|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-247 |
1.44e-112 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 323.93 E-value: 1.44e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARI 82
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDAL 242
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLREI 242
|
....*
gi 15598510 243 YANEQ 247
Cdd:COG3638 243 YGGEA 247
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-243 |
9.84e-88 |
|
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: 260.58 E-value: 9.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARI 82
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDAL 242
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 15598510 243 Y 243
Cdd:cd03256 241 Y 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-244 |
8.76e-65 |
|
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: 202.53 E-value: 8.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARI 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDAL 242
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
..
gi 15598510 243 YA 244
Cdd:TIGR02315 242 YG 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-243 |
1.43e-49 |
|
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: 163.68 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLrarI 82
Cdd:COG1120 2 LEAENLS-VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAGRLGqwplWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYP----HLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV-DRAALDA 241
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVlTPELLEE 233
|
..
gi 15598510 242 LY 243
Cdd:COG1120 234 VY 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-243 |
1.43e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.93 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsaaarQRLRARI 82
Cdd:COG1121 7 IELENLT-VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQ--RVVSAVLAGRLGQWPLWKSLVslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:COG1121 78 GYVPQRAEVDWDFpiTVRDVVLMGRYGRRGLFRRPS----RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 161 LYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALD 240
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLS 232
|
...
gi 15598510 241 ALY 243
Cdd:COG1121 233 RAY 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-256 |
3.25e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 139.76 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLA---SQWRPSAGRVELLGE--EPWALSAAARQRLRARIGLVHQAPPL 91
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRtvQREGRLARDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 PPRQRVVSAVLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:PRK09984 98 VNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 172 EPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDALYANEQLQAE 251
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINRVEE 257
|
....*
gi 15598510 252 RASPA 256
Cdd:PRK09984 258 NAKAA 262
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-225 |
5.64e-40 |
|
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: 138.01 E-value: 5.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRAR-IGLVHQAPPLPPR 94
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAgrlgqwPLwkSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:cd03255 97 LTALENVEL------PL--LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 175 SAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLAlQHFPRVIGLRAGRI 225
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-225 |
6.35e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.87 E-value: 6.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQ---RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRL- 78
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 RARIGLVHQAPPLPPRQRVVSAV-LAGRLGQWPLWKslvslvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVaLPLLLAGVSRKE---------RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLAlQHFPRVIGLRAGRI 225
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-256 |
4.12e-39 |
|
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: 136.47 E-value: 4.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVH---ADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLR 79
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 80 ARIGLVHQAPP--LPPRQRVVSAVLAgrlgqwPLWkslvSLVYPLDRAGAHDALQRLDLGDK-LFQRCDQLSGGQLQRVG 156
Cdd:COG1124 79 RRVQMVFQDPYasLHPRHTVDRILAE------PLR----IHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 157 IARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHavDLAL-QHF-PRVIGLRAGRIAFDLPAGEV 234
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSH--DLAVvAHLcDRVAVMQNGRIVEELTVADL 226
|
250 260
....*....|....*....|..
gi 15598510 235 DRAALDAlYANEQLQAERASPA 256
Cdd:COG1124 227 LAGPKHP-YTRELLAASLAFER 247
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-243 |
2.45e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.04 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarQRLRARIGLVHQAPPLPP 93
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAV-LAGRLgqwplwkslvslvYPLDRAGA----HDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:COG1131 87 DLTVRENLrFFARL-------------YGLPRKEAreriDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 169 LADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDALY 243
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELL-RELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVF 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-228 |
2.60e-38 |
|
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: 133.43 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsaaarQRLRARIGLVHQAPPLPp 93
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSID- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSA---VLAGRLGQWPLWKSLVSLvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:cd03235 81 RDFPISVrdvVLMGLYGHKGLFRRLSKA----DKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 171 DEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-225 |
1.92e-36 |
|
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: 129.16 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPP--LPP 93
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMssLNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAgrlgqwPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03257 98 RMTIGEQIAE------PLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYpHELSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASLHavDLAL-QHFP-RVIGLRAGRI 225
Cdd:cd03257 172 PTSALDVSVQAQILDLLKKLQEELGLTLLFITH--DLGVvAKIAdRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-225 |
1.11e-35 |
|
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: 125.63 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLrarIGLVHQApp 90
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK---IAYVPQA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 lpprqrvvsavlagrlgqwplwkslvslvypldragahdaLQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:cd03214 82 ----------------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 171 DEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-233 |
3.05e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.55 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARI 82
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRV---VSAVL--AGRlgQWPLWKSLVSlvypldragahDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVyenVALPLrvTGK--SRKEIRRRVR-----------EVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLaLQHFP-RVIGLRAGRIAFDLPAGE 233
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLEL-VDRMPkRVLELEDGRLVRDEARGV 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-234 |
3.27e-34 |
|
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: 123.21 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARI 82
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAP------P-------LPPRQRVVSAVLAgrlgqwplwkslvslvypldRAGAHDALQRLDLGDKLFQRCDQLSG 149
Cdd:COG1122 78 GLVFQNPddqlfaPtveedvaFGPENLGLPREEI--------------------RERVEEALELVGLEHLADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 150 GQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDL 229
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
....*
gi 15598510 230 PAGEV 234
Cdd:COG1122 217 TPREV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-234 |
1.23e-33 |
|
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: 127.33 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVH----ADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRL 78
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 RARIGLVHQAP--PLPPRQRVvsavlagrlGQwplwkslvSLVYPLDRAG----------AHDALQRLDLGDKLFQR-CD 145
Cdd:COG1123 341 RRRVQMVFQDPysSLNPRMTV---------GD--------IIAEPLRLHGllsraerrerVAELLERVGLPPDLADRyPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 146 QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
....*....
