.85e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.31 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhhIGMIF-QNYNLISPLTA 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR----IGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:cd03267 113 IDSF--------YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 60390566 177 DPKSTTIVMDILRRLAKEKQLIILINLHQV-DIAmAYTDHIVGINSGAIVFEG 228
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMkDIE-ALARRVLVIDKGRLLYDG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-242 |
2.18e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrKVRHHIGMIFQN---YN 89
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAYVPEDrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPLTALENVLHGRLGAKSTvagmLGLYS-SAEKQEALQLLDEVGLK-EYAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:COG1129 341 LVLDLSIRENITLASLDRLSR----GGLLDrRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILIN--LHQVdIAMAytDHIVGINSGAIVFEGATNEVD-DAVLQHIY 242
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISseLPEL-LGLS--DRILVMREGRIVGELDREEATeEAIMAAAT 491
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-188 |
9.09e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.82 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIFQNynlispLTALENv 100
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKAD------LSTLEN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 101 LHGrlgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKS 180
Cdd:PRK13543 103 LHF----------LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
....*...
gi 60390566 181 TTIVMDIL 188
Cdd:PRK13543 173 ITLVNRMI 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-190 |
9.20e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDirqankaelrkvrhhiGMIF---QNYnLisPL 94
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------------RVLFlpqRPY-L--PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVLhgrlgakstvagmlgLYSSAEKQ----EALQLLDEVGLKEYAyQRCDQ-------LSGGQQQRVGIARALMQH 163
Cdd:COG4178 440 GTLREAL---------------LYPATAEAfsdaELREALEAVGLGHLA-ERLDEeadwdqvLSLGEQQRLAFARLLLHK 503
|
170 180
....*....|....*....|....*..
gi 60390566 164 PKMILCDEPIASLDPKSTTIVMDILRR 190
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-228 |
1.02e-18 |
|
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: 85.45 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqanKAELRKVRHHIGMIFQNYNLIS 92
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PLTALENVL-HGRLGAKSTVAGMLglyssaekqEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:TIGR01257 1017 HLTVAEHILfYAQLKGRSWEEAQL---------EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 172 PIASLDPKSTTIVMDILrrLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-201 |
1.13e-18 |
|
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: 80.55 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRkvRHHIGMI---FQNYN 89
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI--RAGIAYVpedRKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPLTALENVLHGRLgakstvagmlglyssaekqealqlldevglkeyayqrcdqLSGGQQQRVGIARALMQHPKMILC 169
Cdd:cd03215 89 LVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190
....*....|....*....|....*....|..
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-205 |
1.87e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkVRHHIGmifqNYNLISP-LTA 96
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYLG----HRNAMKPaLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVlhgrlgakSTVAGMLGlyssAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASL 176
Cdd:PRK13539 91 AENL--------EFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|
gi 60390566 177 DPKSTTIVMD-ILRRLAKEKqlIILINLHQ 205
Cdd:PRK13539 159 DAAAVALFAElIRAHLAQGG--IVIAATHI 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-238 |
1.96e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkvRHHIG--MIFQNYNLISPLT 95
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK----AHQLGiyLVPQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVLHG---RLGAKSTVAGMLglyssAEKQEALQLLDEVGLKEYAyqrcdqlsggQQQRVGIARALMQHPKMILCDEP 172
Cdd:PRK15439 103 VKENILFGlpkRQASMQKMKQLL-----AALGCQLDLDSSAGSLEVA----------DRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60390566 173 IASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEVDDAVL 238
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-222 |
2.25e-18 |
|
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: 83.72 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIR--DDSGQILLDDTDIRQANKAELRkvR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTE--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 79 HHIGMIFQNYNLISPLTALENVLhgrLGAKSTVAGMLGLYSsAEKQEALQLLDEVGLKEYAYQR-CDQLSGGQQQRVGIA 157
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIF---LGNEITLPGGRMAYN-AMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSG 222
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAVCDTICVIRDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-206 |
4.36e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 19 KAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDT-DIRQANkaeLRKVRHHIGMIFQN---------- 87
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDIN---LKWWRSKIGVVSQDpllfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 ---YNLIS--PLTALENVLH-----------GRLGAKSTVAGMLGL----------------YSSAEKQEALQLLDEVGL 135
Cdd:PTZ00265 479 nikYSLYSlkDLEALSNYYNedgndsqenknKRNSCRAKCAGDLNDmsnttdsneliemrknYQTIKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 136 KEYAYQRCDQ-----------LSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLH 204
Cdd:PTZ00265 559 HDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
..
gi 60390566 205 QV 206
Cdd:PTZ00265 639 RL 640
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-225 |
4.59e-18 |
|
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: 79.76 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHS-LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqaNKAELRKVRHH 80
Cdd:cd03369 7 IEVENLSVRYAPDLPPvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISpltalenvlhgrlGAKSTVAGMLGLYSSAEKQEALQlLDEVGLkeyayqrcdQLSGGQQQRVGIARAL 160
Cdd:cd03369 84 LTIIPQDPTLFS-------------GTIRSNLDPFDEYSDEEIYGALR-VSEGGL---------NLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQliILINLHQVDIAMAYtDHIVGINSGAIV 225
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNST--ILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-233 |
1.17e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD--------SGQILLDDTDIRQANKAELRKVRhhiGMIFQNYN 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLR---AVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPLTALENVLHGRLGAkstvAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQ------- 162
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPH----ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 163 --HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-244 |
2.52e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKHSLKAV---NFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANK------ 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVrnlSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 72 ----AELRKVR-HHIGMIFQnynliSPLTALENVLhgrlGAKSTVAGMLGLYSSAEKQEAL----QLLDEVGLKE----- 137
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQ-----EPMTSLNPVF----TVGEQIAESIRLHQGASREEAMveakRMLDQVRIPEaqtil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 138 --YAYQrcdqLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDH 215
Cdd:PRK10261 163 srYPHQ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250 260
....*....|....*....|....*....
gi 60390566 216 IVGINSGAIVFEGATNEVDDAVlQHIYRQ 244
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAP-QHPYTR 266
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-233 |
3.62e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKT-TILRSINQL---IRDDSGQILLDDTDIrqaNKAELRKVrhHIGMIFQNynlisPLTA 96
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPV---APCALRGR--KIATIMQN-----PRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGRLGAKSTVAGmLGLYSSAekQEALQLLDEVGLKE-------YAYQrcdqLSGGQQQRVGIARALMQHPKMILC 169
Cdd:PRK10418 92 FNPLHTMHTHARETCLA-LGKPADD--ATLTAALEAVGLENaarvlklYPFE----MSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-220 |
3.95e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDK---TYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILlddtdirqankaelRKV 77
Cdd:PRK09544 1 MTSLVSLENvsvSFG-QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTAlenvlhgrlgaksTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:PRK09544 66 KLRIGYVPQKLYLDTTLPL-------------TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGIN 220
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-244 |
4.37e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD----SGQILLDDTDIRQANKAELRK-VRHHIGMIFQNYNliSPLT 95
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRKlVGHNVSMIFQEPQ--SCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVlhGRLGAKS----TVAGMLGLYSSAEKQEALQLLDEVGLKE-------YAYQrcdqLSGGQQQRVGIARALMQHP 164
Cdd:PRK15093 104 PSERV--GRQLMQNipgwTYKGRWWQRFGWRKRRAIELLHRVGIKDhkdamrsFPYE----LTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVfEGATNEVDDAVLQHIYRQ 244
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV-ETAPSKELVTTPHHPYTQ 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-238 |
8.21e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 8.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 14 NKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKV--------RHHIGmif 85
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRG--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 qnynLISPLTALENVLHGRLGAKSTVAGMLgLYSSAEKQEALQLldevgLKEY------AYQRCDQLSGGQQQRVGIARA 159
Cdd:COG3845 347 ----LVPDMSVAENLILGRYRRPPFSRGGF-LDRKAIRAFAEEL-----IEEFdvrtpgPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLhqvDIAMAYTDHIVGINSGAIVFEGATNEVDDAV 237
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLIseDL---DEILALSDRIAVMYEGRIVGEVPAAEATREE 493
|
.
