|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-245 |
6.42e-136 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 382.48 E-value: 6.42e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR 80
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIE 240
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLR 240
|
....*
gi 488231729 241 TIYQS 245
Cdd:COG3638 241 EIYGG 245
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-243 |
3.92e-128 |
|
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: 362.27 E-value: 3.92e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRRI 82
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIETI 242
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 488231729 243 Y 243
Cdd:cd03256 241 Y 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-244 |
1.05e-126 |
|
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: 358.92 E-value: 1.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIET 241
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
...
gi 488231729 242 IYQ 244
Cdd:TIGR02315 241 IYG 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-225 |
8.10e-75 |
|
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: 226.22 E-value: 8.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK- 78
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQHYNLVSRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLL--------LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAiDYSDRIIGVNSGKI 225
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-226 |
1.90e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 220.69 E-value: 1.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:COG1136 4 LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 -RRRIGMIFQHYNLVSRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLL--------LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAiDYSDRIIGVNSGKIV 226
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-244 |
3.40e-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: 215.68 E-value: 3.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRR 81
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL---ASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGaaglYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGRYPHLGLFGR----PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKEKIE 240
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTPELLE 232
|
....
gi 488231729 241 TIYQ 244
Cdd:COG1120 233 EVYG 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-234 |
7.48e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 209.47 E-value: 7.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNeLKRKELRKKRRR 81
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVlhgCLGYKTTLsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENV---TLAPIKVK----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKritnELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMR----DLAkegMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-234 |
1.51e-66 |
|
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: 214.38 E-value: 1.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYP----NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRK 77
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYN--LVSRLTVIENV-----LHGCLGykttlsgaaglyREEEKEQAFDLIEKVDLSA-FAYTRCDELSG 149
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIaeplrLHGLLS------------RAERRERVAELLERVGLPPdLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 150 GQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*
gi 488231729 230 RPYEL 234
Cdd:COG1123 488 PTEEV 492
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-234 |
4.27e-66 |
|
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: 204.74 E-value: 4.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ---ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQHYNLVSRLTVIENVlhgclGYKTTLsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENV-----ALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-231 |
1.50e-65 |
|
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: 202.70 E-value: 1.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKelrkkr 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQHYNLVSRLTVIENVLhgcLGYKttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVA---LGLE-----LQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIigvnsgkIVFEGRP 231
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRV-------VVLSARP 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-234 |
3.15e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.08 E-value: 3.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ---ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKR 79
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRLTVIENVlhgclgykttlsgA-----AGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQR 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENV-------------AlpleiAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-225 |
1.04e-64 |
|
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: 200.45 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRrI 82
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQK-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLhgcLGYKTTLsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENIT---LAPIKVK----GMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-230 |
1.16e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 200.66 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRRI 82
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENV---LHgclgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENValpLR-----------VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLV---NLHQVETaidYSDRIIGVNSGKIVFEGR 230
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIathDLELVDR---MPKRVLELEDGRLVRDEA 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
2.64e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 201.09 E-value: 2.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkeLRK 77
Cdd:COG1116 6 PALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP--------VTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVSRLTVIENVLhgcLGYKttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVA---LGLE-----LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIigvnsgkIVFEGRP 231
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV-------VVLSARP 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-226 |
2.94e-64 |
|
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: 199.28 E-value: 2.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRI 82
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGClgykttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGL--------KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-244 |
7.85e-64 |
|
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: 199.05 E-value: 7.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGcLGYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFP-LREHTDLS------EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIET 241
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPW 236
|
...
gi 488231729 242 IYQ 244
Cdd:COG1127 237 VRQ 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-224 |
3.37e-63 |
|
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: 195.48 E-value: 3.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNeLKRKELRKKRRRI 82
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-DLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGclgykttlsgaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARALM 162
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGK 224
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-245 |
4.35e-63 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 198.31 E-value: 4.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSG----------TIRFEDRemnelK 71
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGR-----L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQHYNLVSRLTVIENVLHGCLG----YKTTLSgaagLYREEEKEQAFDLIEKVDLSAFAYTRCDEL 147
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGstpfWRTCFS----WFTREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVF 227
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|....*...
gi 488231729 228 EGRPYELTKEKIETIYQS 245
Cdd:PRK09984 234 DGSSQQFDNERFDHLYRS 251
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-234 |
1.23e-61 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 197.24 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM--------Nelkrk 73
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekrN----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 74 elrkkrrrIGMIFQHYNLVSRLTVIENVLHGclgykttLSgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQ 153
Cdd:COG3842 79 --------VGMVFQDYALFPHLTVAENVAFG-------LR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE 233
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
.
gi 488231729 234 L 234
Cdd:COG3842 223 I 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-243 |
1.78e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.97 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkRKELRKKRRRI 82
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHgclgykttlsgAAGLY---REEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRF-----------FARLYglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
....
gi 488231729 240 ETIY 243
Cdd:COG1131 224 EDVF 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-234 |
5.48e-61 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 191.39 E-value: 5.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYN--LVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:COG1122 78 GLVFQNPDdqLFAP-TVEEDVAFGPENL--------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
6.39e-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: 6.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkeLRKKRR 80
Cdd:COG1121 5 PAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--------PRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSR--LTVIENVLHGCLGYKttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:COG1121 76 RIGYVPQRAEVDWDfpITVRDVVLMGRYGRR----GLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNsGKIVFEGRPYE-LTKE 237
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEvLTPE 229
|
....*.
gi 488231729 238 KIETIY 243
Cdd:COG1121 230 NLSRAY 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-231 |
2.39e-58 |
|
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: 184.95 E-value: 2.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnELKRKELRKKRRRI 82
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED--ITGLPPHEIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREEEK--EQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRP 231
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-234 |
3.78e-58 |
|
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: 184.36 E-value: 3.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrrrI 82
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-----V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgCLGYKTtlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03300 75 NTVFQNYALFPHLTVFENI---AFGLRL-----KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-229 |
4.45e-58 |
|
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: 184.25 E-value: 4.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQHY--NLVSRLTVIENV-----LHGCLGYKttlsgaaglyrEEEKEQAFDLIEKVDLSA-FAYTRCDELSGG 150
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIaeplrIHGKLSKK-----------EARKEAVLLLLVGVGLPEeVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-234 |
1.27e-56 |
|
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: 180.78 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRRI 82
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENV---LHgclgYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVafpLR----EHTRLS------EEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.25e-55 |
|
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: 178.69 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkelrkkrr 80
Cdd:COG0411 3 PLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 riGM------------IFQHYNLVSRLTVIENVLHGCL-----GYKTTLSGAAGLYREEEK--EQAFDLIEKVDLSAFAY 141
Cdd:COG0411 70 --GLpphriarlgiarTFQNPRLFPELTVLENVLVAAHarlgrGLLAALLRLPRARREEREarERAEELLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 142 TRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVN 221
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
250
....*....|..
gi 488231729 222 SGKIVFEGRPYE 233
Cdd:COG0411 228 FGRVIAEGTPAE 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-233 |
3.84e-55 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 180.00 E-value: 3.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR 80
Cdd:PRK11153 3 ELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENV---LHgclgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNValpLE-----------LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE 233
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-234 |
4.30e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 180.34 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKkrr 80
Cdd:COG1118 1 MSIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rIGMIFQHYNLVSRLTVIENVlhgclgykttlsgAAGL-----YREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRV 155
Cdd:COG1118 77 -VGFVFQHYALFPHMTVAENI-------------AFGLrvrppSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-224 |
6.87e-55 |
|
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: 175.35 E-value: 6.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrrI 82
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNL-VSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENL--------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGK 224
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-229 |
2.38e-54 |
|
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: 173.87 E-value: 2.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkeLRKKRRRIG 83
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--------LEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQHYNlVSR---LTVIENVLHGCLGYKttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03235 72 YVPQRRS-IDRdfpISVRDVVLMGLYGHK----GLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNsGKIVFEG 229
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-234 |
1.02e-53 |
|
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: 173.26 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgclgykTTLSGAAGLYREEEKEQAFDLIEKVDL--SAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENI--------ALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-234 |
8.64e-53 |
|
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: 178.17 E-value: 8.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNG-NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDREMnelKRKELRK 77
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL---LELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHY-NLVSRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVG 156
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALE--------NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-229 |
1.80e-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: 168.00 E-value: 1.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNElkrkelrkkrrrig 83
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 miFQHYNLVSRLTVIEnvlhgclgykttlsgaaglyreeekeQAfdlIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ 163
Cdd:cd03214 66 --LSPKELARKIAYVP--------------------------QA---LELLGLAHLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-229 |
3.41e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.11 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR 80
Cdd:PRK11124 1 MSIQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 ---RIGMIFQHYNLVSRLTVIENVLHG-ClgykttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVG 156
Cdd:PRK11124 80 lrrNVGMVFQQYNLWPHLTVQQNLIEApC--------RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDylkrITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVS----IIRELAetgITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-234 |
2.11e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.88 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIFQHYNLVSRLTVIENVLHGCLGYKttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK09493 80 -GMVFQQFYLFPHLTALENVMFGPLRVR-------GASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-226 |
2.50e-50 |
|
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: 164.98 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrIGMIFQHYnlvsrltviENVLHGCLGYKTTLS-GAAGLYREEEKEQAFDLIEKVDL-SAFAYTRCDELSGGQKQRVG 156
Cdd:COG1124 81 ---VQMVFQDP---------YASLHPRHTVDRILAePLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVEtAIDY-SDRIIGVNSGKIV 226
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLA-VVAHlCDRVAVMQNGRIV 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-229 |
2.86e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.42 E-value: 2.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR 80
Cdd:COG4161 1 MSIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 ---RIGMIFQHYNLVSRLTVIENVLHGCLGykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:COG4161 80 lrqKVGMVFQQYNLWPHLTVMENLIEAPCK-------VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDylkrITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVE----IIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-241 |
3.66e-50 |
|
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: 164.26 E-value: 3.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelKRKELRKKRRR 81
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHgclgykttLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRY--------FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIET 241
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-225 |
7.64e-50 |
|
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: 162.58 E-value: 7.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRRI 82
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgclGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENV-----AFALEVTGVP---PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-234 |
1.23e-49 |
|
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: 162.89 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGnQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrr 80
Cdd:cd03296 1 MSIEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rIGMIFQHYNLVSRLTVIENVLHGcLGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03296 76 -VGFVFQHYALFRHMTVFDNVAFG-LRVKPRSERPP---EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-234 |
1.74e-49 |
|
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: 163.78 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQH--YNLVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLS-AFAYTRCDELSGGQKQRV 155
Cdd:TIGR04521 81 RKKVGLVFQFpeHQLFEE-TVYKDIAFGPKNL--------GLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-235 |
7.00e-49 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 160.69 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpnGNQALQdISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRI 82
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgCLGYKTTLSgaaglYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNI---GLGLRPGLK-----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELT 235
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-234 |
3.09e-48 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 160.12 E-value: 3.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK-RRRIGMIFQHYNLVSRLT 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 97 VIENVLHGclgykttLSgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIAS 176
Cdd:cd03294 119 VLENVAFG-------LE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 177 LDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-234 |
1.03e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 161.01 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkELRKKRRRI 82
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGclgykttLSgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFP-------LK-LRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLH-QVEtAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVE-AMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-224 |
1.55e-47 |
|
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: 156.64 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENV---LHgclgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENValpLE-----------VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGK 224
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-244 |
8.98e-47 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 156.01 E-value: 8.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrrIG 83
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR---LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQHYNLVSRLTVIENVLHGCLGYkttlSGaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ 163
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGRFPY----SK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKEKIETI 242
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEiITPEVLSDI 232
|
..
gi 488231729 243 YQ 244
Cdd:COG4604 233 YD 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-242 |
9.38e-47 |
|
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: 156.44 E-value: 9.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN-QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDreMNELKRKELRKKRRR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQhyN----LVSRlTVIENVLHGC--LGykttlsgaagLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRV 155
Cdd:TIGR04520 79 VGMVFQ--NpdnqFVGA-TVEDDVAFGLenLG----------VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYEL- 234
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIf 224
|
....*....
gi 488231729 235 -TKEKIETI 242
Cdd:TIGR04520 225 sQVELLKEI 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-226 |
4.18e-46 |
|
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: 153.49 E-value: 4.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKtYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEA-----DSGTIRFEDREMNeLKRKELRK 77
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIY-DLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVsRLTVIENV-----LHGCLGykttlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCD--ELSGG 150
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVayglrLHGIKL------------KEELDERVEEALRKAALWDEVKDRLHalGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITcLV--NLHQvetAIDYSDRIIGVNSGKIV 226
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIV-IVthNMQQ---AARVADRTAFLLNGRLV 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-225 |
8.04e-46 |
|
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: 151.01 E-value: 8.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrKELRKKRRRI 82
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgclgykttlsgaaglyreeekeqafdliekvdlsafaytrcdELSGGQKQRVGIARALM 162
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL--------------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-237 |
1.95e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 155.88 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrrr 81
Cdd:PRK09452 14 LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKTTlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTP--------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-226 |
4.16e-45 |
|
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: 150.48 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkELRKKRRRI 82
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGCLGYKTTlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVP--------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLH-QVEtAIDYSDRIIGVNSGKIV 226
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVE-AMTMADRIAVMNDGQIQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-237 |
4.74e-45 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 150.66 E-value: 4.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRRI 82
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgclgykttLSGAAGLYREEEKEQafdlIEKV-----DLSAFAYTRCDELSGGQKQRVGI 157
Cdd:cd03224 78 GYVPEGRRIFPELTVEENL----------LLGAYARRRAKRKAR----LERVyelfpRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-175 |
5.37e-45 |
|
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: 148.18 E-value: 5.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRIGMIFQHYNLVSRLTVI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT---DDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 ENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD----ELSGGQKQRVGIARALMQNPALILCDEPI 174
Cdd:pfam00005 78 ENLRLGLLLK--------GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 488231729 175 A 175
Cdd:pfam00005 150 A 150
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-234 |
7.29e-45 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 154.24 E-value: 7.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 15 GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIrFEDRE--MNELKRKELRKKRRRIGMIFQHYNLV 92
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQI-FIDGEniMKQSPVELREVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 SRLTVIENVlhgCLGYKTtlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDE 172
Cdd:TIGR01186 84 PHMTILQNT---SLGPEL-----LGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 173 PIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-226 |
9.96e-45 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 149.78 E-value: 9.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKR 79
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRLTVIENVlhgclgyKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNV-------QMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQvETAIDYSDRIIGVNSGKIV 226
Cdd:TIGR02982 155 ALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-234 |
1.99e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 149.90 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKR--- 79
Cdd:PRK11264 4 IEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 --RRIGMIFQHYNLVSRLTVIENVLHGCLGYKttlsgaaGLYREEEKEQAFDLIEKVDLSA--FAYTRcdELSGGQKQRV 155
Cdd:PRK11264 83 lrQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-------GEPKEEATARARELLAKVGLAGkeTSYPR--RLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-178 |
2.02e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.00 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGNQ---ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFE---------DRemn 68
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgpgaDR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 69 elkrkelrkkrrriGMIFQHYNLVSRLTVIENVlhgCLGYKTtlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELS 148
Cdd:COG4525 79 --------------GVVFQKDALLPWLNVLDNV---AFGLRL-----RGVPKAERRARAEELLALVGLADFARRRIWQLS 136
|
170 180 190
....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-225 |
2.43e-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: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS---AMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHynlvSRL---TVIENVLHgclgykttlsgaAGLYREEE--KEQAFDLIEKVDLSA-FAYTRCDELSGGQKQRVG 156
Cdd:COG4619 77 AYVPQE----PALwggTVRDNLPF------------PFQLRERKfdRERALELLERLGLPPdILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-226 |
4.02e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.03 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN----------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELK 71
Cdd:COG4608 7 LLEVRDLKKHFPVRGglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQH-Y-NLVSRLTV---IENVL--HGCLGykttlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRC 144
Cdd:COG4608 87 GRELRPLRRRMQMVFQDpYaSLNPRMTVgdiIAEPLriHGLAS------------KAERRERVAELLELVGLRPEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 -DELSGGQKQRVGIARALMQNPALILCDEPIASLDpKS--AKtIMDYLKRITNELAITCLV---NLHQVEtaidY-SDRI 217
Cdd:COG4608 155 pHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSiqAQ-VLNLLEDLQDELGLTYLFishDLSVVR----HiSDRV 228
|
....*....
gi 488231729 218 IGVNSGKIV 226
Cdd:COG4608 229 AVMYLGKIV 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-238 |
5.31e-42 |
|
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: 150.29 E-value: 5.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS---DLDPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHynlvSRL---TVIENVLhgclgykttlsgaagLYR----EEEKEQAfdlIEKVDLSAFAY-------TRCDE-- 146
Cdd:COG4988 414 AWVPQN----PYLfagTIRENLR---------------LGRpdasDEELEAA---LEAAGLDEFVAalpdgldTPLGEgg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 --LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGK 224
Cdd:COG4988 472 rgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLAL-LAQADRILVLDDGR 548
|
250
....*....|....
gi 488231729 225 IVFEGRPYELTKEK 238
Cdd:COG4988 549 IVEQGTHEELLAKN 562
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-229 |
1.40e-41 |
|
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: 141.26 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKElrkkrrrI 82
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHgclgykttLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVY--------LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDylkrITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKD----VIRELAragKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-234 |
1.91e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.85 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRR 80
Cdd:PRK13635 5 IIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHY-NLVSRLTVIENVLHGclgykttLSGaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:PRK13635 82 QVGMVFQNPdNQFVGATVQDDVAFG-------LEN-IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-234 |
2.72e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.86 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR-- 80
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 --------RIGMIFQHYNLVSRLTVIENVLHGCLgykTTLsgaaGLYREEEKEQAFDLIEKVDLsafaYTRCD----ELS 148
Cdd:COG4598 88 rqlqrirtRLGMVFQSFNLWSHMTVLENVIEAPV---HVL----GRPKAEAIERAEALLAKVGL----ADKRDaypaHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPksaKTIMDYLKRITnELAI---TCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKVMR-DLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
....*....