gi 15598510 226 AFDLPAGEV 234
Cdd:COG1123 484 VEDGPTEEV 492
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-225 |
3.28e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.91 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwALSAAARQRLRARI 82
Cdd:COG4619 1 LELEGLS-FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK---PLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRqrVVSAVLagrlgqwPLWKSLVSLVYplDRAGAHDALQRLDLGDKLFQR-CDQLSGGQLQRVGIARVL 161
Cdd:COG4619 77 AYVPQEPALWGG--TVRDNL-------PFPFQLRERKF--DRERALELLERLGLPPDILDKpVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-173 |
5.04e-31 |
|
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: 112.74 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwALSAAARQRLRARIGLVHQAPPLPPRQRVV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ---DLTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 99 SAVLAGRLGQwplwkslvSLVYPLDRAGAHDALQRLDLGDKLFQRCD----QLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:pfam00005 78 ENLRLGLLLK--------GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-224 |
1.09e-30 |
|
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: 113.72 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 4 SLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARI 82
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD---LTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPplppRQRVVSAVLAGRLGQWPLwksLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:cd03225 78 GLVFQNP----DDQFFGPTVEEEVAFGLE---NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-225 |
1.35e-30 |
|
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: 113.27 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 8 VDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQ 87
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVVSAV-LAGRLGQWP--LWKSLVSlvypldragahDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQR 164
Cdd:cd03292 86 DFRLLPDRNVYENVaFALEVTGVPprEIRKRVP-----------AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 165 AELILADEPVSAMDPVLAGHTLALLNrEAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-225 |
1.52e-30 |
|
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: 113.69 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLPPR 94
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIARLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRLGQWPLWKSLVSLVYPLD--RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03219 90 LTVLENVMVAAQARTGSGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 173 PVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03219 170 PAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-260 |
2.37e-30 |
|
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: 118.47 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSA---GRVELLGEEPWALSAAARQRL 78
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 rarIGLVHQAP-----PLPPRQRVVSAVLAGRLGQwplwkslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQ 153
Cdd:COG1123 85 ---IGMVFQDPmtqlnPVTVGDQIAEALENLGLSR------------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 154 RVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGE 233
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
250 260
....*....|....*....|....*..
gi 15598510 234 VDRAAlDALYANEQLQAERASPAGEPA 260
Cdd:COG1123 230 ILAAP-QALAAVPRLGAARGRAAPAAA 255
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-224 |
1.14e-29 |
|
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: 110.80 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 5 LDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGL 84
Cdd:TIGR02673 4 FHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 85 VHQAPPLPPRQRVVSAV-LAGRLGQWP--LWKSLVslvypldragaHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVL 161
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVaLPLEVRGKKerEIQRRV-----------GAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLL-KRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-233 |
2.78e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.61 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 24 LRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglvhqAPPLPPRQRVVSAVL- 102
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---------------------LTALPPAERPVSMLFq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 103 --------------------AGRLGqwplwkslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:COG3840 79 ennlfphltvaqniglglrpGLKLT-------------AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGE 233
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-201 |
4.09e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQ---RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarqrlr 79
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 80 ARIGLVHQAPPLPPrqrvvsavlagrlgqwplWKSL---VSLvyPLDRAG---------AHDALQRLDLGDKLFQRCDQL 147
Cdd:COG1116 80 PDRGVVFQEPALLP------------------WLTVldnVAL--GLELRGvpkaerrerARELLELVGLAGFEDAYPHQL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598510 148 SGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLL 201
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVL 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-226 |
5.95e-29 |
|
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: 109.15 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPWAlsaaarqrlrari 82
Cdd:cd03259 1 LELKGLS-KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDVT------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 glvhqapPLPPRQRVVSAVLAgrlgQWPLWKSLV---SLVYPLDRAG---------AHDALQRLDLGDKLFQRCDQLSGG 150
Cdd:cd03259 66 -------GVPPERRNIGMVFQ----DYALFPHLTvaeNIAFGLKLRGvpkaeirarVRELLELVGLEGLLNRYPHELSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 151 QLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:cd03259 135 QQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
15-225 |
7.05e-29 |
|
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: 107.48 E-value: 7.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWAlsaaARQRLRARIGLVHQAPPLPPR 94
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVvsavlagrlgqwplwkslvslvypldragaHDALqrldlgdklfqrcdQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:cd03230 88 LTV------------------------------RENL--------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 175 SAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03230 124 SGLDPESRREFWELL-RELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-234 |
1.62e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.05 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PWALSAAArqrlrariGLV 85