gi 60390566 238 L 238
Cdd:COG3845 494 I 494
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-233 |
1.90e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.25 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD----SGQILLDDTDIRQANKAELRK-VRHHIGMIFQNynlisPLT 95
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKiIGREIAMIFQE-----PSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 AL-----------ENVLHgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKE-------YAYQrcdqLSGGQQQRVGIA 157
Cdd:COG4170 101 CLdpsakigdqliEAIPS------WTFKGKWWQRFKWRKKRAIELLHRVGIKDhkdimnsYPHE----LTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 158 RALMQHPKMILCDEPIASLDPksTTIVmDILRRLAKEKQL----IILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMES--TTQA-QIFRLLARLNQLqgtsILLIS-HDLESISQWADTITVLYCGQTVESGPTEQI 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-244 |
4.52e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 4 VIQLDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQI--------LLDdtdirqankaelr 75
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVevngrvsaLLE------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 kvrhhIGMIFQNYnlispLTALENVlhgRLgakstVAGMLGLyssaEKQEALQLLDEV----GLKEYAYQRCDQLSGGQQ 151
Cdd:COG1134 95 -----LGAGFHPE-----LTGRENI---YL-----NGRLLGL----SRKEIDEKFDEIvefaELGDFIDQPVKTYSSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDP----KSttivMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFE 227
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLAVGDAafqkKC----LARIRELRESGRTVIFVS-HSMGAVRRLCDRAIWLEKGRLVMD 227
|
250
....*....|....*..
gi 60390566 228 GATNEVDDAVLQHIYRQ 244
Cdd:COG1134 228 GDPEEVIAAYEALLAGR 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-215 |
5.89e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYgSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI---RQANKAELRKV 77
Cdd:PRK13540 1 MLDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGmifqnynlISP-LTALENVLHGrlgakstvagmlgLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGI 156
Cdd:PRK13540 80 GHRSG--------INPyLTLRENCLYD-------------IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQvDIAMAYTDH 215
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTS-HQ-DLPLNKADY 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-201 |
1.08e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.95 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSI--NQLIRDDSGQILLDDTDIRQAnKAELRkVRHHIGMIFQ--------- 86
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILEL-SPDER-ARAGIFLAFQypveipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISplTALENVLHGRLGAKstvagmlglyssAEKQEALQLLDEVGLKEYAYQRC--DQLSGGQQQRVGIARALMQHP 164
Cdd:COG0396 94 VSNFLR--TALNARRGEELSAR------------EFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILII 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-205 |
1.94e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDS--GQILLDDtdiRQANKAELRKvrhhIGMIFQNYNLISPLT 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILKR----TGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVLhgrlgakstVAGMLGLYSSAEKQEALQLLDEVgLKEYAYQRCDQ----------LSGGQQQRVGIARALMQHPK 165
Cdd:PLN03211 157 VRETLV---------FCSLLRLPKSLTKQEKILVAESV-ISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAkEKQLIILINLHQ 205
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQ 265
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-201 |
2.98e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDI-----RQANKAelr 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 kvrhHIGMIFQNYNLISPLTALENVLHGRlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVG 155
Cdd:PRK10762 80 ----GIGIIHQELNLIPQLTIAENIFLGR----EFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYI 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-205 |
5.80e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 71.02 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 14 NKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSI--NQLIRDDSGQILLDDTDIRQANKAElrKVRHHIGMIFQNYNLI 91
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALEnvlhgrlgakstvagmlglyssaekqealqLLDEVGlkeyayqrcDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:cd03217 90 PGVKNAD------------------------------FLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....
gi 60390566 172 PIASLDPKSTTIVMDILRRLAKEKQLIILINLHQ 205
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ 164
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-232 |
8.75e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQaNKAELRKvrhHIGMIF-QNYNLISP 93
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFAR---RIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTALEN-VLHGRlgakstvagmlgLY--SSAEKQEALQLLDEV-GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:COG4586 111 LPAIDSfRLLKA------------IYriPDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQV-DIAmAYTDHIVGINSGAIVFEGATNE 232
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMdDIE-ALCDRVIVIDHGRIIYDGSLEE 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-241 |
1.36e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 17 SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrKVRHHIGMIFQNYNLISPLTA 96
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHGRLGAKstvagmlGLYSSAEK--QEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIA 174
Cdd:PRK10982 91 MDNMWLGRYPTK-------GMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 175 SLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVfegATNEVDDAVLQHI 241
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYIS-HKMEEIFQLCDEITILRDGQWI---ATQPLAGLTMDKI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-228 |
1.59e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.82 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDD---TDIRqankaeLRKVRHHIGMIFQNY 88
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQ------LDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 89 NLISPLTAlENVLHGRLGAkstvagmlglySSAEKQEALQLLD--------------EVGlkeyayQRCDQLSGGQQQRV 154
Cdd:PRK10789 399 FLFSDTVA-NNIALGRPDA-----------TQQEIEHVARLASvhddilrlpqgydtEVG------ERGVMLSGGQKQRI 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 155 GIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIilINLHQVDiAMAYTDHIVGINSGAIVFEG 228
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVI--ISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-233 |
5.06e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIrDDSGQILLDDTDIRQANKAELRKVRhhiGMIFQNynlISPLTAL 97
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQ---QTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 EnVLHgrlgakstvagMLGLY--SSAEKQEALQLLDEV----GLKEYAYQRCDQLSGGQQQRVGIARALMQ-------HP 164
Cdd:PRK03695 85 P-VFQ-----------YLTLHqpDKTRTEAVASALNEVaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAkEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-188 |
1.44e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTdirqankaelrkVRhh 80
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET------------VK-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISP-LTALENVLHGRLGAK-STVAGMLG--LYSSAEkqealqlldevglkeyAYQRCDQLSGGQQQRVGI 156
Cdd:COG0488 380 IGYFDQHQEELDPdKTVLDELRDGAPGGTeQEVRGYLGrfLFSGDD----------------AFKPVGVLSGGEKARLAL 443
|
170 180 190
....*....|....*....|....*....|..