gi 488231729 226 VFEGRPYEL 234
Cdd:COG4598 233 EEQGPPAEV 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
5.84e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 141.75 E-value: 5.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNeLKRKELRKKRRR 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQhyNLVSRL---TVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:PRK13639 80 VGIVFQ--NPDDQLfapTVEEDVAFGPLNL--------GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEk 238
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD- 227
|
....*...
gi 488231729 239 IETIYQSK 246
Cdd:PRK13639 228 IETIRKAN 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-229 |
7.52e-41 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 139.25 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGnQALQDISFSLEKGEFVsIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelKRKELRKKRRRI 82
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD----VLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIEnvlhgCLGYKTTLSGAAGlyrEEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03264 75 GYLPQEFGVYPNFTVRE-----FLDYIAWLKGIPS---KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAItcLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-224 |
8.52e-41 |
|
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: 137.90 E-value: 8.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNG-NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRR 81
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR---DLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVlhgclgykttlsgaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARAL 161
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI---------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETAIDYsDRIIGVNSGK 224
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-238 |
1.76e-40 |
|
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: 147.67 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ--- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENvlhgclgykttLSGAAGLYREEEKEQAfdlIEKVDLSAFA-------YTRCDE----LSGG 150
Cdd:COG2274 551 IGVVLQDVFLFSG-TIREN-----------ITLGDPDATDEEIIEA---ARLAGLHDFIealpmgyDTVVGEggsnLSGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVETaIDYSDRIIGVNSGKIVFEGR 230
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLST-IRLADRIIVLDKGRIVEDGT 692
|
....*...
gi 488231729 231 PYELTKEK 238
Cdd:COG2274 693 HEELLARK 700
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-224 |
1.85e-40 |
|
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: 136.61 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRIG 83
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQhynlvsrltvienvlhgclgykttlsgaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARALMQ 163
Cdd:cd00267 77 YVPQ-----------------------------------------------------------LSGGQRQRVALARALLL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGK 224
Cdd:cd00267 98 NPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-237 |
2.40e-40 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 142.14 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrr 80
Cdd:PRK10851 1 MSIEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rIGMIFQHYNLVSRLTVIENVLHGClgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK10851 76 -VGFVFQHYALFRHMTVFDNIAFGL----TVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-244 |
4.33e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 138.75 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRR 80
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA---DWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK13548 77 RRAVLPQHSSLSFPFTVEEVVAMGRAPH--------GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 161 LMQ------NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE- 233
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEv 228
|
250
....*....|.
gi 488231729 234 LTKEKIETIYQ 244
Cdd:PRK13548 229 LTPETLRRVYG 239
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-235 |
6.74e-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: 6.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNG-NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKkrrr 81
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENV-LHGCLgykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLrFYARL---------KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAItcLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELT 235
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-238 |
1.27e-39 |
|
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: 143.75 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRR 81
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR---DLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVLHGClgykttlsGAAGlyrEEEKEQAfdlIEKVDLSAFA-------YTRCDE----LSGG 150
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLAR--------PDAT---DEELWAA---LERVGLGDWLaalpdglDTWLGEggrrLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE---LAITclvnlHQvETAIDYSDRIIGVNSGKIVF 227
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtvLLIT-----HR-LAGLERMDRILVLEDGRIVE 549
|
250
....*....|.
gi 488231729 228 EGRPYELTKEK 238
Cdd:COG4987 550 QGTHEELLAQN 560
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
1.31e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 137.04 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRR 80
Cdd:COG0410 2 PMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAglyREEEKEQAFDLIEKvdLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLL---LGAYARRDRAE---VRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLV---NLHQvetAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLveqNARF---ALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-196 |
1.79e-39 |
|
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: 139.03 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEA---DSGTIRFEDREMNELKRKEL 75
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKK-RRRIGMIFQH-YN-LVSRLTVIENV-----LHGclgykttlsgaaGLYREEEKEQAFDLIEKVDLSAfAYTRCD-- 145
Cdd:COG0444 81 RKIrGREIQMIFQDpMTsLNPVMTVGDQIaeplrIHG------------GLSKAEARERAIELLERVGLPD-PERRLDry 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488231729 146 --ELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNEL 196
Cdd:COG0444 148 phELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-226 |
4.47e-39 |
|
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: 135.25 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQA---LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRF---------ED----- 64
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaldEDararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 65 REMNelkrkelrkkrrrIGMIFQHYNLVSRLTVIENVLHGCLgykttLSGAAglyreEEKEQAFDLIEKVDLSAfaytRC 144
Cdd:COG4181 88 RARH-------------VGFVFQSFQLLPTLTALENVMLPLE-----LAGRR-----DARARARALLERVGLGH----RL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 D----ELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAiDYSDRIIGV 220
Cdd:COG4181 141 DhypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRL 219
|
....*.
gi 488231729 221 NSGKIV 226
Cdd:COG4181 220 RAGRLV 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-218 |
4.91e-39 |
|
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: 134.67 E-value: 4.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 5 VKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRE-MNELKRKELRKKRRRIG 83
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtPPLNSKKASKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQHYNLVSRLTVIENVLHGCLGYKTTlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ 163
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLS--------KKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAiDYSDRII 218
Cdd:TIGR03608 152 PPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA-KQADRVI 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-237 |
1.01e-38 |
|
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: 137.24 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 34 IIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRIGMIFQHYNLVSRLTVIENVLHGClgykttls 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 114 GAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRIT 193
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488231729 194 NELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
1.13e-38 |
|
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: 133.76 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKkrr 80
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rIGMIFqHYN-LVSRLTVIENvlhgclgykttLSGAAGLY-REEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:COG4133 77 -LAYLG-HADgLKPELTVREN-----------LRFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|...
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKR 191
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-228 |
1.35e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.21 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRkelrkk 78
Cdd:COG1101 2 LELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrigmiFQHYNLVSR------------LTVIENVL-----HGCLGYKTTLSGAaglYREEEKEQ--AFDL-IE-----K 133
Cdd:COG1101 76 -------YKRAKYIGRvfqdpmmgtapsMTIEENLAlayrrGKRRGLRRGLTKK---RRELFRELlaTLGLgLEnrldtK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 134 VDLsafaytrcdeLSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDY 213
Cdd:COG1101 146 VGL----------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDY 215
|
250
....*....|....*
gi 488231729 214 SDRIIGVNSGKIVFE 228
Cdd:COG1101 216 GNRLIMMHEGRIILD 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
1.55e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 135.25 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHY-NLVSRLTVIENVLHGCLGykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK13647 82 GLVFQDPdDQVFSSTVWDDVAFGPVN--------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-229 |
3.41e-38 |
|
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: 132.80 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 21 DISFSLEkGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELR-KKRRRIGMIFQHYNLVSRLTVIE 99
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLpPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 100 NVlhgCLGYKttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDP 179
Cdd:cd03297 95 NL---AFGLK-------RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488231729 180 KSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-234 |
6.37e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.62 E-value: 6.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIrFEDREmnelKRKELRKKRRRI 82
Cdd:PRK11432 7 VVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGE----DVTHRSIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVlhgclGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENV-----GYGLKMLGVP---KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-234 |
6.40e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 139.53 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED---REMNelkrkeLRKKR 79
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLT------LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRlTVIENVLHGCLGykttlsgaaglYREEEKEQAfdlIEKVDLSAFA-------YTRCDE----LS 148
Cdd:COG1132 414 RQIGVVPQDTFLFSG-TIRENIRYGRPD-----------ATDEEVEEA---AKAAQAHEFIealpdgyDTVVGErgvnLS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE---LAITclvnlHQVETAIDySDRIIGVNSGKI 225
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrttIVIA-----HRLSTIRN-ADRILVLDDGRI 552
|
....*....
gi 488231729 226 VFEGRPYEL 234
Cdd:COG1132 553 VEQGTHEEL 561
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-239 |
8.25e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 138.24 E-value: 8.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRE---------MNelk 71
Cdd:COG3845 4 PALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsprdaIA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 rkelrkkrRRIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAGlyREEEKEQAFDLIEK----VDLSAfaytRCDEL 147
Cdd:COG3845 80 --------LGIGMVHQHFMLVPNLTVAENIV---LGLEPTKGGRLD--RKAARARIRELSERygldVDPDA----KVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQNPA-LILcDEPIASLDPKSAKTIMDYLKRITNE----LAITclvnlHQVETAIDYSDRIIGVNS 222
Cdd:COG3845 143 SVGEQQRVEILKALYRGARiLIL-DEPTAVLTPQEADELFEILRRLAAEgksiIFIT-----HKLREVMAIADRVTVLRR 216
|
250
....*....|....*..
gi 488231729 223 GKIVFEGRPYELTKEKI 239
Cdd:COG3845 217 GKVVGTVDTAETSEEEL 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-229 |
1.15e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.70 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkelRKKRRRI 82
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GmifqhY-----NLVSRLTVIEnvlhgCLGYKTTLsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:COG4152 74 G-----YlpeerGLYPKMKVGE-----QLVYLARL---KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKritnELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIR----ELAakgTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-234 |
1.42e-37 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 131.34 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGT-------IRFEDREMNELkrkel 75
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREVRRR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 rkkrrrIGMIFQHYNLVSRLTVIENV-LHGCLgykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQR 154
Cdd:cd03265 75 ------IGIVFQDLSVDDELTGWENLyIHARL---------YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-244 |
1.54e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.16 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRrr 81
Cdd:COG4559 1 MLEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIFQHYNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:COG4559 78 -AVLPQHSSLAFPFTVEEVVALGRAPH--------GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQ-------NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVnLHQVETAIDYSDRIIGVNSGKIVFEGRPYE- 233
Cdd:COG4559 149 AQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAV-LHDLNLAAQYADRILLLHQGRLVAQGTPEEv 227
|
250
....*....|.
gi 488231729 234 LTKEKIETIYQ 244
Cdd:COG4559 228 LTDELLERVYG 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-236 |
3.08e-37 |
|
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: 130.92 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrrrI 82
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-----I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGcLGYKTTLsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYG-LKKRKVD-------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTK 236
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-179 |
4.84e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 134.08 E-value: 4.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGE-FVsIIGPSGAGKSTILRTINRLIEADSGTIRFED-----------REMNELKrkelrkkrrrIGMI 85
Cdd:COG4175 42 GVNDASFDVEEGEiFV-IMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGeditklskkelRELRRKK----------MSMV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 86 FQHYNLVSRLTVIENVlhgclGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNP 165
Cdd:COG4175 111 FQHFALLPHRTVLENV-----AFGLEIQGVP---KAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDP 182
|
170
....*....|....
gi 488231729 166 ALILCDEPIASLDP 179
Cdd:COG4175 183 DILLMDEAFSALDP 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-210 |
1.19e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.17 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 -RRRIGMIFQHYNLVSRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK11629 85 rNQKLGFIYQFHHLLPDFTALENVAMPLL--------IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETA 210
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
1.63e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 130.98 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIR--FEDREMNELKRKE 74
Cdd:PRK13651 1 MQIKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 75 LRKKRRR-------------------IGMIFQ--HYNLVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEK 133
Cdd:PRK13651 81 EKVLEKLviqktrfkkikkikeirrrVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM--------GVSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 134 VDL-------SAFaytrcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQ 206
Cdd:PRK13651 152 VGLdesylqrSPF------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488231729 207 VETAIDYSDRIIGVNSGKIVFEGRPYELTKEK---IETIYQSKKLLV 250
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNkflIENNMEPPKLLN 271
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-226 |
2.68e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 135.62 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQA---LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRR-IGMIFQHYNLVSRLTVIENVlhgclgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNV--------EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDySDRIIGVNSGKIV 226
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-211 |
3.02e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 128.66 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKElrkkrrr 81
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIFQHYNLVSRLTVIENVLHGClgykttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGL--------QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARAL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAI 211
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-234 |
6.27e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 131.11 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRkkrrr 81
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKttlsgaagLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDK--------LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 162 MQNPALILCDEPIASLDPK----SAKTIMDYLKRItnelAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-234 |
6.59e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.16 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTI----------RFEDREMNELKR 72
Cdd:PRK10619 6 LNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 73 KELRKKRRRIGMIFQHYNLVSRLTVIENVLHGCLGykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQ 151
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQ-------VLGLSKQEARERAVKYLAKVGIDERAQGKYPvHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 152 KQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRP 231
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
...
gi 488231729 232 YEL 234
Cdd:PRK10619 237 EQL 239
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-239 |
6.74e-36 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 129.05 E-value: 6.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 10 KTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkRKELRKKRRRIGMIFQHY 89
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV----VREPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 90 NLVSRLTVIEN-VLHGCLgykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALI 168
Cdd:TIGR01188 76 SVDEDLTGRENlEMMGRL---------YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 169 LCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELtKEKI 239
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL-KRRL 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-229 |
2.38e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.56 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKk 78
Cdd:cd03266 1 MITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrIGMIFQHYNLVSRLTVIENVLHgclgykttLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:cd03266 80 ---LGFVSDSTGLYDRLTARENLEY--------FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-223 |
2.67e-35 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 125.66 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELrkkrrrigMIFQHYNLVSRLTVI 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 ENVlhgCLGYKTTLSGAaglyREEEKEQAFD-LIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASL 177
Cdd:TIGR01184 73 ENI---ALAVDRVLPDL----SKSERRAIVEeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488231729 178 DPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSG 223
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-238 |
7.54e-35 |
|
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: 124.26 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRIG 83
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR---DISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQHYNLVSRlTVIENVLHGCLGYKttlsgaaglyREEEKE-----QAFDLIEKV--DLSAFAYTRCDELSGGQKQRVG 156
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNAT----------DEEVIEaakeaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYELTK 236
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLST-IKNADKILVLDDGKIIEEGTHDELLA 226
|
..
gi 488231729 237 EK 238
Cdd:cd03254 227 KK 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-234 |
8.53e-35 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 124.19 E-value: 8.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMneLKRKELRKKRRRI 82
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLhgCLGYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03218 78 GYLPQEASIFRKLTVEENIL--AVLEIRGLS------KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 163 QNPALILCDEPIASLDPKSAKTImdylKRITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDI----QKIIKILKdrgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
1.31e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.35 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRr 81
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRES- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHY-NLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK13636 84 VGMVFQDPdNQLFSASVYQDVSFGAVNL--------KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEK 238
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-238 |
1.42e-34 |
|
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: 123.88 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRRI 82
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRlTVIENVLHGCLGykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAY-TRCDE----LSGGQKQRVGI 157
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRPD--------ATDEEVIEAAKAAQIHDKIMRFPDGYdTIVGErglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
.
gi 488231729 238 K 238
Cdd:cd03253 226 G 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-229 |
2.00e-34 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 122.71 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkELRKKRRRI 82
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEqafdLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLL--------GIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-234 |
6.68e-34 |
|
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: 125.21 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVkNITKTYpnGNQALqDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRF----------------ED 64
Cdd:COG4148 1 MMLEV-DFRLRR--GGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsargiflppHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 65 RemnelkrkelrkkrrRIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAGLYREEekeqafdLIEKVDLSAFAYTRC 144
Cdd:COG4148 77 R---------------RIGYVFQEARLFPHLSVRGNLL---YGRKRAPRAERRISFDE-------VVELLGIGHLLDRRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGK 224
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
250
....*....|
gi 488231729 225 IVFEGRPYEL 234
Cdd:COG4148 212 VVASGPLAEV 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-229 |
9.37e-34 |
|
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: 121.06 E-value: 9.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSL-----------EKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRIGMIF 86
Cdd:cd03298 2 RLDKIRFSYgeqpmhfdltfAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----TAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 87 QHYNLVSRLTVIENVlhgclgyktTLSGAAGLYREEEKEQAFDLI-EKVDLSAFAYTRCDELSGGQKQRVGIARALMQNP 165
Cdd:cd03298 77 QENNLFAHLTVEQNV---------GLGLSPGLKLTAEDRQAIEVAlARVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 166 ALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-237 |
1.09e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 122.89 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ-----ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDreMNELKRKELR 76
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRRIGMIFQHY-NLVSRLTVIENVLHGclgykttlSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRV 155
Cdd:PRK13633 82 DIRNKAGMVFQNPdNQIVATIVEEDVAFG--------PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYELT 235
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
..
gi 488231729 236 KE 237
Cdd:PRK13633 233 KE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-234 |
1.13e-33 |
|
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: 124.45 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 7 NITKTYpnGNQALqDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR-RIGMI 85
Cdd:TIGR02142 4 RFSKRL--GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKrRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 86 FQHYNLVSRLTVIENVLHGclgYKTTlsgaaglyREEEKEQAFD-LIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQN 164
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYG---MKRA--------RPSERRISFErVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 165 PALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-180 |
1.26e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRR 80
Cdd:COG1129 3 PLLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVlhgCLGyktTLSGAAGLY-REEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENI---FLG---REPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180
....*....|....*....|.
gi 488231729 160 ALMQNPALILCDEPIASLDPK 180
Cdd:COG1129 154 ALSRDARVLILDEPTASLTER 174
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-244 |
1.64e-33 |
|
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: 121.34 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLI-EADSGTIR-----------FEDREMn 68
Cdd:COG1119 2 PLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRlfgerrggedvWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 69 elkrkelrkkrrrIGMI--FQHYNLVSRLTVIENVLHGclgykttLSGAAGLYRE---EEKEQAFDLIEKVDLSAFAYTR 143
Cdd:COG1119 80 -------------IGLVspALQLRFPRDETVLDVVLSG-------FFDSIGLYREptdEQRERARELLELLGLAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 144 CDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAIT-CLVNlHQVETAIDYSDRIIGVNS 222
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTlVLVT-HHVEEIPPGITHVLLLKD 218
|
250 260
....*....|....*....|...