Cdd:COG4559 9 VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawsPWELARRR--------AVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 86 HQAPPLPPRQRVVSAVLAGRLGQwplwkslvSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ-- 163
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH--------GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 164 -----RAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLAHQHAVLRLA-RQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-224 |
3.16e-28 |
|
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: 105.40 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAaarqrlrariglvhqapp 90
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 lpprqrvvsavlagrlgqwPLWKSLVSLVypldragahdalqrldlgdklfqrcDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:cd00267 69 -------------------EELRRRIGYV-------------------------PQLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598510 171 DEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:cd00267 105 DEPTSGLDPASRERLLELL-RELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-218 |
6.95e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 6.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgeepwalsaaarQRLRARIGLVHQAPPLPP 93
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 R--QRVVSAVLAGRLGQWPLWKSLVSLvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:NF040873 69 SlpLTVRDLVAMGRWARRGLWRRLTRD----DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598510 172 EPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVI 218
Cdd:NF040873 145 EPTTGLDAESRERIIALL-AEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-184 |
1.52e-27 |
|
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: 105.63 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR---ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarqrlr 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 80 ARIGLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSLvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIAR 159
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEA--------RERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180
....*....|....*....|....*
gi 15598510 160 VLYQRAELILADEPVSAMDPVLAGH 184
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQ 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-225 |
3.98e-27 |
|
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: 104.15 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpWALSAAARQRLRARIGLVHQAPPLPPR 94
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-LTDDKKNINELRQKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGrlgqwPLWkslvslVYPLDRAGA----HDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:cd03262 91 LTVLENITLA-----PIK------VKGMSKAEAeeraLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 171 DEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03262 160 DEPTSALDPELVGEVLDVM-KDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-224 |
7.02e-27 |
|
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: 102.65 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEePWALSAAARQRLRARIGLVHQAPPLPPR 94
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-DLTDLEDELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVvsavlagrlgqwplwkslvslvypldragahdaLQRLDLGdklfqrcdqLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:cd03229 91 LTV---------------------------------LENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598510 175 SAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-234 |
8.19e-27 |
|
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: 104.40 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHaDGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAG-RVELLGEE-----PWALsaaarq 76
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedVWEL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 rlRARIGLVHQA--PPLPPRQRVVSAVLAGRLGQWPLWKSlvslVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQR 154
Cdd:COG1119 77 --RKRIGLVSPAlqLRFPRDETVLDVVLSGFFDSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-234 |
1.98e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 103.15 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWAlSAAARQRLRARIGLVHQAPPLPP 93
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLRRKVGMVFQQFNLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGrlgqwPLWkslvslVYPLDRAGAH----DALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELIL 169
Cdd:COG1126 91 HLTVLENVTLA-----PIK------VKKMSKAEAEeramELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 170 ADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVM-RDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
2.25e-26 |
|
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: 107.54 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD---LSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPP---------------RQRVVSAvlagrlgqwplwkslvslvypLDRAGAHDALQRLDLG--DKLFQRC 144
Cdd:COG4988 413 IAWVPQNPYLFAgtirenlrlgrpdasDEELEAA---------------------LEAAGLDEFVAALPDGldTPLGEGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 145 DQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNReaAARGSTLLASLHavDLA-LQHFPRVIGLRAG 223
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGRTVILITH--RLAlLAQADRILVLDDG 547
|
...
gi 15598510 224 RIA 226
Cdd:COG4988 548 RIV 550
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
15-231 |
9.33e-26 |
|
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: 101.65 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PWALSAAarqrlrariGLV--HQ 87
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglpPHRIARL---------GIArtFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVVSAVLAGRLGQ--WPLWKSLVSLVYPLD-----RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARlgRGLLAALLRLPRARReereaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 161 LYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR-IAFDLPA 231
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRvIAEGTPA 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-231 |
1.35e-25 |
|
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: 100.59 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALA---DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSA-AARQRL 78
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 RARIGLVHQAPPLPPrqrvvsavlagrlgqwplwkSLVSLVY---PLDRAGAHDA-------LQRLDLGDKLFQRCDQLS 148
Cdd:COG4181 89 ARHVGFVFQSFQLLP--------------------TLTALENvmlPLELAGRRDArararalLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 149 GGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLAlQHFPRVIGLRAGRIAFD 228
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVED 227
|
...