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDIL 188
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEAL 475
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-223 |
1.62e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELR-KVRHHIGMIFQNY 88
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 89 NLISPlTALENVLHGRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEyayqRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:cd03290 89 WLLNA-TVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGE----RGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 169 CDEPIASLDPKSTTIVMD--ILRRLAKEKQLIILINlHQVDIaMAYTDHIVGINSGA 223
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVT-HKLQY-LPHADWIIAMKDGS 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-228 |
2.32e-13 |
|
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: 67.43 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 6 QLDKTYGSNKHSLKAVNFtaKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqANKAELrkvrhhigmif 85
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV--SYKPQY----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 86 qnynlISPLTalenvlhgrlgaKSTVAGML-----GLYSSAE-KQEALQLLDEVGLKEyayQRCDQLSGGQQQRVGIARA 159
Cdd:cd03237 70 -----IKADY------------EGTVRDLLssitkDFYTHPYfKTEIAKPLQIEQILD---REVPELSGGELQRVAIAAC 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHqvDIAMA--YTDHIvginsgaIVFEG 228
Cdd:cd03237 130 LSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEH--DIIMIdyLADRL-------IVFEG 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-228 |
2.40e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSnkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIlldDTDIRQANK-------------AE 73
Cdd:PRK13409 346 LTKKLGD--FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKISYKpqyikpdydgtveDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 74 LRKVRHHIGMIFQNYNLISPLtALENvlhgrlgakstvagmlglyssaekqealqLLDevglkeyayQRCDQLSGGQQQR 153
Cdd:PRK13409 421 LRSITDDLGSSYYKSEIIKPL-QLER-----------------------------LLD---------KNVKDLSGGELQR 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 154 VGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHqvDIAMaytdhIVGINSGAIVFEG 228
Cdd:PRK13409 462 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH--DIYM-----IDYISDRLMVFEG 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-244 |
6.56e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 19 KAVNFTAKPGEVTAIIGPSGAGKTTI-----------------------------------------LRSINQL------ 51
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgMKNVNEFsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 52 -------IRDDSGQILLDDTDIRQANkaeLRKVRHHIGMIFQNYNLISpLTALENVLHGRLGA-KSTVAGMLGLYSSAEK 123
Cdd:PTZ00265 1265 gsgedstVFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLFN-MSIYENIKFGKEDAtREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 124 QEALQLLDEVGLKEYAyqrcDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINL 203
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYG----KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1416
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 60390566 204 HQVdIAMAYTDHIVGIN----SGAIVFEGATNEVDDAVLQHIYRQ 244
Cdd:PTZ00265 1417 HRI-ASIKRSDKIVVFNnpdrTGSFVQAHGTHEELLSVQDGVYKK 1460
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-224 |
6.77e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 19 KAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQanKAELRKVRHHIGMI---------FQNYN 89
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKKGMAYItesrrdngfFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPLTALENVLHGRLGakstvaGMLGLY-SSAEKQEALQLLDEVGLKEYAY-QRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:PRK09700 358 IAQNMAISRSLKDGGYK------GAMGLFhEVDEQRTAENQRELLALKCHSVnQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIaMAYTDHIVGINSGAI 224
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI-ITVCDRIAVFCEGRL 487
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-222 |
7.13e-13 |
|
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: 65.57 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIllddtdirqankaelrkvrHHIGMIF--------QNyn 89
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------------SVPGSIAyvsqepwiQN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 lispLTALENVLHG------RLgaKSTVagmlglySSAEKQEALQLLD-----EVGlkeyayQRCDQLSGGQQQRVGIAR 158
Cdd:cd03250 80 ----GTIRENILFGkpfdeeRY--EKVI-------KACALEPDLEILPdgdltEIG------EKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 159 ALMQHPKMILCDEPIASLDPK-STTIVMDILRRLAKEKQLIILINlHQVDIAmAYTDHIVGINSG 222
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVT-HQLQLL-PHADQIVVLDNG 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-178 |
1.29e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILrsinQLIRDDSGQILLDDTDI--RQANKAE-LRKVRHHIGMIFQNYNL---I 91
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITGDHPQGYSNDLTLfgRRRGSGEtIWDIKKHIGYVSSSLHLdyrV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SplTALENV-LHGRLGAkstvagmLGLY---SSAEKQEALQLLDEVGL-KEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PRK10938 352 S--TSVRNViLSGFFDS-------IGIYqavSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTL 422
|
170
....*....|..
gi 60390566 167 ILCDEPIASLDP 178
Cdd:PRK10938 423 LILDEPLQGLDP 434
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-180 |
1.83e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDtDIRqankaelrkvrhhIGMIFQ 86
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-GIK-------------VGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYNLISPLTALENVLHGRLGAKSTVAGMLGLYSS-----------AEKQEALQ-LLDEVGLKEYAYQ--------RC--- 143
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKyaepdadfdklAAEQAELQeIIDAADAWDLDSQleiamdalRCppw 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 60390566 144 DQ----LSGGQQQRVGIARALMQHPKMILCDEPIASLDPKS 180
Cdd:TIGR03719 156 DAdvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-205 |
2.13e-12 |
|
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: 63.80 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 9 KTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQliRDDS----GQILLDDtdirQANKAELRKVrhhIGMI 84
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILING----RPLDKNFQRS---TGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 85 FQNYNLISpltalenvlhgrlgaKSTVagmlglyssaekQEALQLldevglkeYAYQRcdQLSGGQQQRVGIARALMQHP 164
Cdd:cd03232 85 EQQDVHSP---------------NLTV------------REALRF--------SALLR--GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 60390566 165 KMILCDEPIASLDPKSTTIVMDILRRLAKEKQlIILINLHQ 205
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTIHQ 167
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
2.24e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.47 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDsGQILLDDTdirQANKAELRKVRHHIGMIFQNYNLISpltal 97
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV---SWNSVTLQTWRKAFGVIPQKVFIFS----- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQL-----------SGGQQQRVGIARALMQHPKM 166
Cdd:TIGR01271 1306 -----------GTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKI 1374
|
170 180
....*....|....*....|....*...
gi 60390566 167 ILCDEPIASLDPksttIVMDILRRLAKE 194
Cdd:TIGR01271 1375 LLLDEPSAHLDP----VTLQIIRKTLKQ 1398
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-225 |
2.49e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVrhhIGMIFQNYNLISpltal 97
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV---LSIIPQSPVLFS----- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhgrlgakSTVAGMLGLYSS---AEKQEALQ---LLDEV-----GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PLN03232 1324 -----------GTVRFNIDPFSEhndADLWEALErahIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRlaKEKQLIILINLHQVDIAMAyTDHIVGINSGAIV 225
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-228 |
3.48e-12 |
|
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: 65.58 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 7 LDKTYGSnkHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIlldDTDIRQANKAElrKVRHHIGMIFQ 86
Cdd:COG1245 347 LTKSYGG--FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKISYKPQ--YISPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 87 NYnlispltaLENVLHGRLGakstvagmlglySSAEKQEALQLLdevGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:COG1245 420 EF--------LRSANTDDFG------------SSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHqvDIAMaytdhIVGINSGAIVFEG 228
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH--DIYL-----IDYISDRLMVFEG 531
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-189 |
3.57e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVrhhIGMIFQNYNLISpltal 97
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV---LGIIPQAPVLFS----- 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhgrlgakSTVAGML---GLYSSAEKQEALQ---LLDEV-----GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PLN03130 1327 -----------GTVRFNLdpfNEHNDADLWESLErahLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180
....*....|....*....|...
gi 60390566 167 ILCDEPIASLDPKSTTIVMDILR 189
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIR 1418
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-194 |
3.85e-12 |
|
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: 64.49 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDsGQILLDDTDirqANKAELRKVRHHIGMIFQNYNLISpltal 97
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVS---WNSVPLQKWRKAFGVIPQKVFIFS----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhgrlgakSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQL-----------SGGQQQRVGIARALMQHPKM 166
Cdd:cd03289 91 -----------GTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKI 159
|
170 180
....*....|....*....|....*...
gi 60390566 167 ILCDEPIASLDPksttIVMDILRRLAKE 194
Cdd:cd03289 160 LLLDEPSAHLDP----ITYQVIRKTLKQ 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
4.57e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 26 KPGEVTAIIGPSGAGKTTILRSInqlirddSGQIL--LDDTDiRQANKAELrkVRHHIGMIFQNYnlispltaLENVLHG 103
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYE-EEPSWDEV--LKRFRGTELQNY--------FKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 104 RLGA--------------KSTVAGMLGlySSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:PRK13409 159 EIKVvhkpqyvdlipkvfKGKVRELLK--KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLII 199
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLV 266
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-228 |
4.76e-12 |
|
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: 63.05 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSNKHS-LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD---SGQILLDDTDIRQANKaelrKV 77
Cdd:cd03233 6 WRNISFTTGKGRSKIPiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE----KY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 78 RHHIGMIFQNYNLISPLTalenvlhgrlgakstVAgmlglyssaekqealQLLDEVG-LKEYAYQRcdQLSGGQQQRVGI 156
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLT---------------VR---------------ETLDFALrCKGNEFVR--GISGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 157 ARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQV-DIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-200 |
5.46e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.42 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTY-GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSInqlirddSGQILLDDTDIRQANKAELRkvrh 79
Cdd:TIGR01257 1937 ILRLNELTKVYsGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKML-------TGDTTVTSGDATVAGKSILT---- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 80 HIGMIFQNYNLISPLTALENVLHGRlGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARA 159
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGR-EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIIL 200
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-201 |
6.01e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDS--GQILLDDT-----DIRQANkaelrkvRHHIGMIFQNYNL 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRDSE-------ALGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 ISPLTALENVLHGRLGAKStvagmlGLYSSAE-KQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:NF040905 90 IPYLSIAENIFLGNERAKR------GVIDWNEtNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190
....*....|....*....|....*....|..