gi 488231729 223 GKIVFEGRPYE-LTKEKIETIYQ 244
Cdd:COG1119 219 GRVVAAGPKEEvLTSENLSEAFG 241
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-225 |
5.93e-33 |
|
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: 119.20 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 23 SFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRIGMIFQHYNLVSRLTVIENVl 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-----TGLAPYQRPVSMLFQENNLFAHLTVRQNI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 103 hgCLGYKTTLSGAAglyreEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSA 182
Cdd:TIGR01277 92 --GLGLHPGLKLNA-----EQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488231729 183 KTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-234 |
5.98e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 122.64 E-value: 5.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkELRKKRRRI 82
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-----ELEPADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENvlhgcLGYKTTLSGAAGLYREEEKEQAFDLIEkvdLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN-----MAYGLKIRGMPKAEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLH-QVEtAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdQVE-AMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-238 |
6.40e-33 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 119.57 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPN--GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRR 81
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR---DLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVLHGclgykttLSGAAGLYREEEKEQAF--DLIEKvdLSAFAYTRCDE----LSGGQKQRV 155
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRYG-------KPDATDEEVEEAAKKANihDFIMS--LPDGYDTLVGErgsqLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITneLAITCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYELT 235
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLST-IRNADLIAVLQNGQVVEQGTHDELM 225
|
...
gi 488231729 236 KEK 238
Cdd:cd03249 226 AQK 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-242 |
7.39e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.92 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnELKRKELR 76
Cdd:PRK13637 1 MSIKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRRIGMIFQH--YNLVSRlTVIENVLHGclgyKTTLsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD--ELSGGQK 152
Cdd:PRK13637 80 DIRKKVGLVFQYpeYQLFEE-TIEKDIAFG----PINL----GLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 153 QRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPY 232
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
250
....*....|..
gi 488231729 233 ELTKE--KIETI 242
Cdd:PRK13637 231 EVFKEveTLESI 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
7.47e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.90 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM-NELKRKEL 75
Cdd:PRK13634 1 MDITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKKRRRIGMIFQ--HYNLVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQK 152
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNF--------GVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 153 QRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPY 232
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
..
gi 488231729 233 EL 234
Cdd:PRK13634 232 EI 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
1.22e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYP----------NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAdSGTIRFEDREMNELK 71
Cdd:COG4172 275 LLEARDLKVWFPikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQH-YN-LVSRLTVIENVLHGCLGYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRC-DELS 148
Cdd:COG4172 354 RRALRPLRRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGLS------AAERRARVAEALEEVGLDPAARHRYpHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLV---NLHQVEtAIdySDRIIGVNSGKI 225
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFishDLAVVR-AL--AHRVMVMKDGKV 504
|
....
gi 488231729 226 VFEG 229
Cdd:COG4172 505 VEQG 508
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-234 |
1.73e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrr 80
Cdd:COG1137 2 MTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rI-----------GM--------IFQhynlvsRLTVIENVLhgclgykttlsgAA----GLYREEEKEQAFDLIEKVDLS 137
Cdd:COG1137 67 -IthlpmhkrarlGIgylpqeasIFR------KLTVEDNIL------------AVlelrKLSKKEREERLEELLEEFGIT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 138 AFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTImdylKRITNELA---ITCLVNLHQVETAIDYS 214
Cdd:COG1137 128 HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADI----QKIIRHLKergIGVLITDHNVRETLGIC 203
|
250 260
....*....|....*....|..
gi 488231729 215 DR--IIgvNSGKIVFEGRPYEL 234
Cdd:COG1137 204 DRayII--SEGKVLAEGTPEEI 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-234 |
1.97e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.94 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:PRK11300 5 LLSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMI--FQHYNLVSRLTVIENVL---HGCLgyKTTLsgAAGL-----YREEEKE---QAFDLIEKVDLSAFAYTRCDELS 148
Cdd:PRK11300 81 -GVVrtFQHVRLFREMTVIENLLvaqHQQL--KTGL--FSGLlktpaFRRAESEaldRAATWLERVGLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFE 228
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
....*.
gi 488231729 229 GRPYEL 234
Cdd:PRK11300 236 GTPEEI 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-218 |
2.19e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 123.55 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRRI 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL---ADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRlTVIENVLHGCLGYKttlsgAAGLYREEEKEQAFDLIEkvDLSAFAYTRCDE----LSGGQKQRVGIA 158
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDAS-----DAEIREALERAGLDEFVA--ALPQGLDTPIGEggagLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNelAITCLVNLHQVETAIDYsDRII 218
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIV 527
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
2-234 |
3.03e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 117.76 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgnQALQdISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRfedreMNELKRKELRKKRRR 81
Cdd:PRK10771 1 MLKLTDITWLYHH--LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-----LNGQDHTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENV---LHGclGYKTTlsgaaglyrEEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIglgLNP--GLKLN---------AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 159 RALM-QNPALILcDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK10771 142 RCLVrEQPILLL-DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-234 |
6.40e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.91 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM-NELKRKELRKKRRRIGMIFQHYNLVSRLT 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 97 VIENVLHGClgykttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIAS 176
Cdd:PRK10070 123 VLDNTAFGM--------ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 177 LDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-226 |
8.17e-32 |
|
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: 115.82 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkeLRKKRRRIG 83
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQH--YNLVSRlTVIENVLhgcLGYKTTlsgaaglyrEEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELL---LGLKEL---------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-179 |
2.19e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.48 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNG--------NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRK 73
Cdd:COG4167 4 LLEVRNLSKTFKYRtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 74 ELRKKrrrIGMIFQHYN--LVSRLTvIENVLHGCLGYKTTLSGaaglyrEEEKEQAFDLIEKVDLSA-FAYTRCDELSGG 150
Cdd:COG4167 84 YRCKH---IRMIFQDPNtsLNPRLN-IGQILEEPLRLNTDLTA------EEREERIFATLRLVGLLPeHANFYPHMLSSG 153
|
170 180
....*....|....*....|....*....
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDP 179
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDM 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-181 |
2.33e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 115.22 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ------ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRF------------E 63
Cdd:COG4778 4 LLEVENLSKTFTLHLQggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdggwvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 64 DREMnelkrkeLRKKRRRIGMIFQHYNLVSRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDL-----SA 138
Cdd:COG4778 84 PREI-------LALRRRTIGYVSQFLRVIPRVSALDVVAEPLL--------ERGVDREEARARARELLARLNLperlwDL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488231729 139 FAYTrcdeLSGGQKQRVGIARALMQNPALILCDEPIASLDPKS 181
Cdd:COG4778 149 PPAT----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-234 |
2.46e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 118.59 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 6 KNITKTYpnGNQAL-QDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkELRKKRRRIGM 84
Cdd:PRK11000 7 RNVTKAY--GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 85 IFQHYNLVSRLTVIENVlhgCLGYKttLSGAAGLYREEEKEQAFDLIEkvdLSAFAYTRCDELSGGQKQRVGIARALMQN 164
Cdd:PRK11000 80 VFQSYALYPHLSVAENM---SFGLK--LAGAKKEEINQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 165 PALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLH-QVEtAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-239 |
3.01e-31 |
|
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: 114.93 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRrrI 82
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAG--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLhgclgykttlSGAAGLYREEEK--EQAFDLIEKvdLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLL----------TGLAALPRRSRKipDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-234 |
9.25e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQ---ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKK 78
Cdd:PRK13650 4 IIEVKNLTFKY-KEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrIGMIFQHY-NLVSRLTVIENVLHGcLGYKttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK13650 83 ---IGMVFQNPdNQFVGATVEDDVAFG-LENK-------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVEtAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-226 |
9.26e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.82 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVlhgclGYKTTLSGAAGlyrEEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNV-----AIPLIIAGASG---DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-247 |
1.32e-30 |
|
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: 118.75 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRL--IEADSGTIRF------------------ 62
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 63 ------------EDREMNELKRKELRKKRRRIGMIFQH-YNLVSRLTVIENVLHGC--LGYKttlsGAAGLYReeekeqA 127
Cdd:TIGR03269 80 epcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALeeIGYE----GKEAVGR------A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 128 FDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQV 207
Cdd:TIGR03269 150 VDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488231729 208 ETAIDYSDRIIGVNSGKIVFEGRPYELTKEKIETIYQSKK 247
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEK 269
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-243 |
2.47e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.06 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRrr 81
Cdd:PRK10895 3 TLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLhgclgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLM-------AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSA---KTIMDYLKritnELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKE 237
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVidiKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDE 228
|
....*.
gi 488231729 238 KIETIY 243
Cdd:PRK10895 229 HVKRVY 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-229 |
2.54e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 112.30 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNG-NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRR 81
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI---RQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVLHGCLGYKT-------TLSGAAGLYREEEKEQAFDLIEkvdlsafaytRCDELSGGQKQR 154
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGAPLADDerilraaELAGVTDFVNKHPNGLDLQIGE----------RGRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVeTAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-243 |
3.13e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 20 QDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrrIGMIFQHYNLVSRLTVIE 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR---IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 100 NVLHGCLGYKTTLSgaagLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDP 179
Cdd:PRK10253 101 LVARGRYPHQPLFT----RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 180 KSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL-TKEKIETIY 243
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvTAELIERIY 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-238 |
3.17e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYPNG-NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrrI 82
Cdd:PRK13632 9 KVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHY-NLVSRLTVIENVLHGCLGYKTTlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAFGLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYELTKEK 238
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
3.29e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.93 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFedreMNELKRKELRKKRR 80
Cdd:PRK13536 40 VAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLhgclgyktTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLL--------VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITnELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-206 |
3.97e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.82 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD-----SGTIRFEDREMNeLKRKELRK 77
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIY-DPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVSrLTVIENVLHGC--LGYK----------TTLSGAAgLYrEEEKeqafdliEKVDLSAFAytrcd 145
Cdd:COG1117 90 LRRRVGMVFQKPNPFP-KSIYDNVAYGLrlHGIKskseldeiveESLRKAA-LW-DEVK-------DRLKKSALG----- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 146 eLSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAItCLV--NLHQ 206
Cdd:COG1117 155 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI-VIVthNMQQ 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-238 |
4.00e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.77 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGN----QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELR 76
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKR-RRIGMIFQH-YNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQKQ 153
Cdd:PRK13641 81 KKLrKKVSLVFQFpEAQLFENTVLKDVEFGPKNF--------GFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQVETAIDYSDRIIGVNSGKIVFEGRPYE 233
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT-HNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
....*
gi 488231729 234 LTKEK 238
Cdd:PRK13641 232 IFSDK 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-225 |
6.17e-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: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQA-LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkelrkkrrr 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 igmifqhynlvsrlTVIENVLHGCLGYkttlsgaaglyreeekeqafdLIEKVDLsaFAYTRCDE-LSGGQKQRVGIARA 160
Cdd:cd03246 68 --------------QWDPNELGDHVGY---------------------LPQDDEL--FSGSIAENiLSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQVETaIDYSDRIIGVNSGKI 225
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIA-HRPET-LASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-226 |
7.07e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.44 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRRI 82
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--FASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQhynlvsrltvienvlhgclgykttlsgaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARALM 162
Cdd:cd03216 78 AMVYQ-----------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-238 |
7.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 7.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGN----QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRE-MNELKRKEL 75
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKKRRRIGMIFQHYNlvSRL---TVIENVLHGCLGYKTTLsgaaglyrEEEKEQAFDLI-------EKVDLSAFaytrcd 145
Cdd:PRK13646 81 RPVRKRIGMVFQFPE--SQLfedTVEREIIFGPKNFKMNL--------DEVKNYAHRLLmdlgfsrDVMSQSPF------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 146 ELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
250
....*....|...
gi 488231729 226 VFEGRPYELTKEK 238
Cdd:PRK13646 225 VSQTSPKELFKDK 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-250 |
1.73e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.64 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRK 77
Cdd:PRK13631 21 ILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRR-------------IGMIFQ--HYNLVsRLTVIENVLHGCLgykttlsgAAGLYREEEKEQAFDLIEKVDL-SAFAY 141
Cdd:PRK13631 101 TNPYskkiknfkelrrrVSMVFQfpEYQLF-KDTIEKDIMFGPV--------ALGVKKSEAKKLAKFYLNKMGLdDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 142 TRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVN 221
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMD 250
|
250 260
....*....|....*....|....*....
gi 488231729 222 SGKIVFEGRPYELTKEKieTIYQSKKLLV 250
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQ--HIINSTSIQV 277
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-240 |
1.91e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.17 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRR 80
Cdd:PRK09536 2 PMIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE---ALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAaglyrEEEKEQAFD-LIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTW-----TETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKEK 238
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADvLTADT 231
|
..
gi 488231729 239 IE 240
Cdd:PRK09536 232 LR 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-234 |
2.07e-29 |
|
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: 110.40 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPN-GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRR 81
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVLHGCLGykttlSGAAGLYREEEKEQAFDLIEKVD--LSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRPG-----ATREEVEEAARAANAHEFIMELPegYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 160 ALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLST-IENADRIVVLEDGKIVERGTHEEL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-229 |
4.03e-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: 108.41 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN-----QALQDISFSLEKGEFVSIIGPSGAGKSTILRTIN--RLIEADSGTIRFEDREMnelkrkEL 75
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKKRRRIGMIFQHynlvsrltvieNVLHGCLGYKTTLSGAAGLyreeekeqafdliekvdlsafaytRCdeLSGGQKQRV 155
Cdd:cd03213 78 RSFRKIIGYVPQD-----------DILHPTLTVRETLMFAAKL------------------------RG--LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYS-DRIIGVNSGKIVFEG 229
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-234 |
1.22e-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: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYP-NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRR 80
Cdd:TIGR02203 330 DVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL---ADYTLASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRlTVIENVlhgclGYkttlsGAAGLYREEEKEQAF------DLIEKVDLSAfaYTRCDE----LSGG 150
Cdd:TIGR02203 407 QVALVSQDVVLFND-TIANNI-----AY-----GRTEQADRAEIERALaaayaqDFVDKLPLGL--DTPIGEngvlLSGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 151 QKQRVGIARALMQN-PALILcDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKIVFEG 229
Cdd:TIGR02203 474 QRQRLAIARALLKDaPILIL-DEATSALDNESERLVQAALERLMQGR--TTLVIAHRLST-IEKADRIVVMDDGRIVERG 549
|
....*
gi 488231729 230 RPYEL 234
Cdd:TIGR02203 550 THNEL 554
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-225 |
1.44e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.61 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRF------EDREmnelkrkelr 76
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplaEARE---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 kkrrRIGMIFQHYNLVSRLTVIENVlhgCLGYKttlsgaaGLYREeekeQAFDLIEKVDLSAFAYTRCDELSGGQKQRVG 156
Cdd:PRK11247 82 ----DTRLMFQDARLLPWKKVIDNV---GLGLK-------GQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-179 |
4.65e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.03 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDREMNELKRKELRkkr 79
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQHYNLVSRLTVIENVLHGClgykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:COG4136 78 --IGILFQDDLLFPHLSVGENLAFAL---------PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180
....*....|....*....|
gi 488231729 160 ALMQNPALILCDEPIASLDP 179
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDA 166
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-175 |
6.45e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 106.74 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMneLKRKELRKKRR 80
Cdd:COG4674 9 PILYVEDLTVSF-DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL--TGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAGLYR---EEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:COG4674 86 GIGRKFQKPTVFEELTVFENLE---LALKGDRGVFASLFArltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEI 162
|
170
....*....|....*...
gi 488231729 158 ARALMQNPALILCDEPIA 175
Cdd:COG4674 163 GMLLAQDPKLLLLDEPVA 180
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-231 |
7.14e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.08 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN--------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRK 73
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 74 ELRKKRRRIGMIFQH----YNlvSRLTVIEnVLHGCLGYKTTLSGAAGLYREEEkeqafdLIEKVDLSA-FAYTRCDELS 148
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsisaVN--PRKTVRE-IIREPLRHLLSLDKAERLARASE------MLRAVDLDDsVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVfE 228
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV-E 232
|
...
gi 488231729 229 GRP 231
Cdd:PRK10419 233 TQP 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-244 |
1.12e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.25 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYpnGNQA-LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKR 79
Cdd:PRK11231 1 MTLRTENLTVGY--GTKRiLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS---MLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRLTVIENVLHGCLGYkttLSGAAGLYREEEK--EQAfdlIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYGRSPW---LSLWGRLSAEDNArvNQA---MEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDyLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTK 236
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvMTP 228
|
....*...
gi 488231729 237 EKIETIYQ 244
Cdd:PRK11231 229 GLLRTVFD 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-234 |
1.59e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.48 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNItKTY-------------PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM 67
Cdd:PRK15079 7 VLLEVADL-KVHfdikdgkqwfwqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 68 NELKRKELRKKRRRIGMIFQH--YNLVSRLTVIENVLHGCLGYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRC- 144
Cdd:PRK15079 86 LGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYHPKLS------RQEVKDRVKAMMLKVGLLPNLINRYp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIgvnsgk 224
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL------ 233
|
250
....*....|
gi 488231729 225 IVFEGRPYEL 234
Cdd:PRK15079 234 VMYLGHAVEL 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-196 |
2.63e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 109.23 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRRI 82
Cdd:PRK11288 5 LSFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTVIENVLHGclgyktTLSGAAGLYREEE-KEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG------QLPHKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLdpkSAKTImDYLKRITNEL 196
Cdd:PRK11288 156 ARNARVIAFDEPTSSL---SAREI-EQLFRVIREL 186
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-210 |
2.75e-27 |
|
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: 103.66 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 12 YPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRrIGMIFQHYN- 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQR-VGLVFQDPDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 91 -LVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALIL 169
Cdd:TIGR01166 80 qLFAA-DVDQDVAFGPLNL--------GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488231729 170 CDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETA 210
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-236 |
3.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQA--LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKr 79
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQH-YNLVSRLTVIENVLHGclgykttLSGAAGLYrEEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:PRK13648 85 --IGIVFQNpDNQFVGSIVKYDVAFG-------LENHAVPY-DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYELTK 236
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-231 |
3.88e-27 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 104.11 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNElkrkelrkkrrr 81
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGmifqHYNLVSRLTVI--ENVLhgclgykttLSG-------AAGLYREEEKEQAfdlIEKVDLSAFA-------YTRCD 145
Cdd:cd03244 71 IG----LHDLRSRISIIpqDPVL---------FSGtirsnldPFGEYSDEELWQA---LERVGLKEFVeslpgglDTVVE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 146 E----LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSA----KTIMDYLKRITnELAITclvnlHQVETAIDYsDRI 217
Cdd:cd03244 135 EggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDaliqKTIREAFKDCT-VLTIA-----HRLDTIIDS-DRI 207
|
250
....*....|....