gi 15598510 229 LPA 231
Cdd:COG4181 228 TAA 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
2.22e-25 |
|
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: 99.48 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHaDGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsAAARQRLRA 80
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPLPPRQRVV-----SAVLAGRlgqwplwkslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRV 155
Cdd:COG4133 76 RLAYLGHADGLKPELTVRenlrfWAALYGL---------------RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPvlAGHTL--ALLNREAAARGSTLLASLHAVDLA 210
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDA--AGVALlaELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-228 |
2.65e-25 |
|
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: 99.49 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 24 LRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALsaaarqrlrariglvhqapplPPRQRVVSAVLA 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA---------------------PPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 104 GR-------------LGQWPLWKslvslVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:cd03298 78 ENnlfahltveqnvgLGLSPGLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 171 DEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
3.37e-25 |
|
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: 104.08 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLra 80
Cdd:COG4987 333 SLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 rIGLVHQAPPLpprqrvVSAVLAG--RLGQwP------LWKSLvslvyplDRAGAHDALQRLDLG--DKLFQRCDQLSGG 150
Cdd:COG4987 411 -IAVVPQRPHL------FDTTLREnlRLAR-PdatdeeLWAAL-------ERVGLGDWLAALPDGldTWLGEGGRRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 151 QLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLAlqHFPRVIGLRAGRIA 226
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL-LEALAGRTVLLITHRLAGLE--RMDRILVLEDGRIV 548
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-225 |
8.70e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADGQrALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpWALSAAARQRLRA 80
Cdd:PRK11124 1 MSIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-FDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 R----IGLVHQapplpprqrvvsavlagrlgQWPLWKSLVSL---------VYPLDRAGAHDA----LQRLDLGDKLFQR 143
Cdd:PRK11124 79 ElrrnVGMVFQ--------------------QYNLWPHLTVQqnlieapcrVLGLSKDQALARaeklLERLRLKPYADRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 144 CDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAG 223
Cdd:PRK11124 139 PLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
..
gi 15598510 224 RI 225
Cdd:PRK11124 218 HI 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-235 |
1.16e-24 |
|
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: 97.89 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwALSAAARQRLRARI 82
Cdd:cd03224 1 LEVENLN-AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD--ITGLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAGRlgqwplwkslvslvYPLDRAGAHDALQRL-----DLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGA--------------YARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVD 235
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-245 |
1.36e-24 |
|
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: 102.60 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAP---- 89
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID---LRQIDPASLRRQIGVVLQDVflfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 -----------PLPPRQRVVSAvlagrlgqwplwkslvslvypLDRAGAHDALQRLDLGD--KLFQRCDQLSGGQLQRVG 156
Cdd:COG2274 563 gtirenitlgdPDATDEEIIEA---------------------ARLAGLHDFIEALPMGYdtVVGEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 157 IARVLYQRAELILADEPVSAMDPVLAGHTLALLNReaAARGSTLLASLHavDLA-LQHFPRVIGLRAGRIAFDLPAGEVd 235
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRR--LLKGRTVIIIAH--RLStIRLADRIIVLDKGRIVEDGTHEEL- 696
|
250
....*....|
gi 15598510 236 rAALDALYAN 245
Cdd:COG2274 697 -LARKGLYAE 705
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
1.39e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHAdGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE---PWALSAAARQR 77
Cdd:COG4161 1 MSIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 78 LRARIGLVHQAPPLPPRQRVVSAVLAGrlgqwPLWksLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHLTVMENLIEA-----PCK--VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-239 |
2.27e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 4 SLDGVDL-VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PWALSAAArqr 77
Cdd:PRK13548 2 MLEARNLsVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladwsPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 78 lrariGLVHQAPPL--PPRqrvVSAVLagRLGQWPLwkslvSLVYPLDRAGAHDALQRLD---LGDKLFQrcdQLSGGQL 152
Cdd:PRK13548 79 -----AVLPQHSSLsfPFT---VEEVV--AMGRAPH-----GLSRAEDDALVAAALAQVDlahLAGRDYP---QLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 153 QRVGIARVLYQRAE------LILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:PRK13548 141 QRVQLARVLAQLWEpdgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
250
....*....|...