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQGITSIII 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-205 |
7.36e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQliRDDSGQIlldDTDIRQANKAELRK-VRHHIGMIFQNYNLISPLTA 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI---TGGDRLVNGRPLDSsFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVlhgRLGAKstvagmLGLYSSAEKQEALQLLDEV----GLKEYAyqrcDQLSG--------GQQQRVGIARALMQHP 164
Cdd:TIGR00956 854 RESL---RFSAY------LRQPKSVSKSEKMEYVEEVikllEMESYA----DAVVGvpgeglnvEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 60390566 165 KMIL-CDEPIASLDPKSTTIVMDILRRLAKEKQlIILINLHQ 205
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIHQ 961
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-180 |
8.63e-12 |
|
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: 61.31 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDirqankaelrkvrhHI 81
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIfqnynlispltalenvlhgrlgakstvagmlglyssaekqealqlldevglkeyayqrcDQLSGGQQQRVGIARALM 161
Cdd:cd03221 66 GYF-----------------------------------------------------------EQLSGGEKMRLALAKLLL 86
|
170
....*....|....*....
gi 60390566 162 QHPKMILCDEPIASLDPKS 180
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLES 105
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-178 |
2.09e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.45 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYN 89
Cdd:PRK10522 331 AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK---LFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 LISPLTALEnvlhGRLGAKSTVAGMLglyssaekqEALQLLDEVGLKEYAYQRCdQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:PRK10522 408 LFDQLLGPE----GKPANPALVEKWL---------ERLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLL 473
|
....*....
gi 60390566 170 DEPIASLDP 178
Cdd:PRK10522 474 DEWAADQDP 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-201 |
2.62e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.00 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNfTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGqillddtdiRQANKAELRKV-RHHIGMIFQNYn 89
Cdd:cd03236 10 YGPNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG---------KFDDPPDWDEIlDEFRGSELQNY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 90 lispltaLENVLHGRLGA----------KSTVAGMLG-LYSSAEKQEAL-QLLDEVGLKEYAYQRCDQLSGGQQQRVGIA 157
Cdd:cd03236 79 -------FTKLLEGDVKVivkpqyvdliPKAVKGKVGeLLKKKDERGKLdELVDQLELRHVLDRNIDQLSGGELQRVAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVV 195
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-228 |
9.49e-11 |
|
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: 59.85 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 15 KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDdtdirqankaelRKVRHHIGMifqNYNLISPL 94
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR------------GRVSSLLGL---GGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVlhgRLgakstVAGMLGLyssaEKQEALQLLDEV----GLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:cd03220 100 TGRENI---YL-----NGRLLGL----SRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-210 |
1.38e-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: 60.95 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 26 KPGEVTAIIGPSGAGKTTILRSInqlirddSGQIL--LDDTDirqaNKAELRKV-RHHIGMIFQNYnlispltaLENVLH 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGELKpnLGDYD----EEPSWDEVlKRFRGTELQDY--------FKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 103 GRLGA--------------KSTVAGMLGLYSsaEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMIL 168
Cdd:COG1245 158 GEIKVahkpqyvdlipkvfKGTVRELLEKVD--ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 60390566 169 CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHqvDIAM 210
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVE-H--DLAI 274
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-228 |
2.12e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.10 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 8 DKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSInqlirddsgqilLDDTDIRQANKAELRKVRHHIGMIFQn 87
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG------------LYASGKARLISFLPKFSRNKLIFIDQ- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 88 ynlispltalenvlhgrlgakstvagmlglyssaekqeaLQLLDEVGLkeyAYQRCDQ----LSGGQQQRVGIARALMQH 163
Cdd:cd03238 68 ---------------------------------------LQFLIDVGL---GYLTLGQklstLSGGELQRVKLASELFSE 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 164 PK--MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIaMAYTDHIV------GINSGAIVFEG 228
Cdd:cd03238 106 PPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIE-HNLDV-LSSADWIIdfgpgsGKSGGKVVFSG 176
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-206 |
3.55e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrkvRHHIGMIF-----QNYNLI--SP 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYldAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTAleNV---LHGRLGakstvagmLGLYSSAEKQEALQLLDEVGLK-EYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:PRK15439 358 LAW--NVcalTHNRRG--------FWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190
....*....|....*....|....*....|....*....
gi 60390566 170 DEPIASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQV 206
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFIssDLEEI 466
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-228 |
4.00e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.86 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQliRDDSGQIlldDTDIRQANKAELRKVRHHIGMIFQNYNLISP-LTA 96
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI---EGDIRISGFPKKQETFARISGYCEQNDIHSPqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHgrlgakstvAGMLGLYSSAEKQEALQLLDEV-------GLKE--YAYQRCDQLSGGQQQRVGIARALMQHPKMI 167
Cdd:PLN03140 971 RESLIY---------SAFLRLPKEVSKEEKMMFVDEVmelveldNLKDaiVGLPGVTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 168 LCDEPIASLDPKSTTIVMDILRRLAKEKQLIIlINLHQ--VDIAMAYTDHIVGINSGAIVFEG 228
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV-CTIHQpsIDIFEAFDELLLMKRGGQVIYSG 1103
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-233 |
7.34e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqanKAELRKVRHHIGMIFQNYNLISpltal 97
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA---KIGLHDLRFKITIIPQDPVLFS----- 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 envlhgrlGAKSTVAGMLGLYSSAEKQEALQLLD--------EVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILC 169
Cdd:TIGR00957 1374 --------GSLRMNLDPFSQYSDEEVWWALELAHlktfvsalPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 170 DEPIASLDPKSTTIVMDILRrlAKEKQLIILINLHQVDIAMAYTDHIVgINSGAIVFEGATNEV 233
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNL 1506
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-205 |
1.38e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLDKTYGSNKhSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSIN-----QLIrddSGQILLDDTDIRQANKAElr 75
Cdd:CHL00131 7 ILEIKNLHASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKIL---EGDILFKGESILDLEPEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 76 kvRHHIGMI--FQnYNLISPLTALENVLhgRLgAKSTVAGMLGLySSAEKQEALQLLDE----VGLKEYAYQRC--DQLS 147
Cdd:CHL00131 81 --RAHLGIFlaFQ-YPIEIPGVSNADFL--RL-AYNSKRKFQGL-PELDPLEFLEIINEklklVGMDPSFLSRNvnEGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 148 GGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQ 205
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-201 |
1.80e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDktyGSNKHSlkaVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAElrKVRHHI 81
Cdd:PRK10762 258 LKVDNLS---GPGVND---VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNYN---LISPLTALENVLHGRLGAKSTVAGmlGLYSSAEKQEALQLLDEVGLKEYAY-QRCDQLSGGQQQRVGIA 157
Cdd:PRK10762 330 VYISEDRKrdgLVLGMSVKENMSLTALRYFSRAGG--SLKHADEQQAVSDFIRLFNIKTPSMeQAIGLLSGGNQQKVAIA 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 60390566 158 RALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV 451
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-228 |
1.90e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 11 YGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKvrhHIGMIFQNYNL 90
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ---GVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 91 ISPlTALENVLHGRLGAKSTVAGMLglyssaekqEALQLLDEV-GLKEYAYQRC----DQLSGGQQQRVGIARALMQHPK 165
Cdd:PRK10790 427 LAD-TFLANVTLGRDISEEQVWQAL---------ETVQLAELArSLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVD-IAMAytDHIVGINSGAIVFEG 228
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA--HRLStIVEA--DTILVLHRGQAVEQG 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-201 |
2.36e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDS-GQILLD--DTDIRQANKAelrkVRHHIGMIFQN---YNLISPL 94
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDgkPVKIRNPQQA----IAQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVLhgrLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLK-EYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPI 173
Cdd:PRK13549 357 GVGKNIT---LAALDRFTGGSRIDDAAELKTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180
....*....|....*....|....*...