gi 488231729 218 IGVNSGKIVFEGRP 231
Cdd:cd03244 208 LVLDKGRVVEFDSP 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-229 |
5.92e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 108.80 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:TIGR03375 464 IEFRNVSFAYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHynlvSRL---TVIENVLHGclgykttlsgaAGLYREEEKEQAfdlIEKVDLSAFAYT-----------RCDEL 147
Cdd:TIGR03375 541 IGYVPQD----PRLfygTLRDNIALG-----------APYADDEEILRA---AELAGVTEFVRRhpdgldmqigeRGRSL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVeTAIDYSDRIIGVNSGKIVF 227
Cdd:TIGR03375 603 SGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGRIVA 679
|
..
gi 488231729 228 EG 229
Cdd:TIGR03375 680 DG 681
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-237 |
1.13e-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: 103.33 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRR 81
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL---ALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRlTVIENVLhgclgykttlSGAAGLYREEEKEQA-----FDLIEKVDL--SAFAYTRCDELSGGQKQR 154
Cdd:cd03252 78 VGVVLQENVLFNR-SIRDNIA----------LADPGMSMERVIEAAklagaHDFISELPEgyDTIVGEQGAGLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNelAITCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLST-VKNADRIIVMEKGRIVEQGSHDEL 223
|
...
gi 488231729 235 TKE 237
Cdd:cd03252 224 LAE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-234 |
2.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLI---EADSGTIRFEDREMNELKRKELRKK 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrIGMIFQHY-NLVSRLTVIENVLHGCLGykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK13640 86 ---VGIVFQNPdNQFVGATVGDDVAFGLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAiDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-227 |
2.78e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.55 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITkTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD-----SGTIRFEDREMnELKRKELR 76
Cdd:PRK14239 5 ILQVSDLS-VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI-YSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRRIGMIFQHYNLVSrLTVIENVLHGCL--GYK----------TTLSGAAglYREEEKEQAFDliekvdlSAFAytrc 144
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRlkGIKdkqvldeaveKSLKGAS--IWDEVKDRLHD-------SALG---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 deLSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETAIDYSDR-------- 216
Cdd:PRK14239 149 --LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRtgffldgd 224
|
250
....*....|.
gi 488231729 217 IIGVNSGKIVF 227
Cdd:PRK14239 225 LIEYNDTKQMF 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-239 |
3.33e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpnGNQALQD-ISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkRKELRKKRRR 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDgLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLhgclgyktTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLL--------VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRItneLAI--TCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSL---LARgkTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2-237 |
5.56e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRK 77
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 -KRRRIGMIFQH-YNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQKQR 154
Cdd:PRK13643 81 pVRKKVGVVFQFpESQLFEETVLKDVAFGPQNF--------GIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
...
gi 488231729 235 TKE 237
Cdd:PRK13643 232 FQE 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-234 |
8.80e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 8.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQA--LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKr 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQHY-NLVSRLTVIENVLHGCLGykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIA 158
Cdd:PRK13642 83 --IGMVFQNPdNQFVGATVEDDVAFGMEN--------QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-234 |
1.28e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.38 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITktYPNGNQAL-QDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR 80
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLHgclgyktTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-229 |
1.94e-25 |
|
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: 98.54 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRkelrkkrrr 81
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 igmifqhyNLVSRLTVIENVLHgclGYKTTLSGAAGLyreeekeqafdliekvdlsafaytrcdELSGGQKQRVGIARAL 161
Cdd:cd03247 72 --------ALSSLISVLNQRPY---LFDTTLRNNLGR---------------------------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVeTAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-238 |
3.24e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrkelrkkRRR 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR----------DYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRL------TVIENVLHgclgykttlsGAAGLYREEEKEQA------FDLIEKVD--LSAFAYTRCDEL 147
Cdd:PRK11176 412 LASLRNQVALVSQNvhlfndTIANNIAY----------ARTEQYSREQIEEAarmayaMDFINKMDngLDTVIGENGVLL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQN-PALILcDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKIV 226
Cdd:PRK11176 482 SGGQRQRIAIARALLRDsPILIL-DEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST-IEKADEILVVEDGEIV 557
|
250
....*....|..
gi 488231729 227 FEGRPYELTKEK 238
Cdd:PRK11176 558 ERGTHAELLAQN 569
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-181 |
4.29e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.41 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITkTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmneLKRKELRKKRR 80
Cdd:PRK13539 1 MMLEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGmifqHYNLVSR-LTVIENvlhgclgykttLSGAAGLYREEEkEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:PRK13539 77 YLG----HRNAMKPaLTVAEN-----------LEFWAAFLGGEE-LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALAR 140
|
170 180
....*....|....*....|..
gi 488231729 160 ALMQNPALILCDEPIASLDPKS 181
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAA 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-241 |
6.25e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.70 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADS--GTIRFEDREMneLKRKELRKKR 79
Cdd:PRK13549 5 LLEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL--QASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGA---AGLYREEEKeqafdLIEKVDLSAFAYTRCDELSGGQKQRVG 156
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIF---LGNEITPGGImdyDAMYLRAQK-----LLAQLKLDINPATPVGNLGLGQQQLVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTK 236
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTE 232
|
....*
gi 488231729 237 EKIET 241
Cdd:PRK13549 233 DDIIT 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-229 |
7.48e-25 |
|
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: 98.11 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 17 QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDREMNELKRKELrkkrrrIGMIFQHYNLVS 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC------VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 94 RLTVIENV---LHGCLGYKTTlsgaaglYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILC 170
Cdd:cd03234 95 GLTVRETLtytAILRLPRKSS-------DAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 171 DEPIASLDPKSAKTIMDYLKRI--TNELAItclVNLHQVETAI-DYSDRIIGVNSGKIVFEG 229
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLarRNRIVI---LTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-237 |
1.15e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPNGN----QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM-NELKRKEL 75
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKKRRRIGMIFQH-YNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQKQ 153
Cdd:PRK13649 81 KQIRKKVGLVFQFpESQLFEETVLKDVAFGPQNF--------GVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE 233
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
....
gi 488231729 234 LTKE 237
Cdd:PRK13649 232 IFQD 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-178 |
1.35e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.65 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINrLIEA-DSGTIRFEDREMNELK 71
Cdd:PRK11308 5 LLQAIDLKKHYPVKRglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETpTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQH-Y-NLVSRLTViENVLHGCLGYKTTLSgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDEL-S 148
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQNpYgSLNPRKKV-GQILEEPLLINTSLS------AAERREKALAMMAKVGLRPEHYDRYPHMfS 156
|
170 180 190
....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-243 |
1.47e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 97.47 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpnGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKElrkkrrr 81
Cdd:TIGR03740 1 LETKNLSKRF--GKQtAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENvlhgcLGYKTTLSGAaglyreeEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:TIGR03740 72 IGSLIESPPLYENLTAREN-----LKVHTTLLGL-------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLH---QVETAIDYsdriIGVNS-GKIVFEGRPYEltKE 237
Cdd:TIGR03740 140 LNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHilsEVQQLADH----IGIISeGVLGYQGKINK--SE 212
|
....*.
gi 488231729 238 KIETIY 243
Cdd:TIGR03740 213 NLEKLF 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-237 |
2.05e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.61 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD-----SGTIRFEDREMnELKRKELRK 77
Cdd:PRK14267 5 IETVNLRVYYGS-NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI-YSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVSRLTVIENVlhgCLGYKTTlsgaaGLYREEEkeqafDLIEKVDLSAFAYTRCDE----------- 146
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNV---AIGVKLN-----GLVKSKK-----ELDERVEWALKKAALWDEvkdrlndypsn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVnlHQVETAIDYSD--------RII 218
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT--HSPAQAARVSDyvaflylgKLI 227
|
250
....*....|....*....
gi 488231729 219 GVNSGKIVFEGRPYELTKE 237
Cdd:PRK14267 228 EVGPTRKVFENPEHELTEK 246
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-243 |
2.09e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.94 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 5 VKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrrIGM 84
Cdd:PRK10575 14 LRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK---VAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 85 IFQHYNLVSRLTVIENVLHGclgyKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQN 164
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIG----RYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 165 PALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYELTK-EKIETIY 243
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRgETLEQIY 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-230 |
2.30e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.94 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYP----------NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIeADSGTIRFEDREMNEL 70
Cdd:PRK15134 274 PLLDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 71 KRKELRKKRRRIGMIFQHYN--LVSRLTVIENVLHGCLGYKTTLSGAaglyreEEKEQAFDLIEKVDLSAFAYTRC-DEL 147
Cdd:PRK15134 353 NRRQLLPVRHRIQVVFQDPNssLNPRLNVLQIIEEGLRVHQPTLSAA------QREQQVIAVMEEVGLDPETRHRYpAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVF 227
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
...
gi 488231729 228 EGR 230
Cdd:PRK15134 507 QGD 509
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-231 |
3.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFedREMNELKRKELRKKRRR 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQH--YNLVSRlTVIENVLHG----CLGykttlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRV 155
Cdd:PRK13644 79 VGIVFQNpeTQFVGR-TVEEDLAFGpenlCLP------------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELAITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRP 231
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEP 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-195 |
3.37e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 14 NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRfedremnelkrkelRKKRRRIGMIFQHYNLVS 93
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 94 RL--TVIENVLHGCLGYKttlsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCD 171
Cdd:NF040873 69 SLplTVRDLVAMGRWARR----GLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180
....*....|....*....|....
gi 488231729 172 EPIASLDPKSAKTIMDYLKRITNE 195
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHAR 168
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-234 |
4.04e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 100.66 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED-----------REMnelk 71
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslRAA---- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 rkelrkkrrrIGMIFQHynlvsrlTVI------ENVLHGCLGykttlsgaAGlyrEEEKEQAfdlIEKVDLSAF------ 139
Cdd:COG5265 434 ----------IGIVPQD-------TVLfndtiaYNIAYGRPD--------AS---EEEVEAA---ARAAQIHDFieslpd 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 140 AY-TRCDE----LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVETAIDyS 214
Cdd:COG5265 483 GYdTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHRLSTIVD-A 559
|
250 260
....*....|....*....|
gi 488231729 215 DRIIGVNSGKIVFEGRPYEL 234
Cdd:COG5265 560 DEILVLEAGRIVERGTHAEL 579
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-229 |
4.84e-24 |
|
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: 96.25 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIR------FEDREmnelkrkelrKKRRRIGMIF-QHYN 90
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRK----------KFLRRIGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 91 LVSRLTVIEnvlhgclgyktTLSGAAGLYR---EEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPAL 167
Cdd:cd03267 106 LWWDLPVID-----------SFYLLAAIYDlppARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 168 ILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-239 |
6.34e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE-----ADSGTIRFEDREMnelKRKELRK 77
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDI---FKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVSRLTVIENVlhgCLGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCD----ELSGGQKQ 153
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENV---ALGLKLNRLVKS---KKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVnlHQVETAIDYSDRIIGVNSGKIVFEG---- 229
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT--HFPQQAARISDYVAFLYKGQIVEWGptre 231
|
250
....*....|....
gi 488231729 230 ---RP-YELTKEKI 239
Cdd:PRK14247 232 vftNPrHELTEKYV 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-191 |
6.38e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 5 VKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrrRIGM 84
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 85 IFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYR-----EEEKEQAFDLIEKVD--------------LSAF------ 139
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAklaepDEDLERLAELQEEFEalggweaearaeeiLSGLgfpeed 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 140 AYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDpksAKTIM---DYLKR 191
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwleEFLKN 197
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-214 |
9.36e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 9.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINR---LIEA--DSGTIRFEDREMNELKRKELR 76
Cdd:PRK14243 10 VLRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRrIGMIFQHYNLVSRlTVIENVLHGC--LGYKTTLSGAAglyrEEEKEQAF---DLIEKVDLSAFAytrcdeLSGGQ 151
Cdd:PRK14243 89 VRRR-IGMVFQKPNPFPK-SIYDNIAYGAriNGYKGDMDELV----ERSLRQAAlwdEVKDKLKQSGLS------LSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 152 KQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLV-NLHQVETAIDYS 214
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVThNMQQAARVSDMT 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-234 |
9.40e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 9.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED---REMNelkrkeLRKK 78
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVT------RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQHYNLVSRlTVIENVLHGclgyKTTLSGAAgLYREEEKEQAFDLIEKVD--LSAFAYTRCDELSGGQKQRVG 156
Cdd:PRK13657 408 RRNIAVVFQDAGLFNR-SIEDNIRVG----RPDATDEE-MRAAAERAQAHDFIERKPdgYDTVVGERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLST-VRNADRILVFDNGRVVESGSFDEL 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-189 |
1.14e-23 |
|
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: 98.97 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmneLKRKELRKKRRRI 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP---VSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRlTVIENVLHGClgykTTLSGAAgLYREEEKEQAFDLIEkvDLSAFAYTRCDE----LSGGQKQRVGIA 158
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLAR----PDATDEE-LWAALERVGLADWLR--ALPDGLDTVLGEggarLSGGERQRLALA 483
|
170 180 190
....*....|....*....|....*....|.
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYL 189
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
2.67e-23 |
|
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: 97.83 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNIT---KTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKS----TILRTINRLIEADSGTIRFEDREM------- 67
Cdd:COG4172 6 LLSVEDLSvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 68 ------NelkrkelrkkrrRIGMIFQ---------HynlvsrlTVIENV-----LHGclgykttlsgaaGLYREEEKEQA 127
Cdd:COG4172 86 lrrirgN------------RIAMIFQepmtslnplH-------TIGKQIaevlrLHR------------GLSGAAARARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 128 FDLIEKVD-------LSAFAYtrcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE----- 195
Cdd:COG4172 135 LELLERVGipdperrLDAYPH----QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElgmal 210
|
250 260 270
....*....|....*....|....*....|....
gi 488231729 196 LAITClvNLHQVEtaiDYSDRIIGVNSGKIVFEG 229
Cdd:COG4172 211 LLITH--DLGVVR---RFADRVAVMRQGEIVEQG 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-225 |
3.13e-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: 97.80 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFE-------DREmnelkrke 74
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDgadlkqwDRE-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 75 lrKKRRRIGMIFQHYNLVSRlTVIENVLhgclgykttlsgaaglyREEEKEQAFDLIEKVDLSAF---------AY---- 141
Cdd:TIGR01842 389 --TFGKHIGYLPQDVELFPG-TVAENIA-----------------RFGENADPEKIIEAAKLAGVhelilrlpdGYdtvi 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 142 -TRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQVeTAIDYSDRIIGV 220
Cdd:TIGR01842 449 gPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVIT-HRP-SLLGCVDKILVL 526
|
....*
gi 488231729 221 NSGKI 225
Cdd:TIGR01842 527 QDGRI 531
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-181 |
3.84e-23 |
|
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: 92.81 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrri 82
Cdd:TIGR01189 1 LAARNLACSR-GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 gmifqHY-----NLVSRLTVIENV--LHGCLGYkttlsgaaglyreeEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRV 155
Cdd:TIGR01189 76 -----LYlghlpGLKPELSALENLhfWAAIHGG--------------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRL 136
|
170 180
....*....|....*....|....*.