gi 15598510 227 FDLPAGEVDRAAL 239
Cdd:PRK13548 221 ADGTPAEVLTPET 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
15-252 |
2.30e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRV-----ELLGEEPWALSAAARQRLRARIGLVHQAP 89
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 PLPPRQRVVSAVLAGrlgqwplwkSLVSLVYPLDRAGA--HDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAEL 167
Cdd:PRK11264 95 NLFPHRTVLENIIEG---------PVIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 168 ILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIafdlpageVDRAALDALYANEQ 247
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTI-RQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI--------VEQGPAKALFADPQ 236
|
....*
gi 15598510 248 LQAER 252
Cdd:PRK11264 237 QPRTR 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-237 |
7.04e-24 |
|
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: 96.20 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQApplpp 93
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQG----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 rqrvvSAvlagrlgqwpLWKSL-----VSLvyPLDRAG----------AHDALQRLDLGDKLFQRCDQLSGGQLQRVGIA 158
Cdd:COG1127 91 -----GA----------LFDSLtvfenVAF--PLREHTdlseaeirelVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 159 RVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRA 237
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-223 |
1.71e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELL-GEEPWALSaaarqrlra 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPaGARVLFLP--------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 riglvhQAPPLPPrqrvvsavlaGRLGQwplwkslvSLVYP-----LDRAGAHDALQRLDLGDkLFQRCDQ-------LS 148
Cdd:COG4178 433 ------QRPYLPL----------GTLRE--------ALLYPataeaFSDAELREALEAVGLGH-LAERLDEeadwdqvLS 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 149 GGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAarGSTLLASLHAVDLAlQHFPRVIGLRAG 223
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGHRSTLA-AFHDRVLELTGD 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-224 |
2.52e-23 |
|
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: 93.22 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD---LRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLpprqrvvsavLAGrlgqwplwkslvslvypldragahdalqrlDLGDKLfqrcdqLSGGQLQRVGIARVL 161
Cdd:cd03228 78 IAYVPQDPFL----------FSG------------------------------TIRENI------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLnrEAAARGSTLLASLHAVDLaLQHFPRVIGLRAGR 224
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEAL--RALAKGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-241 |
2.55e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPP--LPP 93
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSIsaVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVvsavlaGRLGQWPLwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK10419 105 RKTV------REIIREPL-RHLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDA 241
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPA 246
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-225 |
2.91e-23 |
|
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: 94.57 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR---ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLR 79
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 80 ARIGLVHQAPPLPPRQRVVSAVlagrlgqwplwkslvslVYPLDRAG---------AHDALQRLDLGDKLFQRCDQLSGG 150
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENV-----------------ALPLEIAGvpkaeieerVLELLELVGLEDKADAYPAQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 151 QLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALL---NREaaaRGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLrdiNRE---LGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-236 |
3.51e-23 |
|
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: 94.49 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPL-- 91
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGALfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 ----------PPRQRvvsavlaGRLGQWPLwkslvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVL 161
Cdd:cd03261 91 sltvfenvafPLREH-------TRLSEEEI------------REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDR 236
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-192 |
6.66e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.53 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLpPRQR 96
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQHFNL-LSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAVLAgrlgqwplwkslvslvYPLDRAGAHDA---------LQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAEL 167
Cdd:COG1135 98 TVAENVA----------------LPLEIAGVPKAeirkrvaelLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180
....*....|....*....|....*...
gi 15598510 168 ILADEPVSAMDPVLAGHTLALL---NRE 192
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLkdiNRE 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-228 |
7.98e-23 |
|
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: 93.03 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGeRVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsAAARQRLRARI 82
Cdd:cd03264 1 LQLENLT-KRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAV-LAGRLGQWPLWKSlvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVL 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLdYIAWLKGIPSKEV---------KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLNREAAARgsTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-228 |
1.22e-22 |
|
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: 92.65 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaaRQRLRA 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPLpprqrvvsavLAGRLgqwplwKSLVSLVYPL----------DRAGAHDALQRLDLGDKLF--QRCDQLS 148
Cdd:cd03245 79 NIGYVPQDVTL----------FYGTL------RDNITLGAPLadderilraaELAGVTDFVNKHPNGLDLQigERGRGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 149 GGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARgsTLLASLHAVDLaLQHFPRVIGLRAGRIAFD 228
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSL-LDLVDRIIVMDSGRIVAD 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-226 |
2.60e-22 |
|
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: 92.36 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARI 82
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED---IREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAV-LAGRLGQWPLWKSlvslvypldRAGAHDALQRLDLGDKLF-QRC-DQLSGGQLQRVGIAR 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIaLVPKLLKWPKEKI---------RERADELLALVGLDPAEFaDRYpHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 160 VLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-180 |
3.23e-22 |
|
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: 91.47 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQrALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQW-----RPSAGRVELLGEEPWALSAAARQR 77
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 78 LRArIGLVHQAPPlpprqrvvsavlagrlgqwPLWKSLV-SLVYPLDRAG----------AHDALQRLDLGDKLFQRCD- 145
Cdd:cd03260 80 RRR-VGMVFQKPN-------------------PFPGSIYdNVAYGLRLHGiklkeelderVEEALRKAALWDEVKDRLHa 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598510 146 -QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPV 180
Cdd:cd03260 140 lGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPI 175
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-225 |
4.68e-22 |
|
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: 90.80 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalsaAARQRLRARIGLVHQAPPLPPRQR 96
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAARNRIGYLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVS-AVLAGRLGQWPLWKSlvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVS 175
Cdd:cd03269 87 VIDqLVYLAQLKGLKKEEA---------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598510 176 AMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03269 158 GLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-239 |
6.64e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.80 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 24 LRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglvHQAppLPPRQRVVSAVLA 103
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-------------------HTT--TPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 104 GR-------------LGQWPLWKslvslVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK10771 79 ENnlfshltvaqnigLGLNPGLK-----LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 171 DEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD-----LPAGEVDRAAL 239
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDgptdeLLSGKASASAL 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-231 |
8.94e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWAL-SAAARQRLRARIGLV----HQAPPLPP 93
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdADALAQLRREHFGFIfqryHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRV-VSAVLAGrlgqwplwkslvsLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK10535 104 AQNVeVPAVYAG-------------LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 173 PVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHfPRVIGLRAGRIAFDLPA 231
Cdd:PRK10535 171 PTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQA-ERVIEIRDGEIVRNPPA 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
1.17e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADgQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaaRQRLRA 80
Cdd:PRK11231 1 MTLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS---SRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSLVslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLS----AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 161 LYQRAELILADEPVSAMDpvlAGHTLALLN--REAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAA 238
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD---INHQVELMRlmRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
.