gi 60390566 174 ASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-205 |
5.48e-09 |
|
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: 54.08 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIllddtdirqankaelrkvrhhigmifqnynlISPltAL 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------------------GMP--EG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVL----HGRLGAKStvagmlglyssaekqealqlldevgLKE---YAYQrcDQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:cd03223 64 EDLLflpqRPYLPLGT-------------------------LREqliYPWD--DVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 60390566 171 EPIASLDPKSTTIVMDILRrlakeKQLIILINL-HQ 205
Cdd:cd03223 117 EATSALDEESEDRLYQLLK-----ELGITVISVgHR 147
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-177 |
7.56e-09 |
|
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: 55.71 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 3 KVIQ---LDKTYGSnKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTdirqankaelrkVrh 79
Cdd:TIGR03719 321 KVIEaenLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------V-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 80 HIGMIFQNYNLISP-LTALENVLHG----RLGAKSTVA-GMLGL--YSSAEKQealqlldevglkeyayQRCDQLSGGQQ 151
Cdd:TIGR03719 386 KLAYVDQSRDALDPnKTVWEEISGGldiiKLGKREIPSrAYVGRfnFKGSDQQ----------------KKVGQLSGGER 449
|
170 180
....*....|....*....|....*.
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLD 177
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
12-228 |
2.26e-08 |
|
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: 53.03 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTI-------------LRSINQLIRDDSGQILLDDTD----------IRQ 68
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQMDKPDVDsieglspaiaIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 69 anKAELRKVRHHIGMIFQNYNLISpltalenVLHGRLGAKSTvagmlglyssaekqeaLQLLDEVGLkEY--AYQRCDQL 146
Cdd:cd03270 85 --KTTSRNPRSTVGTVTEIYDYLR-------LLFARVGIRER----------------LGFLVDVGL-GYltLSRSAPTL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 147 SGGQQQRVGIARALMQHPKMIL--CDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIaMAYTDHIV------G 218
Cdd:cd03270 139 SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE-HDEDT-IRAADHVIdigpgaG 216
|
250
....*....|
gi 60390566 219 INSGAIVFEG 228
Cdd:cd03270 217 VHGGEIVAQG 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-180 |
4.64e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKViqlDKTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDtDIRqankaelrkvrhh 80
Cdd:PRK11819 9 MNRV---SKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-GIK------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALENVlhgrlgakstvagMLGLyssAEKQEALQLLDEVG-------------LKEYA-YQ----- 141
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENV-------------EEGV---AEVKAALDRFNEIYaayaepdadfdalAAEQGeLQeiida 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 142 -----------------RC-------DQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKS 180
Cdd:PRK11819 136 adawdldsqleiamdalRCppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
104-237 |
5.36e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 104 RLGAKSTVAGMLGLY---------SSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIA 174
Cdd:NF000106 94 R*GRRESFSGRENLYmigr*ldlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60390566 175 SLDPKSTTIVMDILRRLAKEKQLIILINLHqVDIAMAYTDHIVGINSGAIVFEGATNEVDDAV 237
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRDGATVLLTTQY-MEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-249 |
1.90e-07 |
|
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: 51.01 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGqillddtdirqankaelrKVRHHIGMIF-QNYNLISPLTA 96
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------------KIKHSGRISFsSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 97 LENVLHG----RLGAKSTV-AGMLGLYSSAEKQEALQLLDEVGLkeyayqrcdQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:cd03291 115 KENIIFGvsydEYRYKSVVkACQLEEDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 172 PIASLDPKSTTIVMD--ILRRLAKEKQLIILINLHQVDIAmaytDHIVGINSGAIVFEGATNEVDDavlqhiyRQPDQST 249
Cdd:cd03291 186 PFGYLDVFTEKEIFEscVCKLMANKTRILVTSKMEHLKKA----DKILILHEGSSYFYGTFSELQS-------LRPDFSS 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-201 |
1.98e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 14 NKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqaNKAELRKVRHHIGMIFQNYNLISP 93
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN--NHNANEAINHGFALVTEERRSTGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTALEnvlhgrLGAKSTVAGM------LGLYSSAEKQEALQ-LLDEVGLKEYAYQ-RCDQLSGGQQQRVGIARALMQHPK 165
Cdd:PRK10982 338 YAYLD------IGFNSLISNIrnyknkVGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190
....*....|....*....|....*....|....*.
gi 60390566 166 MILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILI 201
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
2.26e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 1 MLKVIQLdkTYGSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELRKVRHH 80
Cdd:PRK13541 1 MLSLHQL--QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGmifqnynLISPLTALENVlhgRLGAKstvagmlgLYSSAEKQEALqlLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:PRK13541 79 LG-------LKLEMTVFENL---KFWSE--------IYNSAETLYAA--IHYFKLHDLLDEKCYSLSSGMQKIVAIARLI 138
|
170 180
....*....|....*....|....*...
gi 60390566 161 MQHPKMILCDEPIASLDPKSTTIVMDIL 188
Cdd:PRK13541 139 ACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-90 |
2.56e-07 |
|
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: 50.95 E-value: 2.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANKAELrkvRHHIGMIFQNYNL 90
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY---RQLFSAVFSDFHL 417
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-178 |
2.95e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRQANkaeLRKVRHHIGMIFQNYNLISPlTAL 97
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 98 ENVlHGRLGAkstvagmlglySSAEKQEALQLldeVGLKEYAYQRCDQL-----------SGGQQQRVGIARALMQH-PK 165
Cdd:PTZ00243 1402 QNV-DPFLEA-----------SSAEVWAALEL---VGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKgSG 1466
|
170
....*....|...
gi 60390566 166 MILCDEPIASLDP 178
Cdd:PTZ00243 1467 FILMDEATANIDP 1479
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-233 |
3.44e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 10 TYGSNkHSLKAVNFTAKPGEVTAIIGPSGAGKTTIL------RSINQlirddsGQILLDDTDIrqANKAELRKVRHHIGM 83
Cdd:NF033858 10 RYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQQ------GRVEVLGGDM--ADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 84 IFQNY--NLISPLTALENV-LHGRLgakstvagmLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARAL 160
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENLdFFGRL---------FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 161 MQHPKMILCDEPIASLDPKSttivmdilRRlakekQ---LIILINLHQ----VDIAMAYT------DHIVGINSGAIVFE 227
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLS--------RR-----QfweLIDRIRAERpgmsVLVATAYMeeaerfDWLVAMDAGRVLAT 218
|
....*.
gi 60390566 228 GATNEV 233
Cdd:NF033858 219 GTPAEL 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-204 |
4.12e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILL-----DDTDIrqankaelrKVRHHIGMIFQNYNLISPLT 95
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI---------ATRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALEN-VLHGRLgakstvagmLGLysSAEKQEAL--QLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEP 172
Cdd:NF033858 356 VRQNlELHARL---------FHL--PAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190
....*....|....*....|....*....|....*.