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKS 181
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAG 162
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-229 |
6.13e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.84 E-value: 6.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGnQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRR 81
Cdd:PRK11701 6 LLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 I------GMIFQH------------YNLVSRLTVIENVLHGCLgykttlsgaaglyreeeKEQAFDLIEKVDLSAfayTR 143
Cdd:PRK11701 85 RllrtewGFVHQHprdglrmqvsagGNIGERLMAVGARHYGDI-----------------RATAGDWLERVEIDA---AR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 144 CDEL----SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIG 219
Cdd:PRK11701 145 IDDLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250
....*....|
gi 488231729 220 VNSGKIVFEG 229
Cdd:PRK11701 225 MKQGRVVESG 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
6.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.10 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYN-LVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:PRK13652 80 VGLVFQNPDdQIFSPTVEQDIAFGPINL--------GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-178 |
7.82e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 96.74 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQA-LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEdremnelkrkelrkkrrr 81
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD------------------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIFQHYNlVSRL----------------TVIENV----------------LHGC--------LGYKTTLsGAAGLYre 121
Cdd:COG4618 393 -GADLSQWD-REELgrhigylpqdvelfdgTIAENIarfgdadpekvvaaakLAGVhemilrlpDGYDTRI-GEGGAR-- 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 122 eekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:COG4618 468 -------------------------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-225 |
8.00e-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: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPN--GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKr 79
Cdd:cd03248 11 IVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQHYNLVSRlTVIENVLHGCLGYKTTLSGAAGlyreeEKEQAFDLIEKVDLSAfaYTRCDE----LSGGQKQRV 155
Cdd:cd03248 90 --VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAA-----QKAHAHSFISELASGY--DTEVGEkgsqLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETaIDYSDRIIGVNSGKI 225
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-210 |
1.29e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.15 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQA---LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM-NELKRKELRK 77
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQHYNLVSRLTVIENVLHGCLgykttLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGI 157
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPAL-----LRGES---SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETA 210
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-234 |
1.45e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrkelrkkrr 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI------------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 rigmifQHYN---LVSRLTVIENVLH---GCLgyKTTLSGAAGLYREEEKEQAfdlIEKVDLSAFAYTrcDE-------- 146
Cdd:PRK11160 405 ------ADYSeaaLRQAISVVSQRVHlfsATL--RDNLLLAAPNASDEALIEV---LQQVGLEKLLED--DKglnawlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 ----LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE---LAITclvnlHQVeTAIDYSDRIIG 219
Cdd:PRK11160 472 ggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktvLMIT-----HRL-TGLEQFDRICV 545
|
250
....*....|....*
gi 488231729 220 VNSGKIVFEGRPYEL 234
Cdd:PRK11160 546 MDNGQIIEQGTHQEL 560
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-218 |
2.12e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrrri 82
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIF--QH-YnlvsrltvienVLHGCLgyKTTLS--GAAGLYREEEKEQAfdlIEKVDLSAFAyTRCDE-------LSGG 150
Cdd:COG4178 427 RVLFlpQRpY-----------LPLGTL--REALLypATAEAFSDAELREA---LEAVGLGHLA-ERLDEeadwdqvLSLG 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRitnELAITCLVNL-HQvETAIDYSDRII 218
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE---ELPGTTVISVgHR-STLAAFHDRVL 554
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-231 |
2.86e-22 |
|
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: 90.93 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrrr 81
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHyNLVSRLTVIEN---VLHGCLgyKTTLSgAAGLYREEEKEQAFDLIEKvdlsafaytrCDELSGGQKQRVGIA 158
Cdd:cd03369 72 ISTIPLE-DLRSSLTIIPQdptLFSGTI--RSNLD-PFDEYSDEEIYGALRVSEG----------GLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMdylKRITNELA-ITCLVNLHQVETAIDYsDRIIGVNSGKIVFEGRP 231
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQ---KTIREEFTnSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-226 |
3.17e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN----------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELK 71
Cdd:PRK10261 313 ILQVRNLVTRFPLRSgllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQ--HYNLVSRLTVIENVL-----HGClgykttlsgaagLYREEEKEQAFDLIEKVDL-SAFAYTR 143
Cdd:PRK10261 393 PGKLQALRRDIQFIFQdpYASLDPRQTVGDSIMeplrvHGL------------LPGKAAAARVAWLLERVGLlPEHAWRY 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 144 CDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSG 223
Cdd:PRK10261 461 PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
...
gi 488231729 224 KIV 226
Cdd:PRK10261 541 QIV 543
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-238 |
3.22e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPN--GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED---REMNelkrkeLR 76
Cdd:TIGR00958 478 LIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplVQYD------HH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRRIGMIFQHYNLVSRlTVIENVLHGCLGYKTTLSGAAGlyreeEKEQAFDLIEKvdLSAFAYTRCDE----LSGGQK 152
Cdd:TIGR00958 552 YLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAA-----KAANAHDFIME--FPNGYDTEVGEkgsqLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 153 QRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRitneLAITCLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPY 232
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAHRLST-VERADQILVLKKGSVVEMGTHK 698
|
....*.
gi 488231729 233 ELTKEK 238
Cdd:TIGR00958 699 QLMEDQ 704
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-196 |
4.75e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRR 81
Cdd:PRK09700 5 YISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKTTLsGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKVC-GVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLDPKSaktiMDYLKRITNEL 196
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKE----VDYLFLIMNQL 191
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-235 |
1.80e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 5 VKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELrkkrrrIGM 84
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 85 IFQHYNLVSRLTVI--ENVLHGCLGYKTTLSGAaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALM 162
Cdd:PRK15056 83 VPQSEEVDWSFPVLveDVVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVnSGKIVFEGrPYELT 235
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG-PTETT 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-250 |
2.76e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.53 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYP-----NGN---------------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIR-- 61
Cdd:COG4586 3 EVENLSKTYRvyekePGLkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 62 ----FEDREMNelkrkelrkkRRRIGMIF-QHYNLVSRLTVIEN-VLHGCLgYKttLSGAAglYREEEKEqafdLIEKVD 135
Cdd:COG4586 83 gyvpFKRRKEF----------ARRIGVVFgQRSQLWWDLPAIDSfRLLKAI-YR--IPDAE--YKKRLDE----LVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 136 LSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLV---NLHQVEtaiD 212
Cdd:COG4586 144 LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLtshDMDDIE---A 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 488231729 213 YSDRIIGVNSGKIVFEGrpyelTKEKIETIYQSKKLLV 250
Cdd:COG4586 221 LCDRVIVIDHGRIIYDG-----SLEELKERFGPYKTIV 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-239 |
3.67e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.95 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTY--PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM---NELKRKELRKK 78
Cdd:PRK14246 9 DVFNISRLYlyINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RRRIGMIFQHYNLVSRLTVIENVLHgclgyktTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCD----ELSGGQKQR 154
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAY-------PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLV-NLHQVETAID-----YSDRIIGVNSGKIVFE 228
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVShNPQQVARVADyvaflYNGELVEWGSSNEIFT 241
|
250
....*....|.
gi 488231729 229 GRPYELTKEKI 239
Cdd:PRK14246 242 SPKNELTEKYV 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-237 |
4.84e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.44 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIeADSGTIRFEDREMNELKRKELRKKRRRI 82
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GmifQHYNLVsRLTVIENVLHGclgyKTTLSgaaglyrEEEKEQAfdlIEKVDLSAFAYTRCD-----------ELSGGQ 151
Cdd:PRK11174 429 G---QNPQLP-HGTLRDNVLLG----NPDAS-------DEQLQQA---LENAWVSEFLPLLPQgldtpigdqaaGLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 152 KQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETAIDYsDRIIGVNSGKIVFEGRP 231
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDY 567
|
....*.
gi 488231729 232 YELTKE 237
Cdd:PRK11174 568 AELSQA 573
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-226 |
5.09e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 91.42 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADS--GTIRFEDREMneLKRKELRKKR 79
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPL--KASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAGLYrEEEKEQAFDLIEKVDLSAFAYTR-CDELSGGQKQRVGIA 158
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIF---LGNEITLPGGRMAY-NAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-214 |
6.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.56 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADS-----GTIRF-----EDREMNELKR 72
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 73 KELrkkrrrIGMIFQHYNLVSrLTVIENVLHGC--LGYKTTLSGAAGLYREEEKEQAFDLIE-KVDLSAFaytrcdELSG 149
Cdd:PRK14258 87 RRQ------VSMVHPKPNLFP-MSVYDNVAYGVkiVGWRPKLEIDDIVESALKDADLWDEIKhKIHKSAL------DLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 150 GQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLK--RITNELAITCLV-NLHQVETAIDYS 214
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVShNLHQVSRLSDFT 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-224 |
1.45e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 86.37 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ----ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrkelrkk 78
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 rrrIGMIFQHYNLVSRlTVIENVLHGclgykttlsgaaglyREEEKEQAFDLIE----KVDLSAFAY---TRCDE----L 147
Cdd:cd03250 68 ---IAYVSQEPWIQNG-TIRENILFG---------------KPFDEERYEKVIKacalEPDLEILPDgdlTEIGEkginL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLkrITNELAI--TCLVNLHQVEtAIDYSDRIIGVNSGK 224
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLNnkTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-208 |
1.63e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.55 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE--ADSGTIRFEDREMNelkrkelrkkrrrigmifqhynlvSRLT 96
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG------------------------REAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 97 VIENVlhgclgykttlsgaaglYREEEKEQAFDLIEKVDLS-AFAYTRC-DELSGGQKQRVGIARALMQNPALILCDEPI 174
Cdd:COG2401 102 LIDAI-----------------GRKGDFKDAVELLNAVGLSdAVLWLRRfKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....
gi 488231729 175 ASLDPKSAKTIMDYLKRITNELAITCLVNLHQVE 208
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-228 |
1.69e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.86 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRR 81
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGclgykttlsgaaGLYREEEK-----EQAFDLIEKvdLSAFAYTRCDELSGGQKQRVG 156
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG------------GFFAERDQfqeriKWVYELFPR--LHERRIQRAGTMSGGEQQMLA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFE 228
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-240 |
3.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.37 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 7 NITKTY----PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM--NELKRKELRKKRR 80
Cdd:PRK13645 11 NVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQ--HYNLVSRlTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAYTRCD-ELSGGQKQRVGI 157
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNL--------GENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE---- 233
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEifsn 241
|
250
....*....|
gi 488231729 234 ---LTKEKIE 240
Cdd:PRK13645 242 qelLTKIEID 251
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-236 |
3.67e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDREMNELKRKELRkkrrriGMIFQHYNLVSRL 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS------AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIENvlhgcLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYT------RCDELSGGQKQRVGIARALMQNPALIL 169
Cdd:TIGR00955 115 TVREH-----LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 170 CDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAI-DYSDRIIGVNSGKIVFEGRPYELTK 236
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-178 |
5.24e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrkelrkkrRR 81
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------VK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHY-NLVSRLTVIENVLHGclgykttlsgaaglyREEEKEQ---AFdliekvdLSAF------AYTRCDELSGGQ 151
Cdd:COG0488 380 IGYFDQHQeELDPDKTVLDELRDG---------------APGGTEQevrGY-------LGRFlfsgddAFKPVGVLSGGE 437
|
170 180 190
....*....|....*....|....*....|..
gi 488231729 152 KQRVGIARALMQNPALILCDEP-----IASLD 178
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPtnhldIETLE 469
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-237 |
5.83e-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: 88.32 E-value: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN----QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRF----EDREMNELKRK 73
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 74 ELRKKRRRIGMIFQHYNLVSRLTVIENvlhgclgykttLSGAAGLYREEE----------------KEQAFDLIEKvdls 137
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDN-----------LTEAIGLELPDElarmkavitlkmvgfdEEKAEEILDK---- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 138 afaYTrcDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRI 217
Cdd:TIGR03269 424 ---YP--DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRA 498
|
250 260
....*....|....*....|
gi 488231729 218 IGVNSGKIVFEGRPYELTKE 237
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIVEE 518
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-233 |
5.90e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ---------------------ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIR 61
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 62 FEDR-----EMnelkrkelrkkrrriGMIFQhynlvSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQaFDLIEkvdl 136
Cdd:COG1134 85 VNGRvsallEL---------------GAGFH-----PELTGRENIYLNGRLL--------GLSRKEIDEK-FDEIV---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 137 sAFAytrcdEL-----------SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlH 205
Cdd:COG1134 132 -EFA-----ELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS-H 204
|
250 260
....*....|....*....|....*...
gi 488231729 206 QVETAIDYSDRIIGVNSGKIVFEGRPYE 233
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-234 |
6.85e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 15 GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREM---NELKRKELRKKRRRIGMIFQHYNL 91
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 92 VSrLTVIENVLHGCLGYKTtlsgaagLYREEEKEQAFDLIEKVDLSAFAYTRCDE----LSGGQKQRVGIARALMQNPAL 167
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKL-------VPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 168 ILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-229 |
7.07e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKT--YPNG------NQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKR 72
Cdd:PRK15112 3 TLLEVRNLSKTfrYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 73 KELRKKrrrIGMIFQ----HYNLVSRltvIENVLHGCLGYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCdeLS 148
Cdd:PRK15112 83 SYRSQR---IRMIFQdpstSLNPRQR---ISQILDFPLRLNTDLEPEQ---REKQIIETLRQVGLLPDHASYYPHM--LA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFE 228
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
.
gi 488231729 229 G 229
Cdd:PRK15112 232 G 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-186 |
8.20e-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: 84.08 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRrI 82
Cdd:cd03231 1 LEADELTCER-DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLY-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GmifqHYN-LVSRLTVIENVLHGClgykttlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:cd03231 79 G----HAPgIKTTLSVLENLRFWH--------------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLL 140
|
170 180
....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIM 186
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFA 165
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-230 |
7.83e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 7.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 34 IIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRR-RIGMIFQHYNLVSRLTVIENVLHGClgykttl 112
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKrRIGYVFQDARLFPHYKVRGNLRYGM------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 113 sgaaglyREEEKEQaFDL------IEKVdLSAFAYTrcdeLSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIM 186
Cdd:PRK11144 102 -------AKSMVAQ-FDKivallgIEPL-LDRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488231729 187 DYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGR 230
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-185 |
8.39e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 20 QDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKElrkkrrrigmifqHYNLV------- 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-------------HQDLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 --SRLTVIENvlhgclgykttLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILC 170
Cdd:PRK13538 85 ikTELTALEN-----------LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|....*
gi 488231729 171 DEPIASLDPKSAKTI 185
Cdd:PRK13538 154 DEPFTAIDKQGVARL 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-239 |
1.59e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkRKELRKKRRR 81
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI----TGLSPRERRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIF-----QHYNLVSRLTVIENVLhgcLG--YKTTLSGAAGLYREEEKEQAFDLIEKVDLSA-FAYTRCDELSGGQKQ 153
Cdd:COG3845 333 LGVAYipedrLGRGLVPDMSVAENLI---LGryRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTpGPDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKR----------ITNELaitclvnlhqvETAIDYSDRIIGVNSG 223
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLElrdagaavllISEDL-----------DEILALSDRIAVMYEG 478
|
250
....*....|....*.
gi 488231729 224 KIVFEGRPYELTKEKI 239
Cdd:COG3845 479 RIVGEVPAAEATREEI 494
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-229 |
1.63e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQ---ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED---REMNELKRKEL 75
Cdd:PRK10261 12 VLAVENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 76 RKKRRR--------IGMIFQH--YNLVSRLTVIENV-----LHgclgykttlsgaAGLYREEEKEQAFDLIEKVD----- 135
Cdd:PRK10261 92 EQSAAQmrhvrgadMAMIFQEpmTSLNPVFTVGEQIaesirLH------------QGASREEAMVEAKRMLDQVRipeaq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 136 --LSAFAYtrcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDY 213
Cdd:PRK10261 160 tiLSRYPH----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEI 235
|
250
....*....|....*.
gi 488231729 214 SDRIIGVNSGKIVFEG 229
Cdd:PRK10261 236 ADRVLVMYQGEAVETG 251
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-238 |
2.83e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 83.64 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKrkelrkkrrrI 82
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID----------R 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRL------TVIENVLhgcLGYKTTLSgaaglyrEEEKEQAFDLIE-KVDLSAFA---YTRCDE----LS 148
Cdd:TIGR01193 544 HTLRQFINYLPQEpyifsgSILENLL---LGAKENVS-------QDEIWAACEIAEiKDDIENMPlgyQTELSEegssIS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaiTCLVNLHQVETAiDYSDRIIGVNSGKIVFE 228
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQ 689
|
250
....*....|
gi 488231729 229 GRPYELTKEK 238
Cdd:TIGR01193 690 GSHDELLDRN 699
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-226 |
5.14e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGNQALQ---DISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD-----SGTIRFEDREM-NELKR 72
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 73 KELRKKRRRIGMIFQHyNLVS--RLTVIENVLHgclgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCD---EL 147
Cdd:PRK15134 85 TLRGVRGNKIAMIFQE-PMVSlnPLHTLEKQLY------EVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-229 |
9.37e-18 |
|
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: 79.11 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN---------------------QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIr 61
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 62 feDREMNELkrkelrkkrrriGMIFQHYNLVSRLTVIENVLHGCLGYkttlsgaaGLYREEEKEQAFDLIEKVDLSAFAY 141
Cdd:cd03220 80 --TVRGRVS------------SLLGLGGGFNPELTGRENIYLNGRLL--------GLSRKEIDEKIDEIIEFSELGDFID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 142 TRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQVETAIDYSDRIIGVN 221
Cdd:cd03220 138 LPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLE 216
|
....*...
gi 488231729 222 SGKIVFEG 229
Cdd:cd03220 217 KGKIRFDG 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-231 |
1.01e-17 |
|
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: 82.37 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 5 VKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKkrrrIG 83
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS----LG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 84 MIFQHYNLVSRLTVIENVLhgclgYKTTLSGAAglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ 163
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHIL-----FYAQLKGRS---WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNelAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRP 231
Cdd:TIGR01257 1079 DAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-190 |
1.19e-17 |
|
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: 77.58 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrrri 82
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIF--QHynlvsrltvienvlhgclGYKTTlsgaaGLYREeekeqafdliekvdlsAFAYTRCDELSGGQKQRVGIARA 160
Cdd:cd03223 65 DLLFlpQR------------------PYLPL-----GTLRE----------------QLIYPWDDVLSGGEQQRLAFARL 105
|
170 180 190
....*....|....*....|....*....|
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLK 190
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-221 |
1.92e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrkelrkkrRR 81
Cdd:PRK09544 4 LVSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVienvlhgclgyktTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK09544 69 IGYVPQKLYLDTTLPL-------------TVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVN 221
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-196 |
2.51e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTY--PNGN-QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDRE-MNELKRKE 74
Cdd:PRK09473 12 LLDVKDLRVTFstPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREiLNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 75 LRKKRRRIGMIFQH--YNLVSRLTVIENVLHGCLGYKttlsgaaGLYREEEKEQAFDLIEKVDLSAfAYTRCD----ELS 148
Cdd:PRK09473 92 NKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHK-------GMSKAEAFEESVRMLDAVKMPE-ARKRMKmyphEFS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLkritNEL 196
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL----NEL 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-246 |
6.96e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAdSGTIRFEDREMNELKRKELRKKRrriGMIFQHYNLVSRLTVI 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 EnvlhgclgYkTTLSGAAGLyREEEKEQAF-DLIEKVDLSAFaYTR-CDELSGGQKQRVGIARALMQ-----NP--ALIL 169
Cdd:COG4138 88 Q--------Y-LALHQPAGA-SSEAVEQLLaQLAEALGLEDK-LSRpLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 170 CDEPIASLD--PKSAktimdyLKRITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKEKIETIY 243
Cdd:COG4138 157 LDEPMNSLDvaQQAA------LDRLLRELCqqgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPENLSEVF 230
|
...