gi 15598510 239 L 239
Cdd:PRK11231 230 L 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
1.86e-21 |
|
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: 93.12 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaaRQRLRAR 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD---ADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPPrQRVVSAVLAGRLGQwplwkSLVSLVYPLDRAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIAR 159
Cdd:TIGR02857 398 IAWVPQHPFLFA-GTIAENIRLARPDA-----SDAEIREALERAGLDEFVAALPQGldTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 160 VLYQRAELILADEPVSAMDPVLAGHTLALLnrEAAARGSTLLASLHAVDLA 210
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEAL--RALAQGRTVLLVTHRLALA 520
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-225 |
2.48e-21 |
|
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: 89.22 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALsaaarQRLRARIGLVHQAPPLPP 93
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPVNTVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAG-RLGQWPlwKSLVslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03300 86 HLTVFENIAFGlRLKKLP--KAEI-------KERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-239 |
3.14e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 5 LDGVDLVHADGQRALA-DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIG 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH---IQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPPRQRVVSAVLAGRLGQWPL---WKSLvslvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARGRYPHQPLftrWRKE-------DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 161 LYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAAL 239
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-237 |
7.31e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADG---QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE---PWAlsaaa 74
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgPGA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 75 rqrlraRIGLVHQAPPLPPRQRVVSAV-LAGRLGQWPLWKSlvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQ 153
Cdd:COG4525 77 ------DRGVVFQKDALLPWLNVLDNVaFGLRLRGVPKAER---------RARAEELLALVGLADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 154 RVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGL--RAGRIA--FDL 229
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVerLEL 221
|
250
....*....|....
gi 15598510 230 P------AGEVDRA 237
Cdd:COG4525 222 DfsrrflAGEDARA 235
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-237 |
9.26e-21 |
|
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: 91.47 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPL-- 91
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVD---IRQIDPADLRRNIGYVPQDPRLfy 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 -PPRQRVVSAVLAGrlgqwplwkSLVSLVYPLDRAGAHDALQRLDLGDKLF--QRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:TIGR03375 553 gTLRDNIALGAPYA---------DDEEILRAAELAGVTEFVRRHPDGLDMQigERGRSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 169 LADEPVSAMDPVLAGHTLALLNREAAarGSTLLASLHAVDLaLQHFPRVIGLRAGRIAFDLPAGEVDRA 237
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSL-LDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-243 |
1.34e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.83 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLPP 93
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLD---VATTPSRELAKRLAILRQENHINS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRlgqWPlwkslvslvY------PLDRAGAHDALQRLDLGDklFQRC--DQLSGGQLQRVGIARVLYQRA 165
Cdd:COG4604 89 RLTVRELVAFGR---FP---------YskgrltAEDREIIDEAIAYLDLED--LADRylDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 166 ELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV-DRAALDALY 243
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIiTPEVLSDIY 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-189 |
2.06e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.00 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PWAlsaaarq 76
Cdd:COG3842 5 ALELENVS-KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtglpPEK------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 rlrARIGLVHQAPPL------------PPRQRVVSAvlAGRlgqwplwkslvslvypldRAGAHDALQRLDLGDKLFQRC 144
Cdd:COG3842 77 ---RNVGMVFQDYALfphltvaenvafGLRMRGVPK--AEI------------------RARVAELLELVGLEGLADRYP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598510 145 DQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALL 189
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-234 |
2.31e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGrvELLGEepwALSAAARQRLRARI----GLVHQAPPLPPR 94
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG--DLIVD---GLKVNDPKVDERLIrqeaGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGrlgqwPLwkslvsLVYPLDRAGAHDalQRLDLGDK--LFQRCD----QLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK09493 92 LTALENVMFG-----PL------RVRGASKEEAEK--QARELLAKvgLAERAHhypsELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 169 LADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-173 |
2.89e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlraRIGLVHQAPPLPPRQRVV 98
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------RIGYLPQEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQWPLWKSLVSLVYP-----------------LDRAGAHDA-------LQRLDLGDKLFQR-CDQLSGGQLQ 153
Cdd:COG0488 80 DTVLDGDAELRALEAELEELEAKlaepdedlerlaelqeeFEALGGWEAearaeeiLSGLGFPEEDLDRpVSELSGGWRR 159
|
170 180
....*....|....*....|
gi 15598510 154 RVGIARVLYQRAELILADEP 173
Cdd:COG0488 160 RVALARALLSEPDLLLLDEP 179
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-228 |
4.33e-20 |
|
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: 85.81 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEePWALSAAARQR--LRARIGLVHQAPPLPPRQRVVSAVLAGrl 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINLppQQRKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 107 gqwplwksLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTL 186
Cdd:cd03297 100 --------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598510 187 ALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-241 |
5.60e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 86.40 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQ-APPLPPR 94
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQdSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRLgqwplwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:TIGR02769 104 RMTVRQIIGEPL------RHLTSLDESEQKARIAELLDMVGLRSEDADKLpRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 174 VSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAALDA 241
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPA 245
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-226 |
9.24e-20 |
|
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: 84.91 E-value: 9.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 24 LRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalSAAARQRLRARIGLVHQAPPLPPRQRVVSAVla 103