gi 60390566 173 IASLDPksttIVMD----ILRRLAKEKQLIILINLH 204
Cdd:NF033858 425 TSGVDP----VARDmfwrLLIELSREDGVTIFISTH 456
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
21-192 |
4.71e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAkpgEVTAIIGPSGAGKTTILRSI---------------NQLIRDDSGQ------ILLDDTDIR------------ 67
Cdd:COG0419 19 IDFDD---GLNLIVGPNGAGKSTILEAIryalygkarsrsklrSDLINVGSEEasveleFEHGGKRYRierrqgefaefl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 68 QANKAELRKVrhhIGMIFQnynlispLTALENvLHGRLGAKSTvagmlGLYSSAEKQEALQLLDEVGLKEY-AYQRCDQL 146
Cdd:COG0419 96 EAKPSERKEA---LKRLLG-------LEIYEE-LKERLKELEE-----ALESALEELAELQKLKQEILAQLsGLDPIETL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 60390566 147 SGGQQQRVGIARALmqhpKMILcDepIASLDPKSTTIVMDILRRLA 192
Cdd:COG0419 160 SGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALEELA 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-177 |
7.47e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 3 KVIQ---LDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTdirqankaelrkVrh 79
Cdd:PRK11819 323 KVIEaenLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET------------V-- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 80 HIGMIFQNynlispltalenvlHGRLGAKSTVAgmlglyssaekQEALQLLD--EVGLKEY---AY------------QR 142
Cdd:PRK11819 388 KLAYVDQS--------------RDALDPNKTVW-----------EEISGGLDiiKVGNREIpsrAYvgrfnfkggdqqKK 442
|
170 180 190
....*....|....*....|....*....|....*
gi 60390566 143 CDQLSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:PRK11819 443 VGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-232 |
9.23e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSInqlirddsgqilLDDTDIRQANKAELRKVRHHIGMIFQNYNLis 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVVIRGTVAYVPQVSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 plTALENVLHG------RLGAKSTVAGMlglyssaekQEALQLLDEVGLKEYAyQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PLN03130 694 --TVRDNILFGspfdpeRYERAIDVTAL---------QHDLDLLPGGDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 167 ILCDEPIASLDPKSTTIVMD--ILRRLAKEKQLIILINLHqvdiAMAYTDHIVGINSGAIVFEGATNE 232
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNQLH----FLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
146-228 |
1.10e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 146 LSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMD--ILRRLAKEKQLIIlinLHQVDIaMAYTDHIVGINSGA 223
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTRVLA---THQVHV-VPRADYVVALGDGR 858
|
....*
gi 60390566 224 IVFEG 228
Cdd:PTZ00243 859 VEFSG 863
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-208 |
1.22e-06 |
|
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: 46.98 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 27 PGEVTAIIGPSGAGKTTILRSI-NQLIRDDSGQILLDDTDIRQANKAELRKVRHHIGMIfqnynlispltalenvlhgrl 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 106 gakstvagmlglyssaekqealqlldevglkeyayqrcdQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVM 185
Cdd:smart00382 60 ---------------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*....
gi 60390566 186 DILR------RLAKEKQLIILINLHQVDI 208
Cdd:smart00382 101 LLEElrllllLKSEKNLTVILTTNDEKDL 129
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-233 |
2.31e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 127 LQLLDEVGLkeyAYQRCDQ----LSGGQQQRVGIARALMQ---HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLII 199
Cdd:TIGR00630 810 LQTLCDVGL---GYIRLGQpattLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVV 886
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 60390566 200 LI--NLHQVDIAmaytDHIV------GINSGAIVFEGATNEV 233
Cdd:TIGR00630 887 VIehNLDVIKTA----DYIIdlgpegGDGGGTVVASGTPEEV 924
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-249 |
2.45e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSInqlirddSGQILLDDTDIRqankaelrkvrhHIGMIF--QNYNLISPLT 95
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI-------MGELEPSEGKIK------------HSGRISfsPQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 96 ALENVLHGRLGAKSTVAGMLglySSAEKQEALQLL---DEVGLKEYAYQrcdqLSGGQQQRVGIARALMQHPKMILCDEP 172
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVI---KACQLEEDIALFpekDKTVLGEGGIT----LSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 173 IASLDpksTTIVMDILRR-----LAKEKQLIILINLHQVDIAmaytDHIVGINSGAIVFEGATNEvddavLQHiyRQPDQ 247
Cdd:TIGR01271 576 FTHLD---VVTEKEIFESclcklMSNKTRILVTSKLEHLKKA----DKILLLHEGVCYFYGTFSE-----LQA--KRPDF 641
|
..
gi 60390566 248 ST 249
Cdd:TIGR01271 642 SS 643
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-202 |
2.68e-06 |
|
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: 47.90 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDD-SGQILLD--DTDIRQANKAelrkVRHHIGMIFQN---YNLISPL 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNPAQA----IRAGIAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVlhgRLGAKSTVAGMLGLYSSAEKQEALQLLDEVGLKEYA-YQRCDQLSGGQQQRVGIARALMQHPKMILCDEPI 173
Cdd:TIGR02633 355 GVGKNI---TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180
....*....|....*....|....*....
gi 60390566 174 ASLDPKSTTIVMDILRRLAKEKQLIILIN 202
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-225 |
4.20e-06 |
|
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: 46.83 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGSN-KHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIrqaNKAELRKVRHH 80
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI---SKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 81 IGMIFQNYNLISPLTALeNVLHGRLGAKSTVagmlglyssAEKQEALQLLDEV-----GLKEYAYQRCDQLSGGQQQRVG 155
Cdd:cd03288 97 LSIILQDPILFSGSIRF-NLDPECKCTDDRL---------WEALEIAQLKNMVkslpgGLDAVVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 156 IARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILInlHQVDIAMAyTDHIVGINSGAIV 225
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIA--HRVSTILD-ADLVLVLSRGILV 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-201 |
5.97e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 22 NFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIlldDTDIRQANKAELRKVRHHIGMIFQ--NYNLISPltALEN 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER---QSQFSHITRLSFEQLQKLVSDEWQrnNTDMLSP--GEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 100 VlhGRlgaksTVAGMLGLYSSAEkQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIASLDPK 179
Cdd:PRK10938 98 T--GR-----TTAEIIQDEVKDP-ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|..
gi 60390566 180 STTIVMDILRRLAKEKQLIILI 201
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-177 |
7.59e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 23 FTAKPGEVTAIIGPSGAGKTTILRSInqlirddSGQILLDD------TDI-----RQ------------------ANKAE 73
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriiyeQDLivarlQQdpprnvegtvydfvaegiEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 74 LRKVRHHIG-MIFQNYN--LISPLTALENVL--HG--RLGAK-STVAGMLGLysSAEKQealqlldevgLKEyayqrcdq 145
Cdd:PRK11147 97 YLKRYHDIShLVETDPSekNLNELAKLQEQLdhHNlwQLENRiNEVLAQLGL--DPDAA----------LSS-------- 156
|
170 180 190
....*....|....*....|....*....|..
gi 60390566 146 LSGGQQQRVGIARALMQHPKMILCDEPIASLD 177
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-228 |
7.75e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 127 LQLLDEVGLKEYAYQRC-DQLSGGQQQRVGIARALMQHPKMI--LCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINL 203
Cdd:PRK00635 457 LSILIDLGLPYLTPERAlATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
90 100
....*....|....*....|....*
gi 60390566 204 HQVDIAMAytDHIVGINSGAIVFEG 228
Cdd:PRK00635 537 DEQMISLA--DRIIDIGPGAGIFGG 559
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-228 |
7.77e-06 |
|
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: 45.26 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 146 LSGGQQQRVGIARALMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIvginsgaIV 225
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-------HV 144
|
...