gi 488231729 244 QSK 246
Cdd:COG4138 231 GVK 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-177 |
8.13e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRR 81
Cdd:PRK10762 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT--FNGPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAAGLYREEEKEqAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARAL 161
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIF---LGREFVNRFGRIDWKKMYAE-ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170
....*....|....*.
gi 488231729 162 MQNPALILCDEPIASL 177
Cdd:PRK10762 157 SFESKVIIMDEPTDAL 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-207 |
8.34e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTyPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRR 80
Cdd:PRK10247 6 PLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI---STLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRlTVIENVLhgcLGYKttlsgaagLYREEEKEQAFdlieKVDLSAFAY------TRCDELSGGQKQR 154
Cdd:PRK10247 82 QVSYCAQTPTLFGD-TVYDNLI---FPWQ--------IRNQQPDPAIF----LDDLERFALpdtiltKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488231729 155 VGIARALMQNPALILCDEPIASLDPKSaktimdylKRITNELaITCLVNLHQV 207
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESN--------KHNVNEI-IHRYVREQNI 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-225 |
1.84e-16 |
|
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: 74.78 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITktypnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:cd03215 4 VLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIF-----QHYNLVSRLTVIENVLHGCLgykttlsgaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVG 156
Cdd:cd03215 76 -GIAYvpedrKREGLVLDLSVAENIALSSL----------------------------------------LSGGNQQKVV 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 157 IARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE-LAItcLVNLHQVETAIDYSDRIIGVNSGKI 225
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAV--LLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-239 |
2.38e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITktypnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrr 81
Cdd:COG1129 256 VLEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 iGMIF-----QHYNLVSRLTVIENVlhgclgyktTLS-----GAAGLYRE-EEKEQAFDLIEKVDLSAF-AYTRCDELSG 149
Cdd:COG1129 328 -GIAYvpedrKGEGLVLDLSIRENI---------TLAsldrlSRGGLLDRrRERALAEEYIKRLRIKTPsPEQPVGNLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 150 GQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMdylkRITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIY----RLIRELAaegKAVIVISSELPELLGLSDRILVMREGRIV 473
|
250
....*....|....*
gi 488231729 227 --FEGRpyELTKEKI 239
Cdd:COG1129 474 geLDRE--EATEEAI 486
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-229 |
3.26e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.45 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelKRKELRKKRRRI 82
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL---SSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIfQHYNLVSRLTVIENVLHGclgykttlsgaaglyREEEKEQAFDLIEKVDLSAFA-------YTRCDE----LSGGQ 151
Cdd:PRK10790 418 AMV-QQDPVVLADTFLANVTLG---------------RDISEEQVWQALETVQLAELArslpdglYTPLGEqgnnLSVGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 152 KQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVETAIDySDRIIGVNSGKIVFEG 229
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-199 |
4.25e-16 |
|
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: 77.28 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 6 KNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDremnelkrkelrkkRRRIGMI 85
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP--------------GIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 86 FQHYNLVSRLTVIENVLHGCLGYKTTLS---GAAGLYREEE-------KEQA-----------FDLIEKVDLSAFAYtRC 144
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGVAEIKDALDrfnEISAKYAEPDadfdklaAEQAelqeiidaadaWDLDSQLEIAMDAL-RC 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 145 -------DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE-LAIT 199
Cdd:TIGR03719 153 ppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTvVAVT 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-237 |
7.24e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 11 TYP-NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNElkrkelrkkrrrigmiFQHY 89
Cdd:PRK10789 322 TYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK----------------LQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 90 NLVSRLTVienVLHGCLGYKTTLSGAAGLYR----EEEKEQAFDLIEKVD----LSAFAYTRCDE----LSGGQKQRVGI 157
Cdd:PRK10789 386 SWRSRLAV---VSQTPFLFSDTVANNIALGRpdatQQEIEHVARLASVHDdilrLPQGYDTEVGErgvmLSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELaiTCLVNLHQVeTAIDYSDRIIGVNSGKIVFEGRPYELTKE 237
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-190 |
8.24e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.10 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIrfedremnelkrkelrkkrrri 82
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 gmifqhynlvsrlTVIENVLHGCLgykttlsgaaglyreeekEQafdliekvdlsafaytrcdeLSGGQKQRVGIARALM 162
Cdd:cd03221 58 -------------TWGSTVKIGYF------------------EQ--------------------LSGGEKMRLALAKLLL 86
|
170 180
....*....|....*....|....*...
gi 488231729 163 QNPALILCDEPIASLDPKSAKTIMDYLK 190
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEALK 114
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-177 |
2.62e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADS--GTIRFEDREMNELKRKELRKKR 79
Cdd:NF040905 1 ILEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIgmIFQHYNLVSRLTVIENVLhgcLGYKTTLSGAagLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIAR 159
Cdd:NF040905 80 IVI--IHQELALIPYLSIAENIF---LGNERAKRGV--IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170
....*....|....*...
gi 488231729 160 ALMQNPALILCDEPIASL 177
Cdd:NF040905 153 ALSKDVKLLILDEPTAAL 170
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-237 |
3.94e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.62 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN---QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE------ADSgtIRFEDREMNELKR 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAEK--LEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 73 KELRKKR-RRIGMIFQH--YNLVSRLTVienvlhgclGYKT--TLSGAAGLYREEEKEQAFDLIEKVDLSAFAyTRCD-- 145
Cdd:PRK11022 81 KERRNLVgAEVAMIFQDpmTSLNPCYTV---------GFQImeAIKVHQGGNKKTRRQRAIDLLNQVGIPDPA-SRLDvy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 146 --ELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSG 223
Cdd:PRK11022 151 phQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
250
....*....|....
gi 488231729 224 KIVFEGRPYELTKE 237
Cdd:PRK11022 231 QVVETGKAHDIFRA 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-243 |
9.33e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 15 GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD--------SGTIRFEDREMNELKRKELRKKRrriGMIF 86
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLR---AVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 87 QHYNLVSRLTVIENVLHGCLGYkttlSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ--- 163
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLGRYPH----ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 164 ------NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTK 236
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADvLTP 245
|
....*..
gi 488231729 237 EKIETIY 243
Cdd:PRK13547 246 AHIARCY 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2-186 |
1.09e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkrKELRKKRRR 81
Cdd:PRK13540 1 MLDVIELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENvlhgCLGYKTTLSGAAGLyreEEKEQAFDLIEKVDLSafaytrCDELSGGQKQRVGIARAL 161
Cdd:PRK13540 76 LCFVGHRSGINPYLTLREN----CLYDIHFSPGAVGI---TELCRLFSLEHLIDYP------CGLLSSGQKRQVALLRLW 142
|
170 180
....*....|....*....|....*
gi 488231729 162 MQNPALILCDEPIASLDPKSAKTIM 186
Cdd:PRK13540 143 MSKAKLWLLDEPLVALDELSLLTII 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-178 |
1.29e-14 |
|
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: 72.66 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDremnelkrkelrkkRRRI 82
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE--------------TVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQ-HYNLVSRLTVIENVlhgclgykttlSGaaGLyreeekeqafDLIE--KVDLSAFAYT------------RCDEL 147
Cdd:TIGR03719 388 AYVDQsRDALDPNKTVWEEI-----------SG--GL----------DIIKlgKREIPSRAYVgrfnfkgsdqqkKVGQL 444
|
170 180 190
....*....|....*....|....*....|.
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-179 |
1.54e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemNELKRKELRKKRRR 81
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREeekeqafdLIEKVDLSAFAYTrcdeLSGGQKQRVGIARAL 161
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAA--------LGCQLDLDSSAGS----LEVADRQIVEILRGL 155
|
170
....*....|....*...
gi 488231729 162 MQNPALILCDEPIASLDP 179
Cdd:PRK15439 156 MRDSRILILDEPTASLTP 173
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-230 |
2.57e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 29 GEFVSIIGPSGAGKSTILRTINRLIEADS--GTIRFEDREMnelkrkeLRKKRRRIGMIFQHYNLVSRLTVIENVLHGCL 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP-------TKQILKRTGFVTQDDILYPHLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 107 gykttLSGAAGLYREEEKEQAFDLIEKVDLsafayTRCDE----------LSGGQKQRVGIARALMQNPALILCDEPIAS 176
Cdd:PLN03211 167 -----LRLPKSLTKQEKILVAESVISELGL-----TKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 177 LDPKSAKTIMDYLKRITNElAITCLVNLHQVETAI-DYSDRIIGVNSGKIVFEGR 230
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGK 290
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-238 |
2.87e-14 |
|
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: 70.66 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 15 GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrkelrkkrrrIGMIFQhYNLVSR 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------------ISFSSQ-FSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 95 LTVIENVLHGcLGYKTtlsgaaglYREEEKEQAFDLIEkvDLSAFA---YTRCDE----LSGGQKQRVGIARALMQNPAL 167
Cdd:cd03291 112 GTIKENIIFG-VSYDE--------YRYKSVVKACQLEE--DITKFPekdNTVLGEggitLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 168 ILCDEPIASLDPKSAKTIMD--YLKRITNELAITCLVNLHQVETAidysDRIIGVNSGKIVFEGRPYELTKEK 238
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEscVCKLMANKTRILVTSKMEHLKKA----DKILILHEGSSYFYGTFSELQSLR 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-217 |
9.02e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGN--QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED----REMNELKRKELR 76
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 77 KKRRRIGMIFQH-------YNLVS--RLTVIENVLH------------------GCLG-----YKTTLSGAAGLYREE-- 122
Cdd:PTZ00265 463 GVVSQDPLLFSNsiknnikYSLYSlkDLEALSNYYNedgndsqenknkrnscraKCAGdlndmSNTTDSNELIEMRKNyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 123 --EKEQAFDLIEKVDLSAFAYTRCDE-----------LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYL 189
Cdd:PTZ00265 543 tiKDSEVVDVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260
....*....|....*....|....*....
gi 488231729 190 KRIT-NELAITCLVnLHQVETaIDYSDRI 217
Cdd:PTZ00265 623 NNLKgNENRITIII-AHRLST-IRYANTI 649
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-178 |
1.02e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYpnGNQAL-QDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDremnelkrkelrkkRRR 81
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------------TVK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQ-HYNLVSRLTVIENVlhgclgykttlSGaaGLyreeekeqafDLIE--KVDLSAFAYT------------RCDE 146
Cdd:PRK11819 389 LAYVDQsRDALDPNKTVWEEI-----------SG--GL----------DIIKvgNREIPSRAYVgrfnfkggdqqkKVGV 445
|
170 180 190
....*....|....*....|....*....|..
gi 488231729 147 LSGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-238 |
1.32e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrkelrkkrRR 81
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI------------AK 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMifqhYNLVSRLTVIEN---VLHGCLgyKTTLSgAAGLYREEEKEQAFDLIEkvdLSAFAYT-------RCDE----L 147
Cdd:TIGR00957 1353 IGL----HDLRFKITIIPQdpvLFSGSL--RMNLD-PFSQYSDEEVWWALELAH---LKTFVSAlpdkldhECAEggenL 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKriTNELAITCLVNLHQVETAIDYSdRIIGVNSGKIVF 227
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
250
....*....|.
gi 488231729 228 EGRPYELTKEK 238
Cdd:TIGR00957 1500 FGAPSNLLQQR 1510
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-238 |
3.25e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 15 GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrkelrkkrrrIGMIFQhYNLVSR 94
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------------ISFSPQ-TSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 95 LTVIENVLHGcLGYK----TTLSGAAGLyreEEKEQAFDLIEKVDLSAFAYTrcdeLSGGQKQRVGIARALMQNPALILC 170
Cdd:TIGR01271 501 GTIKDNIIFG-LSYDeyryTSVIKACQL---EEDIALFPEKDKTVLGEGGIT----LSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 171 DEPIASLDPKSAKTIMD--YLKRITNELAITCLVNLHQVETAidysDRIIGVNSGKIVFEGRPYELTKEK 238
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-229 |
4.62e-13 |
|
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: 65.75 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAD---SGTIRFEDREMnelkRKELRKKRRRIGMIFQHYNLVSRL 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY----KEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIEnvlhgclgyktTLSGAAGLyreeekeQAFDLIEKVdlsafaytrcdelSGGQKQRVGIARALMQNPALILCDEPIA 175
Cdd:cd03233 99 TVRE-----------TLDFALRC-------KGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 176 SLDPKSAKTIMDYLKRITNELAITCLVNLHQV-ETAIDYSDRIIGVNSGKIVFEG 229
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-234 |
7.15e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTY--PNGN-QALQDISFSLEKGEFVSIIGPSGAGKSTILRTI------NRLIEADSgtIRFEDREM-NELK 71
Cdd:PRK15093 3 LLDIRNLTIEFktSDGWvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNWRVTADR--MRFDDIDLlRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 72 RKELRKKRRRIGMIFQHYNlvSRLTVIENVlhgclGYKTTLSGAAGLYREE-------EKEQAFDLIEKVD-------LS 137
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQ--SCLDPSERV-----GRQLMQNIPGWTYKGRwwqrfgwRKRRAIELLHRVGikdhkdaMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 138 AFAYtrcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRI 217
Cdd:PRK15093 154 SFPY----ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250
....*....|....*..
gi 488231729 218 IGVNSGKIVFEGRPYEL 234
Cdd:PRK15093 230 NVLYCGQTVETAPSKEL 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-244 |
1.10e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 22 ISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEAdSGTIRFEDREMnelkrkelrkkrrrigmifQHYNLV--------- 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPL-------------------EAWSAAelarhrayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 ---SRLTVIENVLHgclgYkTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQ-----N 164
Cdd:PRK03695 75 sqqQTPPFAMPVFQ----Y-LTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 165 PA--LILCDEPIASLDpKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYE-LTKEKIET 241
Cdd:PRK03695 150 PAgqLLLLDEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPENLAQ 228
|
...
gi 488231729 242 IYQ 244
Cdd:PRK03695 229 VFG 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-234 |
1.53e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNElkrkelrkkrrrigmiFQHYNLVSRLTVI 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK----------------FGLTDLRRVLSII 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 EN---VLHGCLGYKT---TLSGAAGLYREEEKEQAFDLIEK--VDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILC 170
Cdd:PLN03232 1316 PQspvLFSGTVRFNIdpfSEHNDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488231729 171 DEPIASLDPKSAKTIMdylKRITNEL-AITCLVNLHQVETAIDySDRIIGVNSGKIVFEGRPYEL 234
Cdd:PLN03232 1396 DEATASVDVRTDSLIQ---RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-196 |
1.74e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 6 KNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelKRKELRKKRRRIGMI 85
Cdd:PRK10982 2 SNISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 86 FQHYNLVSRLTVIENVLHGCLGYKTTLSGAAGLYREEEKeqafdLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNP 165
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKA-----IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190
....*....|....*....|....*....|.
gi 488231729 166 ALILCDEPIASLDPKSaktiMDYLKRITNEL 196
Cdd:PRK10982 154 KIVIMDEPTSSLTEKE----VNHLFTIIRKL 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-231 |
3.05e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgnqalqdisFSLE-------KGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFE----------- 63
Cdd:PRK13409 340 LVEYPDLTKKLGD---------FSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyik 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 64 -DREMnelkrkelrkkrrrigmifqhynlvsrlTViENVLhgclgYKTTLSGAAGLYREEekeqafdLIEKVDLSAFAYT 142
Cdd:PRK13409 411 pDYDG----------------------------TV-EDLL-----RSITDDLGSSYYKSE-------IIKPLQLERLLDK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 143 RCDELSGGQKQRVGIARALMQNPALILCDEPIASLDP----KSAKTImdylKRITNELAITCLVNLHQVeTAIDY-SDRI 217
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI----RRIAEEREATALVVDHDI-YMIDYiSDRL 524
|
250
....*....|....
gi 488231729 218 igvnsgkIVFEGRP 231
Cdd:PRK13409 525 -------MVFEGEP 531
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-239 |
3.38e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITktypngNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrri 82
Cdd:PRK10762 258 LKVDNLS------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN---- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIF-----QHYNLVSRLTVIENVLHGCLGYkttLSGAAG-LYREEEKEQAFDLIEKVDLSAFAY-TRCDELSGGQKQRV 155
Cdd:PRK10762 328 GIVYisedrKRDGLVLGMSVKENMSLTALRY---FSRAGGsLKHADEQQAVSDFIRLFNIKTPSMeQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE-LAITcLVNLHQVETaIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSII-LVSSEMPEV-LGMSDRILVMHEGRISGEFTREQA 482
|
....*
gi 488231729 235 TKEKI 239
Cdd:PRK10762 483 TQEKL 487
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-237 |
4.27e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNIT---KTyPNGN-QALQDISFSLEKGEFVSIIGPSGAGKSTILRTI------NRLIEADSgtIRFEDRE-MNEL 70
Cdd:COG4170 3 LLDIRNLTieiDT-PQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdNWHVTADR--FRWNGIDlLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 71 KRKELRKKRRRIGMIFQHYN--LVSRLTV----IENVLHgclgykTTLSGAAGLYREEEKEQAFDLIEKVD-------LS 137
Cdd:COG4170 80 PRERRKIIGREIAMIFQEPSscLDPSAKIgdqlIEAIPS------WTFKGKWWQRFKWRKKRAIELLHRVGikdhkdiMN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 138 AFAYtrcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRItNELA-ITCLVNLHQVETAIDYSDR 216
Cdd:COG4170 154 SYPH----ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL-NQLQgTSILLISHDLESISQWADT 228
|
250 260
....*....|....*....|.