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-----SHTGLAPYQRPVSMLFQENNLFAHLTVRQNI-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 104 gRLGQWPLWKslvslVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAG 183
Cdd:TIGR01277 92 -GLGLHPGLK-----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598510 184 HTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-179 |
1.21e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.91 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD---IRDLTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPL---------------PPRQRVVSAvlagrlgqwplwkslvslvypLDRAGAHDALQRLDLG-D-KLFQRC 144
Cdd:COG1132 416 IGVVPQDTFLfsgtirenirygrpdATDEEVEEA---------------------AKAAQAHEFIEALPDGyDtVVGERG 474
|
170 180 190
....*....|....*....|....*....|....*
gi 15598510 145 DQLSGGQLQRVGIARVLYQRAELILADEPVSAMDP 179
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-228 |
1.84e-19 |
|
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: 83.13 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALsaaaRQRLRARIGLVHQAPPLpprq 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKALSSLISVLNQRPYL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 96 rvVSAVLAGRLGQwplwkslvslvypldragahdalqrldlgdklfqrcdQLSGGQLQRVGIARVLYQRAELILADEPVS 175
Cdd:cd03247 87 --FDTTLRNNLGR-------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 176 AMDPVLAGHTLALLNREaaARGSTLLASLHAVdLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03247 128 GLDPITERQLLSLIFEV--LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-228 |
3.09e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.92 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWalsaaarqrlRARIGLVHQapplpprqr 96
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW----------KRRKKFLRR--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 vVSAVLAGRLGQW---PLWKSLVSL--VYPLDRAGAHDALQR----LDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAEL 167
Cdd:cd03267 96 -IGVVFGQKTQLWwdlPVIDSFYLLaaIYDLPPARFKKRLDElselLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 168 ILADEPVSAMDpVLAGHTL-ALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03267 175 LFLDEPTIGLD-VVAQENIrNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-178 |
3.80e-19 |
|
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: 85.54 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSldgVDLVHADGQRALaDIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVElLGEEPWALSAAARQRLRA 80
Cdd:COG4148 1 MMLE---VDFRLRRGGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR-LGGEVLQDSARGIFLPPH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 --RIGLVHQAPPLPPRQRVVSAVLAGRlgqWPLWKslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIA 158
Cdd:COG4148 76 rrRIGYVFQEARLFPHLSVRGNLLYGR---KRAPR-------AERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIG 145
|
170 180
....*....|....*....|
gi 15598510 159 RVLYQRAELILADEPVSAMD 178
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALD 165
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-225 |
4.11e-19 |
|
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: 81.88 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRA-LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD---ISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLpprqrvvsavLAGRLGQwplwkslvslvypldragahdalqrldlgdklfqrcDQLSGGQLQRVGIARVL 161
Cdd:cd03246 78 VGYLPQDDEL----------FSGSIAE------------------------------------NILSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 162 YQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLaLQHFPRVIGLRAGRI 225
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
5.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 5 LDGVDLVHA--DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEePWALSAAARQRLRARI 82
Cdd:PRK13639 2 LETRDLKYSypDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPP---LPPRqrVVSAVLAGrlgqwPLwkslvSLVYPLDRAG--AHDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:PRK13639 81 GIVFQNPDdqlFAPT--VEEDVAFG-----PL-----NLGLSKEEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLAL---LNREaaarGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLlydLNKE----GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
6.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.63 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQapplPP 93
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE---VNAENEKWVRSKVGLVFQ----DP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKSLvSLVYPLDRAGahDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK13647 89 DDQVFSSTVWDDVAFGPVNMGL-DKDEVERRVE--EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 174 VSAMDPVLAGHTLALLNReAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK13647 166 MAYLDPRGQETLMEILDR-LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-237 |
8.08e-19 |
|
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: 85.57 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRA-LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRA 80
Cdd:COG4618 330 RLSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD---LSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPL--------------PPRQRVVSAVlagrlgqwplwkslvslvyplDRAGAHDALQRL------DLGDKL 140
Cdd:COG4618 407 HIGYLPQDVELfdgtiaeniarfgdADPEKVVAAA---------------------KLAGVHEMILRLpdgydtRIGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 141 FqrcdQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPvlAGHtLALLN--REAAARGSTLL------ASLHAVDLALQ 212
Cdd:COG4618 466 A----RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD--EGE-AALAAaiRALKARGATVVvithrpSLLAAVDKLLV 538
|
250 260
....*....|....*....|....*
gi 15598510 213 hfprvigLRAGRIAFDLPAGEVDRA 237
Cdd:COG4618 539 -------LRDGRVQAFGPRDEVLAR 556
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-230 |
8.96e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRA-LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPWAlsaaarqRLRARIGLVHQAPPLPP 93
Cdd:PRK11247 23 GERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLA-------EAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWplwkslvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK11247 95 WKKVIDNVGLGLKGQW--------------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 174 VSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLP 230
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLT 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-178 |
9.75e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG---EEPWALSaaarqrlrariGLVHQ 87
Cdd:PRK11248 9 ADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvEGPGAER-----------GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVVSAVLAGRlgqwplwkSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAEL 167
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGL--------QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|.