gi 60390566 226 FEG 228
Cdd:cd03222 145 FEG 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-233 |
7.94e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSinqlirddsgqiLLDDTDIRQANKAELRKVRHHIGMIFQNYNLis 92
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISA------------MLGELSHAETSSVVIRGSVAYVPQVSWIFNA-- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 plTALENVLHG------RLGAKSTVAGMlglyssaekQEALQLLDEVGLKEYAyQRCDQLSGGQQQRVGIARALMQHPKM 166
Cdd:PLN03232 694 --TVRENILFGsdfeseRYWRAIDVTAL---------QHDLDLLPGRDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 167 ILCDEPIASLDPKSTTIVMD--ILRRLAKEKQLIILINLHqvdiAMAYTDHIVGINSGAIVFEGATNEV 233
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQLH----FLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-239 |
9.30e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 21 VNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDTDIRqankaeLRKVRHHI--GMIF----QNYNLISPL 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIraGIMLcpedRKAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVLHGRLGAKSTVAGMLgLYSSAEKQEALQLLDEVGLKE-YAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPI 173
Cdd:PRK11288 346 HSVADNINISARRHHLRAGCL-INNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60390566 174 ASLDPKSTTIVMDILRRLAKEKQLIILI--NLHQVdiaMAYTDHIVGINSGAIVFEGATNEVD-DAVLQ 239
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVssDLPEV---LGVADRIVVMREGRIAGELAREQATeRQALS 490
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-219 |
9.41e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 27 PGEVTAIIGPSGAGKTTILRSInqlirddsGQILLddtdirQANKAELRKVRHHIGmifqnynLISPltalenvlhgrlg 106
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI--------GLALG------GAQSATRRRSGVKAG-------CIVA------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 107 akstvagmlglYSSAEkqealqlldevglkeyAYQRCDQLSGGQQQRVGIARAL-MQHPK---MILCDEPIASLDPKSTT 182
Cdd:cd03227 66 -----------AVSAE----------------LIFTRLQLSGGEKELSALALILaLASLKprpLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 60390566 183 IVMDILRRLAKEK-QLIILINLHQVdIAMAytDHIVGI 219
Cdd:cd03227 119 ALAEAILEHLVKGaQVIVITHLPEL-AELA--DKLIHI 153
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-250 |
1.15e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTILRSI----NQLIRDDSGQILLDDTDirqanKAELRKvrHHIGMIFqnYNlisp 93
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGIT-----PEEIKK--HYRGDVV--YN---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 ltaLENVLH-GRLGAKST---VAGMLGL---YSSAEKQEALQLLDEVGLKEYAYQRCDQ----------LSGGQQQRVGI 156
Cdd:TIGR00956 144 ---AETDVHfPHLTVGETldfAARCKTPqnrPDGVSREEYAKHIADVYMATYGLSHTRNtkvgndfvrgVSGGERKRVSI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 157 ARALMQHPKmILC-DEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDiAMAYT--DHIVGINSGAIVFEGATNEV 233
Cdd:TIGR00956 221 AEASLGGAK-IQCwDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS-QDAYElfDKVIVLYEGYQIYFGPADKA 298
|
250
....*....|....*...
gi 60390566 234 DDAVLQHIYRQPD-QSTA 250
Cdd:TIGR00956 299 KQYFEKMGFKCPDrQTTA 316
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-180 |
1.93e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 2 LKVIQLDKTYGsNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQillddtdIRQANKAElrkvrhhI 81
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENAN-------I 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 82 GMIFQNY--------NLISPLTALENVLHGRLgaksTVAGMLG--LYSSaekqealqllDEVGLKeyayqrCDQLSGGQQ 151
Cdd:PRK15064 385 GYYAQDHaydfendlTLFDWMSQWRQEGDDEQ----AVRGTLGrlLFSQ----------DDIKKS------VKVLSGGEK 444
|
170 180
....*....|....*....|....*....
gi 60390566 152 QRVGIARALMQHPKMILCDEPIASLDPKS 180
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-177 |
2.60e-05 |
|
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: 45.32 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 17 SLKAVNFTAKPGEVTAIIGPSGAGKTTILRSinqlirddsgqiLLddtdirqankAELRKVRHHIGM-----IFQNYNLI 91
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSA------------LL----------AEMDKVEGHVHMkgsvaYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENVLHGR-LGAKSTVAGMlglyssaekqEALQLLDEV-----GLKEYAYQRCDQLSGGQQQRVGIARALMQHPK 165
Cdd:TIGR00957 711 QNDSLRENILFGKaLNEKYYQQVL----------EACALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170
....*....|..
gi 60390566 166 MILCDEPIASLD 177
Cdd:TIGR00957 781 IYLFDDPLSAVD 792
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-228 |
2.75e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 18 LKAVNFTAKPGEVTAIIGPSGAGKTTIlrSINQLIRDD----SGQILLDDTDIRQANKAElrKVRHHIGMIFQnYNLISP 93
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTL--SATLAGREDyevtGGTVEFKGKDLLELSPED--RAGEGIFMAFQ-YPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTALENVLHGRLGAKSTVAGmlglyssaekQEALQLLDEVGLKEYAYQRCDQ------------LSGGQQQRVGIARALM 161
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRG----------QEPLDRFDFQDLMEEKIALLKMpedlltrsvnvgFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 162 QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINLHQVDIAMAYTDHIVGINSGAIVFEG 228
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-199 |
3.62e-05 |
|
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: 43.36 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 30 VTAIIGPSGAGKTTILRSIN-----QLIRDDSGQILLDDTDIRQANKAELR-KVRHHIGmifQNYNLISPLTALENVLHG 103
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltgELPPNSKGGAHDPKLIREGEVRAQVKlAFENANG---KKYTITRSLAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 104 RlgakstvagmlglyssaekQEALQ--LLDEVGlkeyayqrcdQLSGGQQQ------RVGIARALMQHPKMILCDEPIAS 175
Cdd:cd03240 101 H-------------------QGESNwpLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180
....*....|....*....|....*..
gi 60390566 176 LDPKSTTIVM-DILRRLAKEK--QLII 199
Cdd:cd03240 152 LDEENIEESLaEIIEERKSQKnfQLIV 178
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
12-228 |
4.30e-05 |
|
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: 43.76 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTI--------LRSINQLIRDDSGQ-------------ILLDDTDI---R 67
Cdd:cd03271 5 GARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNhdrieglehidkvIVIDQSPIgrtP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 68 QANKAELRKVRHHIGMIF------QNYNlisPLTaLENVLHGRlgaksTVAGMLGL--YSSAEKQEA-------LQLLDE 132
Cdd:cd03271 85 RSNPATYTGVFDEIRELFcevckgKRYN---RET-LEVRYKGK-----SIADVLDMtvEEALEFFENipkiarkLQTLCD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 133 VGLkeyAYQRCDQ----LSGGQQQRVGIARALMQ---HPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQ 205
Cdd:cd03271 156 VGL---GYIKLGQpattLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIE-HN 231
|
250 260
....*....|....*....|....*....
gi 60390566 206 VDIaMAYTDHIV------GINSGAIVFEG 228
Cdd:cd03271 232 LDV-IKCADWIIdlgpegGDGGGQVVASG 259
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-227 |
4.51e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 13 SNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSI--NQLIRDDSGQILLDDTDIR-----QANKAELRKV---RHHIG 82
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDvstvsDAIDAGLAYVtedRKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 83 MifqnyNLISPLTalENVLHGRLG--AKSTVagmlgLYSSAEKQEALQLLDEVGLKEYA-YQRCDQLSGGQQQRVGIARA 159
Cdd:NF040905 351 L-----NLIDDIK--RNITLANLGkvSRRGV-----IDENEEIKVAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 160 LMQHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQLIILIN--LHQVdIAMayTDHIVGINSGAIVFE 227
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISseLPEL-LGM--CDRIYVMNEGRITGE 485
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-177 |
4.70e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 19 KAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGqillddTDIRQAnkaelrKVR------HHI-GMIFQNYNLI 91
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG------TVFRSA------KVRmavfsqHHVdGLDLSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENVLHGRLGAKSTVAGMLGlyssaekqealqlldevglkEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDE 171
Cdd:PLN03073 594 YMMRCFPGVPEQKLRAHLGSFGVTG--------------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
....*.