gi 488231729 217 IIGVNSGKIVFEGRPYELTKE 237
Cdd:COG4170 229 ITVLYCGQTVESGPTEQILKS 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-240 |
5.48e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTyPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTI--NRLIEADSGTIRF----------EDRemnel 70
Cdd:COG0396 1 LEIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLdgedilelspDER----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 71 krkelrkKRRRIGMIFQHynlvsrLTVIENVlhgclGYKTTLSGAAGLYREEE------KEQAFDLIEKVDLSAFAYTRC 144
Cdd:COG0396 75 -------ARAGIFLAFQY------PVEIPGV-----SVSNFLRTALNARRGEElsarefLKLLKEKMKELGLDEDFLDRY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 --DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE----LAITclvnlHQvETAIDY--SDR 216
Cdd:COG0396 137 vnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPdrgiLIIT-----HY-QRILDYikPDF 210
|
250 260
....*....|....*....|....
gi 488231729 217 IIGVNSGKIVFEGRPyELTKEkIE 240
Cdd:COG0396 211 VHVLVDGRIVKSGGK-ELALE-LE 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-234 |
5.98e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 17 QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRrIGMIFQHYNLVSRLT 96
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQ-VATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 97 VIENVLHGCLGykttlsgAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIAS 176
Cdd:PRK13638 94 DIDSDIAFSLR-------NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 177 LDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-229 |
7.79e-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: 62.26 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 17 QALQDISFSLEKGEFVSIIGPSGAGKSTILRTI-NRlieADSGTIRfedREMNELKRKELRKKRRRIGMIFQHYNLVSRL 95
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVIT---GEILINGRPLDKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIEnvlhgCLGYKTTLSGaaglyreeekeqafdliekvdlsafaytrcdeLSGGQKQRVGIARALMQNPALILCDEPIA 175
Cdd:cd03232 95 TVRE-----ALRFSALLRG--------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 176 SLDPKSAKTIMDYLKRITNE-LAITCLVnlHQVETAI-DYSDRIIGV-NSGKIVFEG 229
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSgQAILCTI--HQPSASIfEKFDRLLLLkRGGKTVYFG 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-231 |
2.14e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.04 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 11 TYPNGNQALQDISFSLEKGEF-----VSIIGPSGAGKSTILRTINRLIEADSGTIRFEdremnelkrkelrkkRRRIGMI 85
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE---------------LDTVSYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 86 FQHYNLVSRLTViENVLHGclgyKTTLSGAAGLYREEekeqafdLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNP 165
Cdd:cd03237 67 PQYIKADYEGTV-RDLLSS----ITKDFYTHPYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 166 ALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVeTAIDY-SDRIigvnsgkIVFEGRP 231
Cdd:cd03237 135 DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDI-IMIDYlADRL-------IVFEGEP 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-179 |
2.18e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 22 ISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRRRIGMIFQHYNLVSRLTVIeNV 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL-CG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 102 LHGCLGYKTTLSGAAglyreeekeqafdlieKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDP 179
Cdd:PRK13543 109 LHGRRAKQMPGSALA----------------IVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-181 |
3.38e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 6 KNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRtINRLIEADS-GTIRFEDremnelkrkelrkkRRRIGM 84
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKEFeGEARPAP--------------GIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 85 IFQHYNLVSRLTVIENVLHGCLGYKTTLS---GAAGLYREEE-------KEQ-----------AFDLIEKVDLSAFAYtR 143
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGVAEVKAALDrfnEIYAAYAEPDadfdalaAEQgelqeiidaadAWDLDSQLEIAMDAL-R 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488231729 144 C-------DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKS 181
Cdd:PRK11819 154 CppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-208 |
3.86e-11 |
|
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: 62.62 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPN-GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADsGTIRFEDREMNelkRKELRKKRRR 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWN---SVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSrltvienvlhgclgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDE-----------LSGG 150
Cdd:TIGR01271 1294 FGVIPQKVFIFS----------------GTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNG 1357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVE 208
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVE 1413
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-237 |
4.04e-11 |
|
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: 60.62 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITkTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTI--NRLIEADSGTIRFEDRemNELKRKELRKKRR 80
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGE--DITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIenvlhgclgykttlsgaaglyreeekeqafDLIEKVDLSafaytrcdeLSGGQKQRVGIARA 160
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNA------------------------------DFLRYVNEG---------FSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE----LAITclvnlHQvETAIDY--SDRIIGVNSGKIVFEGRPyEL 234
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEgksvLIIT-----HY-QRLLDYikPDRVHVLYDGRIVKSGDK-EL 191
|
...
gi 488231729 235 TKE 237
Cdd:cd03217 192 ALE 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-231 |
4.38e-11 |
|
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: 62.11 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNgnqalqdisFSLE-------KGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDRemnelkrke 74
Cdd:COG1245 341 LVEYPDLTKSYGG---------FSLEveggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 75 lrkkrrrIGMIFQHYNLVSRLTVIEnVLHGCLGYKTTLSgaagLYREEekeqafdLIEKVDLSAFAYTRCDELSGGQKQR 154
Cdd:COG1245 403 -------ISYKPQYISPDYDGTVEE-FLRSANTDDFGSS----YYKTE-------IIKPLGLEKLLDKNVKDLSGGELQR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 155 VGIARALMQNPALILCDEPIASLDP----KSAKTImdylKRITNELAITCLVNLHQVeTAIDY-SDRIigvnsgkIVFEG 229
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI----RRFAENRGKTAMVVDHDI-YLIDYiSDRL-------MVFEG 531
|
..
gi 488231729 230 RP 231
Cdd:COG1245 532 EP 533
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-222 |
6.61e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY---PNgNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE-ADSGTIRFEDREMNELKRKELRK- 77
Cdd:PTZ00265 1166 IEIMDVNFRYisrPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEHTNDMTNEQDYQg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 -KRRRIGM-------------------IFQH-------------YNL--VSRLTVI---ENVLHGCLGYKTTLSGAAGLY 119
Cdd:PTZ00265 1245 dEEQNVGMknvnefsltkeggsgedstVFKNsgkilldgvdicdYNLkdLRNLFSIvsqEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 120 REEEKE----QAFD-----LIEKVDLSAFAYTRcdELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLK 190
Cdd:PTZ00265 1325 REDVKRackfAAIDefiesLPNKYDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270
....*....|....*....|....*....|..
gi 488231729 191 RITNELAITCLVNLHQVeTAIDYSDRIIGVNS 222
Cdd:PTZ00265 1403 DIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-61 |
6.80e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 6.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 3 LEVKNITKTYPNGnQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIR 61
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-234 |
6.92e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTY-PNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNElkrkelrkkrrr 81
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK------------ 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 igmiFQHYNLVSRLTVIEN--VLhgclgykttLSGA-------------AGLYREEEKEQAFDLIEK--VDLSAFAYTRC 144
Cdd:PLN03130 1306 ----FGLMDLRKVLGIIPQapVL---------FSGTvrfnldpfnehndADLWESLERAHLKDVIRRnsLGLDAEVSEAG 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKS----AKTIMDYLKritnelAITCLVNLHQVETAIDySDRIIGV 220
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTdaliQKTIREEFK------SCTMLIIAHRLNTIID-CDRILVL 1445
|
250
....*....|....
gi 488231729 221 NSGKIVFEGRPYEL 234
Cdd:PLN03130 1446 DAGRVVEFDTPENL 1459
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-229 |
1.06e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 17 QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE----ADSGTIRFEDREMNElkrkelrkkrrrigmIFQHYnlv 92
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEE---------------IKKHY--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 sRLTVI---ENVLH-GCLGYKTTLSGAA----------GLYREEEKEQAFDLIekvdLSAFAYTRC------DEL----S 148
Cdd:TIGR00956 137 -RGDVVynaETDVHfPHLTVGETLDFAArcktpqnrpdGVSREEYAKHIADVY----MATYGLSHTrntkvgNDFvrgvS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMqNPALILC-DEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQV-ETAIDYSDRIIGVNSGKIV 226
Cdd:TIGR00956 212 GGERKRVSIAEASL-GGAKIQCwDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQI 290
|
...
gi 488231729 227 FEG 229
Cdd:TIGR00956 291 YFG 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-233 |
1.10e-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: 61.50 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDremnelkrkelrkkrrR 81
Cdd:TIGR00957 637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------S 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHyNLVSRLTVIENVLHGCL----GYKTTLSGAAgLYREEEKEQAFDLIEKVDLSAfaytrcdELSGGQKQRVGI 157
Cdd:TIGR00957 701 VAYVPQQ-AWIQNDSLRENILFGKAlnekYYQQVLEACA-LLPDLEILPSGDRTEIGEKGV-------NLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 158 ARALMQNPALILCDEPIASLDPKSAKTIMDY-------LKRITNELAITCLVNLHQVetaidysDRIIGVNSGKIVFEGr 230
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHvigpegvLKNKTRILVTHGISYLPQV-------DVIIVMSGGKISEMG- 843
|
...
gi 488231729 231 PYE 233
Cdd:TIGR00957 844 SYQ 846
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-234 |
1.36e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 107 GYKTTLSGAAGLY---------REEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASL 177
Cdd:NF000106 96 GRRESFSGRENLYmigr*ldlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 178 DPKSAKTIMDYLKRITNELAiTCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPYEL 234
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-239 |
6.16e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 16 NQALQDISFSLEKGEFVSIIGPSGAGKSTilrtinrLIEADSGTIrfEDREMNELKRKELRKKRRRIGMIFQhynlvsrL 95
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTS-------LISAMLGEL--SHAETSSVVIRGSVAYVPQVSWIFN-------A 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIENVLHGClGYKTTLSGAAglYREEEKEQAFDLIEKVDLSAFAyTRCDELSGGQKQRVGIARALMQNPALILCDEPIA 175
Cdd:PLN03232 694 TVRENILFGS-DFESERYWRA--IDVTALQHDLDLLPGRDLTEIG-ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488231729 176 SLDPKSAKTIMDY-----LKRITNELAITCLVNLHQVetaidysDRIIGVNSGKIVFEGRPYELTKEKI 239
Cdd:PLN03232 770 ALDAHVAHQVFDScmkdeLKGKTRVLVTNQLHFLPLM-------DRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-212 |
9.36e-10 |
|
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: 57.56 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPN-GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADsGTIRFEDREMNelkRKELRKKRRR 81
Cdd:cd03289 3 MTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWN---SVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMIFQHYNLVSrltvienvlhgclgykTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDE-----------LSGG 150
Cdd:cd03289 79 FGVIPQKVFIFS----------------GTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElaITCLVNLHQVETAID 212
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLE 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-229 |
1.22e-09 |
|
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: 55.79 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTInrlIEADSGTIRFEDREMNElkrkelrkkrrrigmifqhYNLVSRLTV 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKFS-------------------RNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 98 IENVLHGCLGYkTTLSGAAGlyreeekeqafdliekvdlsafaytrcdELSGGQKQRVGIARALMQNP--ALILCDEPIA 175
Cdd:cd03238 68 LQFLIDVGLGY-LTLGQKLS----------------------------TLSGGELQRVKLASELFSEPpgTLFILDEPST 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 176 SLDPKSAKTIMDYLKRITNeLAITCLVNLHQVETaIDYSDRII------GVNSGKIVFEG 229
Cdd:cd03238 119 GLHQQDINQLLEVIKGLID-LGNTVILIEHNLDV-LSSADWIIdfgpgsGKSGGKVVFSG 176
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-241 |
1.74e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRI 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 83 GMIFQHYNLVSRLTvienvlhgclgykttlsGAAGLYREEEKEQAF----DLIEKVDLSAFAYTRCDeLSGGQKQRVGIA 158
Cdd:PRK10522 400 SAVFTDFHLFDQLL-----------------GPEGKPANPALVEKWlerlKMAHKLELEDGRISNLK-LSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 159 RALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQvETAIDYSDRIIGVNSGKIvfegrpYELTKEK 238
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL------SELTGEE 534
|
...
gi 488231729 239 IET 241
Cdd:PRK10522 535 RDA 537
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-223 |
2.09e-09 |
|
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: 55.80 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 11 TYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDR-EMNELKRKELRKKRRRIGMIFQHY 89
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 90 NLVSRlTVIENVLHGCLGYKTtlsgaaglyREEEKEQAFDLIEKVDLSAFA-YTRCDE----LSGGQKQRVGIARALMQN 164
Cdd:cd03290 89 WLLNA-TVEENITFGSPFNKQ---------RYKAVTDACSLQPDIDLLPFGdQTEIGErginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488231729 165 PALILCDEPIASLDPKSAKTIMD--YLKRITNELAITCLVNlHQVETAIdYSDRIIGVNSG 223
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVT-HKLQYLP-HADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-236 |
2.69e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGT---IRfedremnelkrkELRKKRRRIGMIFQhynlvsrL 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvvIR------------GTVAYVPQVSWIFN-------A 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIENVLHGclgykttlsgaaGLYREEEKEQAFDLIE-KVDLSAFA---YTRCDE----LSGGQKQRVGIARALMQNPAL 167
Cdd:PLN03130 694 TVRDNILFG------------SPFDPERYERAIDVTAlQHDLDLLPggdLTEIGErgvnISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 168 ILCDEPIASLDPKSA-----KTIMDYLKRITNELAITCLVNLHQVetaidysDRIIGVNSGKIVFEGRPYELTK 236
Cdd:PLN03130 762 YIFDDPLSALDAHVGrqvfdKCIKDELRGKTRVLVTNQLHFLSQV-------DRIILVHEGMIKEEGTYEELSN 828
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-181 |
2.81e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 4 EVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTIN--RLIEadSGTIRFEDREMNELkrkelrkkrrr 81
Cdd:NF033858 3 RLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMADA----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 igmifQH---------Y-------NLVSRLTVIENV-LHGCLgykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRC 144
Cdd:NF033858 69 -----RHrravcpriaYmpqglgkNLYPTLSVFENLdFFGRL---------FGQDAAERRRRIDELLRATGLAPFADRPA 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 488231729 145 DELSGGQKQRVGIARALMQNPALILCDEPIASLDPKS 181
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
3.80e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTI---------NRLI----EADSGtirfedremn 68
Cdd:PRK10938 260 RIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLTlfgrRRGSG---------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 69 elkrkelrkkrRRIGMIFQHYNLVSrltvieNVLHgcLGYKTT-------LSG---AAGLYREEEKEQAFDLIEKVDLSA 138
Cdd:PRK10938 329 -----------ETIWDIKKHIGYVS------SSLH--LDYRVStsvrnviLSGffdSIGIYQAVSDRQQKLAQQWLDILG 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488231729 139 FAYTRCD----ELSGGQKQRVGIARALMQNPALILCDEPIASLDP 179
Cdd:PRK10938 390 IDKRTADapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-187 |
8.92e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREmnelkrkelrkkrrriGMIFQHYNLVSRLTV 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----------------ALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 98 IENV-LHGCLgykttlsgaAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIAS 176
Cdd:PRK13545 103 IENIeLKGLM---------MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170
....*....|.
gi 488231729 177 LDPKSAKTIMD 187
Cdd:PRK13545 174 GDQTFTKKCLD 184
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-239 |
9.58e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKtypNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKRrr 81
Cdd:PRK09700 265 VFEVRNVTS---RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 82 IGMI---------FQHYNLVSRLTVIENVLHGclGYKttlsGAAGLYRE-EEKEQAFDLIEKVDLSAFAYTR-CDELSGG 150
Cdd:PRK09700 340 MAYItesrrdngfFPNFSIAQNMAISRSLKDG--GYK----GAMGLFHEvDEQRTAENQRELLALKCHSVNQnITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNElAITCLVNLHQVETAIDYSDRIIGVNSGKI--VFE 228
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLtqILT 492
|
250
....*....|.
gi 488231729 229 GRPyELTKEKI 239
Cdd:PRK09700 493 NRD-DMSEEEI 502
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-178 |
1.94e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTypngNQ-ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELrkkr 79
Cdd:PRK10982 249 VILEVRNLTSL----RQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA---- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrigmIFQHYNLVS---RLTVIENVLHgcLGYKTTLS------GAAGLYREEE-KEQAFDLIEKVDLSAFAY-TRCDELS 148
Cdd:PRK10982 321 -----INHGFALVTeerRSTGIYAYLD--IGFNSLISnirnykNKVGLLDNSRmKSDTQWVIDSMRVKTPGHrTQIGSLS 393
|
170 180 190
....*....|....*....|....*....|
gi 488231729 149 GGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
146-231 |
4.21e-08 |
|
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: 51.42 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 146 ELSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIigvnsgkI 225
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-------H 143
|
....*.
gi 488231729 226 VFEGRP 231
Cdd:cd03222 144 VFEGEP 149
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-195 |
4.57e-08 |
|
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: 53.48 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYP-NGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrkelrkkRR 80
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----------LT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHYNLVSRLTVIENVLHGcLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARA 160
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTG-REHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190
....*....|....*....|....*....|....*
gi 488231729 161 LMQNPALILCDEPIASLDPKSAKTIMDYLKRITNE 195
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-178 |
5.28e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 12 YPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIrFEDREMNelkrkelrkkrrrIGMIFQHYnl 91
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVR-------------MAVFSQHH-- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 92 VSRLTVIENVLhgcLGYKTTLSGAAglyreEEKEQA----FDLIEKVDLSAFaYTrcdeLSGGQKQRVGIARALMQNPAL 167
Cdd:PLN03073 582 VDGLDLSSNPL---LYMMRCFPGVP-----EQKLRAhlgsFGVTGNLALQPM-YT----LSGGQKSRVAFAKITFKKPHI 648
|
170
....*....|.