gi 60390566 172 PIASLD 177
Cdd:PLN03073 654 PSNHLD 659
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-206 |
1.79e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 16 HSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIllddtdirqankaelrkVRH-HIGMIFQNYNLISPL 94
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------------DRNgEVSVIAISAGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 95 TALENVLHGRLgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCDEPIA 174
Cdd:PRK13546 101 TGIENIEFKML--------CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|....
gi 60390566 175 SLDPKSTTIVMDILRRLAKEKQLIILI--NLHQV 206
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNKTIFFVshNLGQV 206
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-235 |
2.48e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 12 GSNKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQIllddtDIRQAnkaelrkvrhhIGMIFQNYNLI 91
Cdd:PRK13545 34 GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGS-----------AALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 92 SPLTALENV-LHGRlgakstvagMLGLYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIARALMQHPKMILCD 170
Cdd:PRK13545 98 GQLTGIENIeLKGL---------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60390566 171 EPIASLDPKSTTIVMDILRRLAKEKQLIILINlHQVDIAMAYTDHIVGINSGAIVFEGATNEVDD 235
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEQGKTIFFIS-HSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-233 |
9.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 122 EKQEALQLLDEVGLkEYAY--QRCDQLSGGQQQRVGIARALMQHPK--MILCDEPIASLDPKSTTIVMDILRRLAKEKQL 197
Cdd:TIGR00630 464 EIRERLGFLIDVGL-DYLSlsRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT 542
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 60390566 198 IILINlHQVDiAMAYTDHIV------GINSGAIVFEGATNEV 233
Cdd:TIGR00630 543 LIVVE-HDED-TIRAADYVIdigpgaGEHGGEVVASGTPEEI 582
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
28-199 |
1.25e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 28 GEVTAIIGPSGAGKTTILRSInQLIRDDSGQILLDDTDIRQANKAELRKVrhHIGMIFQNY---------------NLIS 92
Cdd:COG3593 23 DDLTVLVGENNSGKSSILEAL-RLLLGPSSSRKFDEEDFYLGDDPDLPEI--EIELTFGSLlsrllrlllkeedkeELEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 93 PLTALENVLHGRLGA-KSTVAGMLG---------LYSSAEKQEALQLLDEVGLKEYAYQRCDQLSGGQQQRVGIA--RAL 160
Cdd:COG3593 100 ALEELNEELKEALKAlNELLSEYLKelldgldleLELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLILLAllSAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 60390566 161 MQH-----PKMILCDEPIASLDPKSTTIVMDILRRLAKEK-QLII 199
Cdd:COG3593 180 AELkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEKPnQVII 224
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
20-61 |
1.87e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 38.31 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 60390566 20 AVNFTAKPGEVTAIIGPSGAGKTTILRSINQLIRDDSGQILL 61
Cdd:pfam13604 10 VRALLTSGDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIG 51
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
32-63 |
1.96e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 38.28 E-value: 1.96e-03
10 20 30
....*....|....*....|....*....|...
gi 60390566 32 AIIGPSGAGKTTILRSINQLIRDDSGQIL-LDD 63
Cdd:COG0572 11 GIAGPSGSGKTTFARRLAEQLGADKVVVIsLDD 43
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-111 |
2.28e-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: 38.52 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 30 VTAIIGPSGAGKTTILRSINQLIRDDSGQILLDDT----------DIRQANKAELRKVRHHIGMIF-QNYNLISPLTALE 98
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDErsrnggiggiPSLLNGIDPKEPIEFEISEFLeDGVRYRYGLDLER 80
|
90
....*....|...
gi 60390566 99 NVLHGRLGAKSTV 111
Cdd:pfam13304 81 EDVEEKLSSKPTL 93
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-195 |
2.46e-03 |
|
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: 38.96 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 22 NFTAKPGEVTAIIGPSGAGKTTILRSINQL--------IRDDSGQILLddtdIRQANKAELRKVRHHIgmifqnynlISP 93
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY----VPQRPYMTLGTLRDQI---------IYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 94 LTALENVLHGrlgakstvagmlglYSSaekQEALQLLDEVGLkEYAYQR----------CDQLSGGQQQRVGIARALMQH 163
Cdd:TIGR00954 539 DSSEDMKRRG--------------LSD---KDLEQILDNVQL-THILEReggwsavqdwMDVLSGGEKQRIAMARLFYHK 600
|
170 180 190
....*....|....*....|....*....|..
gi 60390566 164 PKMILCDEPIASLDPKsttiVMDILRRLAKEK 195
Cdd:TIGR00954 601 PQFAILDECTSAVSVD----VEGYMYRLCREF 628
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
127-190 |
2.96e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.06 E-value: 2.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60390566 127 LQLLDEVGLKEYAYQRCDQLSGGQQQRVG---IARALMQH----------PKMILCDEPIASLDPKSTTIVMDILRR 190
Cdd:pfam13558 14 VEVRDEDGSEVETYRRSGGLSGGEKQLLAylpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
127-228 |
3.35e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 127 LQLLDEVGLkeyAYQRCDQ----LSGGQQQRVGIARALM---QHPKMILCDEPiasldpksTT--------IVMDILRRL 191
Cdd:COG0178 807 LQTLQDVGL---GYIKLGQpattLSGGEAQRVKLASELSkrsTGKTLYILDEP--------TTglhfhdirKLLEVLHRL 875
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 60390566 192 AKEKQLIILINlHQVD-IAMAytDHIV------GINSGAIVFEG 228
Cdd:COG0178 876 VDKGNTVVVIE-HNLDvIKTA--DWIIdlgpegGDGGGEIVAEG 916
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-199 |
5.06e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.24 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60390566 136 KEYAYQRCDQLSGGQQQRVGIARAL---MQHPK-MILCDEPIASLDPKSTTIVMDILRRLAKEKQLII 199
Cdd:cd03272 149 KQDEQQEMQQLSGGQKSLVALALIFaiqKCDPApFYLFDEIDAALDAQYRTAVANMIKELSDGAQFIT 216
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
14-52 |
5.71e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 60390566 14 NKHSLKAVNFTAKPGEVTAIIGPSGAGKTTILRSINQLI 52
Cdd:pfam13555 8 NWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-228 |
7.24e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60390566 124 QEALQLLDEVGLkeyAY----QRCDQLSGGQQQRVGIARALM---QHPKMILCDEPIASLDPKSTTIVMDILRRLAKEKQ 196
Cdd:PRK00635 1677 QKPLQALIDNGL---GYlplgQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH 1753
|
90 100 110
....*....|....*....|....*....|....*....
gi 60390566 197 LIILINLHqvdIAMA-YTDHIV------GINSGAIVFEG 228
Cdd:PRK00635 1754 SVIYIDHD---PALLkQADYLIemgpgsGKTGGKILFSG 1789
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-54 |
9.38e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 36.83 E-value: 9.38e-03
10 20 30
....*....|....*....|....*....|....*...
gi 60390566 17 SLKavNFTAKPGEVTAIIGPSGAGKTTILRSInQLIRD 54
Cdd:COG4637 12 SLR--DLELPLGPLTVLIGANGSGKSNLLDAL-RFLSD 46
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
14-48 |
9.41e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 37.09 E-value: 9.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 60390566 14 NKHSLKA---VNFTAKP---GEVTAIIGPSGAGKTTILRSI 48
Cdd:PRK10246 10 NLNSLKGewkIDFTAEPfasNGLFAITGPTGAGKTTLLDAI 50
|
|
| |