gi 488231729 168 ILCDEPIASLD 178
Cdd:PLN03073 649 LLLDEPSNHLD 659
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-229 |
7.72e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEdremnelkrkelrkkrRRIGMIFQHyNLVSRLTVI 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQ-AWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 ENVLhgclgykttlsgaagLYREEEKEQAFDLIE----KVDLSAFA---YTRCDE----LSGGQKQRVGIARALMQNPAL 167
Cdd:PTZ00243 739 GNIL---------------FFDEEDAARLADAVRvsqlEADLAQLGgglETEIGEkgvnLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 168 ILCDEPIASLDPKSAKTIMDYLkrITNELA-ITCLVNLHQVETaIDYSDRIIGVNSGKIVFEG 229
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVEEC--FLGALAgKTRVLATHQVHV-VPRADYVVALGDGRVEFSG 863
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-178 |
8.87e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFED------------REMNELKRKELRKKRRRIGMIF 86
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGTVYDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 87 QHYNLVSRLTVI---ENVLHGCLGYKTTLSgAAGLYREEEKEQafDLIEKVDLSafAYTRCDELSGGQKQRVGIARALMQ 163
Cdd:PRK11147 99 KRYHDISHLVETdpsEKNLNELAKLQEQLD-HHNLWQLENRIN--EVLAQLGLD--PDAALSSLSGGWLRKAALGRALVS 173
|
170
....*....|....*
gi 488231729 164 NPALILCDEPIASLD 178
Cdd:PRK11147 174 NPDVLLLDEPTNHLD 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-234 |
1.13e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNelkRKELRKKRRRIGMIFQHYNLVSRlTVI 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 99 ENVlhgclgykttlsgaaGLYREEEKEQAFDLIEKVDL-------SAFAYTRCDE----LSGGQKQRVGIARALMQ-NPA 166
Cdd:PTZ00243 1402 QNV---------------DPFLEASSAEVWAALELVGLrervaseSEGIDSRVLEggsnYSVGQRQLMCMARALLKkGSG 1466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488231729 167 LILCDEPIASLDPKSAK----TIMDYLKritnelAITCLVNLHQVETAIDYsDRIIGVNSGKIVFEGRPYEL 234
Cdd:PTZ00243 1467 FILMDEATANIDPALDRqiqaTVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-179 |
3.04e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKkrrrIGMIFQHYNLVSRLTV 97
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR----VGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 98 IEN-VLHgclgykttlsgaAGLYR--EEEKEQAFD-LIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPA-LILcDE 172
Cdd:NF033858 357 RQNlELH------------ARLFHlpAAEIAARVAeMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPElLIL-DE 423
|
....*..
gi 488231729 173 PIASLDP 179
Cdd:NF033858 424 PTSGVDP 430
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-187 |
4.24e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 18 ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRfedremnelkrkelrkKRRRIGMIFQHYNLVSRLTV 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD----------------RNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 98 IENVLHG--CLGYKttlsgaaglyREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIA 175
Cdd:PRK13546 103 IENIEFKmlCMGFK----------RKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170
....*....|..
gi 488231729 176 SLDPKSAKTIMD 187
Cdd:PRK13546 173 VGDQTFAQKCLD 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-239 |
5.82e-07 |
|
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: 49.82 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNITKTYPNGN--QALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE-ADSGTIRFEDREMNELKRKELRKK 78
Cdd:TIGR02633 257 ILEARNLTCWDVINPhrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 79 RrrIGMI---FQHYNLVSRLTVIENVLHGCLGYKTTLsgaaGLYREEEKEQAFDL-IEKVDLSAFA-YTRCDELSGGQKQ 153
Cdd:TIGR02633 337 G--IAMVpedRKRHGIVPILGVGKNITLSVLKSFCFK----MRIDAAAELQIIGSaIQRLKVKTASpFLPIGRLSGGNQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 154 RVGIARALMQNPALILCDEPIASLDPKSAKTIMdylkRITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGR 230
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIY----KLINQLAqegVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFV 486
|
....*....
gi 488231729 231 PYELTKEKI 239
Cdd:TIGR02633 487 NHALTQEQV 495
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-65 |
1.85e-06 |
|
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: 48.26 E-value: 1.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488231729 3 LEVKNITKTYPNGNQ----ALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDR 65
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-226 |
1.92e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPngnQAL-QDISFSLEKGEFVSIIGPSGAGKS-TILRTINRL---IEADSGTIRFEDREMnelkrKELRK 77
Cdd:PRK10418 5 IELRNIALQAA---QPLvHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPV-----APCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 78 KRRRIGMIFQH----YNLVsrLTVIENVLHGCLgykttlsgAAGlyREEEKEQAFDLIEKVDL-------SAFAYtrcdE 146
Cdd:PRK10418 77 RGRKIATIMQNprsaFNPL--HTMHTHARETCL--------ALG--KPADDATLTAALEAVGLenaarvlKLYPF----E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQVETAIDYSDRIIGVNSGKIV 226
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
7-172 |
3.28e-06 |
|
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: 47.82 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 7 NITKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTiRFEDREmnelkrkelrkkrrriGMIF 86
Cdd:TIGR00954 456 NIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR-LTKPAK----------------GKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 87 ----QHYnlVSRLTVIENVLHGCLGYKTTLSGaaglYREEEKEQAFDLI-------EKVDLSAFAYTRcDELSGGQKQRV 155
Cdd:TIGR00954 519 yvpqRPY--MTLGTLRDQIIYPDSSEDMKRRG----LSDKDLEQILDNVqlthileREGGWSAVQDWM-DVLSGGEKQRI 591
|
170
....*....|....*..
gi 488231729 156 GIARALMQNPALILCDE 172
Cdd:TIGR00954 592 AMARLFYHKPQFAILDE 608
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-220 |
1.84e-05 |
|
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: 43.89 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 20 QDISFSleKGEFVSIIGPSGAGKSTILRTInrlieadsgtirfedremnelkrkelrkkrrrigmifqhynlvsrltvie 99
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAI-------------------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 100 nvlhgclGYKTTLSGAAGLYREEEKEQAFdlieKVDLSAFAYTRCDELSGGQKQRVGIARAL----MQNPALILCDEPIA 175
Cdd:cd03227 42 -------GLALGGAQSATRRRSGVKAGCI----VAAVSAELIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488231729 176 SLDPKSAKTIMDYLKRITNELAITcLVNLHQVETAIDySDRIIGV 220
Cdd:cd03227 111 GLDPRDGQALAEAILEHLVKGAQV-IVITHLPELAEL-ADKLIHI 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-233 |
2.04e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 DELSGGQKQRVGIARAL---MQNPALILcDEPIASLDPKSAKTIMDYLKRITNELAITCLVNlHQvETAIDYSDRII--- 218
Cdd:PRK00635 475 ATLSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE-HD-EQMISLADRIIdig 551
|
90
....*....|....*...
gi 488231729 219 ---GVNSGKIVFEGRPYE 233
Cdd:PRK00635 552 pgaGIFGGEVLFNGSPRE 569
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-178 |
2.17e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 1 MLLEVKNITKTYPnGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRfedremnelkrkelRKKRR 80
Cdd:PRK11147 318 IVFEMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH--------------CGTKL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 81 RIGMIFQHY-NLVSRLTVIENVLHG------------CLGYkttlsgaaglyreeekeqafdliekvdLSAF------AY 141
Cdd:PRK11147 383 EVAYFDQHRaELDPEKTVMDNLAEGkqevmvngrprhVLGY---------------------------LQDFlfhpkrAM 435
|
170 180 190
....*....|....*....|....*....|....*..
gi 488231729 142 TRCDELSGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PRK11147 436 TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-49 |
2.41e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 2.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488231729 2 LLEVKNITKTYpNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTI 49
Cdd:CHL00131 7 ILEIKNLHASV-NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI 53
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-225 |
3.22e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 21 DISFSLEKGEFVSIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMNELKRKELRKKrrriGMIF-----QHYNLVSRL 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR----GLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 96 TVIENV---LHGCLGYKT-TLSGAAGL--YRE------EEKEQAfdliekvdlsafAYTrcdeLSGGQKQRVGIARALMQ 163
Cdd:PRK15439 357 PLAWNVcalTHNRRGFWIkPARENAVLerYRRalnikfNHAEQA------------ART----LSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 164 NPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLV--NLHQVEtaiDYSDRIIGVNSGKI 225
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFIssDLEEIE---QMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-206 |
5.05e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 29 GEFVSIIGPSGAGKSTILrtiNRLIE-ADSGTIRFEDREMNelKRKELRKKRRRIGMIFQHYNLVSRLTVIENvlhgcLG 107
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLL---NVLAErVTTGVITGGDRLVN--GRPLDSSFQRSIGYVQQQDLHLPTSTVRES-----LR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 108 YKTTLSGAAGLYREEEKEQAFDLIEKVDLSAFAytrcDELSG--------GQKQRVGIARALMQNPALIL-CDEPIASLD 178
Cdd:TIGR00956 859 FSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYA----DAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170 180
....*....|....*....|....*....
gi 488231729 179 PKSAKTIMDYLKRITNE-LAITClvNLHQ 206
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHgQAILC--TIHQ 961
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-206 |
5.10e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 17 QALQDISFSLEKGEFVSIIGPSGAGKSTIL-----RTINRLIEADSGTIRFEDREmnelkrkelrKKRRRIGMIFQHYNL 91
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIEGDIRISGFPKKQ----------ETFARISGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 92 VS-RLTVIENVLhgclgYKTTLSGAAGLYREEEK---EQAFDLIEKVDL--SAFAYTRCDELSGGQKQRVGIARALMQNP 165
Cdd:PLN03140 964 HSpQVTVRESLI-----YSAFLRLPKEVSKEEKMmfvDEVMELVELDNLkdAIVGLPGVTGLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488231729 166 ALILCDEPIASLDPKSAKTIMDYLkRITNELAITCLVNLHQ 206
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTV-RNTVDTGRTVVCTIHQ 1078
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-239 |
6.96e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 3 LEVKNITKTYPN--GNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTINRLIE-ADSGTIRFEDREMNELKRKELRKKR 79
Cdd:PRK13549 260 LEVRNLTAWDPVnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrIGMIFQ---HYNLVSRLTVIENVLHGCLGyktTLSGAAGLYREEEKEQAFDLIEKVDL-SAFAYTRCDELSGGQKQRV 155
Cdd:PRK13549 340 --IAMVPEdrkRDGIVPVMGVGKNITLAALD---RFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQQKA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 156 GIARALMQNPALILCDEPIASLDPKSAKTImdYlkRITNELA---ITCLVNLHQVETAIDYSDRIIGVNSGKIVFEGRPY 232
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEI--Y--KLINQLVqqgVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINH 490
|
....*..
gi 488231729 233 ELTKEKI 239
Cdd:PRK13549 491 NLTQEQV 497
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-229 |
7.21e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 19 LQDISFSLEKGEFVSIIGPSGAGKSTI-LRTI-----NRLIEADSGTIRFEDREMNELKRKELRKKRRRIGMIFQHYNLV 92
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIyaegqRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 SRLTVienvlhgclGYKTTLSGAAGLY--REEEKEQAFDLIEkVDLSAFAYTRCDE-LSGGQKQRVGIARALMQNPALIL 169
Cdd:cd03270 91 PRSTV---------GTVTEIYDYLRLLfaRVGIRERLGFLVD-VGLGYLTLSRSAPtLSGGEAQRIRLATQIGSGLTGVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488231729 170 --CDEPIASLDPKSAKTIMDYLKRITNeLAITCLVNLHQVETaIDYSDRII------GVNSGKIVFEG 229
Cdd:cd03270 161 yvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDT-IRAADHVIdigpgaGVHGGEIVAQG 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
2-185 |
9.03e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 2 LLEVKNItKTYPNGNQALQDISFSLEKGEFVSIIGPSGAGKSTILRTI--NRLIEADSGTIRFEDREMneLKRKELRKKR 79
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDL--LELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 RRIGMIFQHynlVSRLTVIENVLhgclgYKTTLSGAAGLYREEEKEQAFDL-------IEKVDLSAFAYTRCDEL--SGG 150
Cdd:PRK09580 78 EGIFMAFQY---PVEIPGVSNQF-----FLQTALNAVRSYRGQEPLDRFDFqdlmeekIALLKMPEDLLTRSVNVgfSGG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 488231729 151 QKQRVGIARALMQNPALILCDEPIASLDPKSAKTI 185
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIV 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
118-180 |
1.12e-04 |
|
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: 42.35 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488231729 118 LYREEEKEQAFDLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLDPK 180
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
146-231 |
2.06e-04 |
|
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: 41.45 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 146 ELSGGQKQRVGIARALmQNPA----LILCDEPIASLDPKSAKTIMDYLKRITnELAITCLV---NLHQVETAidysDRII 218
Cdd:cd03271 169 TLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVViehNLDVIKCA----DWII 242
|
90
....*....|....*....
gi 488231729 219 ------GVNSGKIVFEGRP 231
Cdd:cd03271 243 dlgpegGDGGGQVVASGTP 261
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
24-192 |
3.03e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 24 FSLEKGEFVsIIGPSGAGKSTILRTINRLIEADSGTIRFEDREMnelkrKELRKKRRRIGMIFQH----YNLV------- 92
Cdd:COG0419 19 IDFDDGLNL-IVGPNGAGKSTILEAIRYALYGKARSRSKLRSDL-----INVGSEEASVELEFEHggkrYRIErrqgefa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 93 --------SRLTVIENVLHgcLGYKTTLSGAAGLYREEEKEQAFDLIEKVDLSA------FAYTRCDELSGGQKQRVGIA 158
Cdd:COG0419 93 efleakpsERKEALKRLLG--LEIYEELKERLKELEEALESALEELAELQKLKQeilaqlSGLDPIETLSGGERLRLALA 170
|
170 180 190
....*....|....*....|....*....|....
gi 488231729 159 RALmqnpALILcDepIASLDPKSAKTIMDYLKRI 192
Cdd:COG0419 171 DLL----SLIL-D--FGSLDEERLERLLDALEEL 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-190 |
5.32e-04 |
|
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: 40.92 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 23 SFSL------EKGEFVSIIGPSGAGKSTILR-----------------TINRLIEADSGTIrfedremnelkrkelrkkr 79
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKilsgelkpnlgdydeepSWDEVLKRFRGTE------------------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 80 rrigmIFQHYNLVS--RLTVIenvlhgclgYKT--------TLSGAAG--LYREEEKEQAFDLIEKVDLSAFAYTRCDEL 147
Cdd:COG1245 148 -----LQDYFKKLAngEIKVA---------HKPqyvdlipkVFKGTVRelLEKVDERGKLDELAEKLGLENILDRDISEL 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLDPK----SAKTIMDYLK 190
Cdd:COG1245 214 SGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlnVARLIRELAE 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-234 |
1.30e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 LSGGQKQRVGIARALMQ---NPALILCDEPIASLDPKSAKTIMDYLKRITnELAITCLV---NLHQVETAidysDRII-- 218
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVViehNLDVIKTA----DYIIdl 904
|
90 100
....*....|....*....|
gi 488231729 219 ----GVNSGKIVFEGRPYEL 234
Cdd:TIGR00630 905 gpegGDGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
147-241 |
1.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 147 LSGGQKQRVGIARALMQNPALILCDEPIASLDPKSAKTIMDYLKRITNELAITCLVNLHQ--VETaIDYSDRIIGVNSGK 224
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpaPET-FDLFDDIILLSEGQ 415
|
90
....*....|....*..
gi 488231729 225 IVFEGrPYELTKEKIET 241
Cdd:PLN03140 416 IVYQG-PRDHILEFFES 431
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-238 |
1.62e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488231729 145 DELSGGQKQRVGIARALmqNPALI----LCDEPIASLDPKSAKTIMDYLKRITNeLAITCLVNLHQVETaIDYSDRII-- 218
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDEDT-IRAADYVIdi 562
|
90 100
....*....|....*....|....
gi 488231729 219 ----GVNSGKIVFEGRPYELTKEK 238
Cdd:TIGR00630 563 gpgaGEHGGEVVASGTPEEILANP 586
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-60 |
1.88e-03 |
|
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: 37.74 E-value: 1.88e-03
10 20 30
....*....|....*....|....*....|...
gi 488231729 28 KGEFVSIIGPSGAGKSTILRTINRLIEADSGTI 60
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
141-191 |
2.39e-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: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488231729 141 YTRCDELSGGQKQRVG---IARALMQ----------NPALILCDEPIASLDPKSAKTIMDYLKR 191
Cdd:pfam13558 27 YRRSGGLSGGEKQLLAylpLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
129-178 |
3.98e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.25 E-value: 3.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488231729 129 DLIEKVDLSAFAYTRCDELSGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
17-52 |
4.94e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 4.94e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488231729 17 QALQDISFSLEKGE-FVSIIGPSGAGKSTILRT-INRL 52
Cdd:COG3267 30 EALARLEYALAQGGgFVVLTGEVGTGKTTLLRRlLERL 67
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
17-61 |
5.29e-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: 36.77 E-value: 5.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488231729 17 QALQDIsfsLEKGEFVSII-GPSGAGKSTILRTINRLIEADSGTIR 61
Cdd:pfam13604 8 AAVRAL---LTSGDRVAVLvGPAGTGKTTALKALREAWEAAGYRVI 50
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-49 |
5.62e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 5.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488231729 3 LEVKNITKTYPNgnqalQDISFS-LEKGEFVSIIGPSGAGKSTILRTI 49
Cdd:cd03279 6 LELKNFGPFREE-----QVIDFTgLDNNGLFLICGPTGAGKSTILDAI 48
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
16-64 |
6.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.22 E-value: 6.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488231729 16 NQALQDISFSLEKGEFVSIIGPSGAGKSTIlrtINRLI---EADSGTIRFED 64
Cdd:PRK01889 182 GEGLDVLAAWLSGGKTVALLGSSGVGKSTL---VNALLgeeVQKTGAVREDD 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
148-178 |
8.56e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.15 E-value: 8.56e-03
10 20 30
....*....|....*....|....*....|.
gi 488231729 148 SGGQKQRVGIARALMQNPALILCDEPIASLD 178
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| |