gi 15598510 168 ILADEPVSAMD 178
Cdd:PRK11248 150 LLLDEPFGALD 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-234 |
1.61e-18 |
|
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: 83.62 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEePWALSAaarqrlrariglvhQAPPLPPRQRVVSA 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR-TLFDSR--------------KGIFLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 101 VLA-GRLgqWPLWKSLVSLVYPLDRAGAHDA-------LQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:TIGR02142 80 VFQeARL--FPHLSVRGNLRYGMKRARPSERrisfervIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-218 |
1.74e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlraRI 82
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------------DL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPrqrvvsavlaGRLGQwplwkslvSLVYPLDragahdalqrldlgdklfqrcDQLSGGQLQRVGIARVLY 162
Cdd:cd03223 67 LFLPQRPYLPL----------GTLRE--------QLIYPWD---------------------DVLSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 163 QRAELILADEPVSAMDPVLAGHTLALLNreaaARGSTLLASLHAVDLaLQHFPRVI 218
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGHRPSL-WKFHDRVL 158
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-228 |
1.78e-18 |
|
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: 81.26 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG----EEPWAlsaaarqrLRARIGLVHQAPPLPP 93
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAE--------ARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLA-GRLgqwplwkslvslvYPLDRAGAHDAL----QRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:cd03266 92 RLTARENLEYfAGL-------------YGLKGDELTARLeelaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 169 LADEPVSAMDpVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03266 159 LLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
2.92e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADgQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaaRQRLRA 80
Cdd:PRK09536 2 PMIDVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS---ARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPLPPRQRVVSAVLAGR---LGQWPLWKslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEMGRtphRSRFDTWT-------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELV-RRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-179 |
3.31e-18 |
|
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: 80.35 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWAL-SAAARQRLRARIGLVHQAPPLPP 93
Cdd:TIGR03608 10 DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnSKKASKFRREKLGYLFQNFALIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKSLVSLVYpldragahDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:TIGR03608 90 NETVEENLDLGLKYKKLSKKEKREKKK--------EALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
....*.
gi 15598510 174 VSAMDP 179
Cdd:TIGR03608 162 TGSLDP 167
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
17-178 |
4.32e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.09 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAP--PLPPR 94
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPyaSLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVvsavlagrlGQwplwkslvSLVYPLDRAGAHDALQRLDLGDKLFQRCD-----------QLSGGQLQRVGIARVLYQ 163
Cdd:COG4608 112 MTV---------GD--------IIAEPLRIHGLASKAERRERVAELLELVGlrpehadryphEFSGGQRQRIGIARALAL 174
|
170
....*....|....*
gi 15598510 164 RAELILADEPVSAMD 178
Cdd:COG4608 175 NPKLIVCDEPVSALD 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-225 |
5.00e-18 |
|
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: 79.99 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalsAAARQRLRARIGLVHQAPPlpp 93
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKERRKSIGYVMQDVD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAG-RLGqwplwkslvSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03226 82 YQLFTDSVREElLLG---------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 173 PVSAMDPvlaGH--TLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03226 153 PTSGLDY---KNmeRVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-225 |
5.74e-18 |
|
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: 81.15 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRL-RARIGLVHQAPPLPPRQR 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAVlagrlgqwplwkslvslVYPLDRAG---------AHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAEL 167
Cdd:cd03294 119 VLENV-----------------AFGLEVQGvpraereerAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 168 ILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-201 |
5.99e-18 |
|
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: 81.64 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQWRpSAGRVELLGEEPWALSAAARQRL-RARIGLVHQAP-- 89
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGI-TSGEILFDGEDLLKLSEKELRKIrGREIQMIFQDPmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 PLPPRQRV---VSAVLAGRLGqwplwkslvslvypLDRAGAH----DALQRLDLGDKLfQRCD----QLSGGQLQRVGIA 158
Cdd:COG0444 98 SLNPVMTVgdqIAEPLRIHGG--------------LSKAEAReraiELLERVGLPDPE-RRLDryphELSGGMRQRVMIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598510 159 RVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLL 201
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAIL 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-228 |
6.84e-18 |
|
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: 80.96 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADG----QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRL 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 RARIGLVHQappLPPRQrvvsavlagrlgqwpLWKSLV---------SLVYPLDRAG--AHDALQRLDLGDKLFQR-CDQ 146
Cdd:TIGR04521 81 RKKVGLVFQ---FPEHQ---------------LFEETVykdiafgpkNLGLSEEEAEerVKEALELVGLDEEYLERsPFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 147 LSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:TIGR04521 143 LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
..
gi 15598510 227 FD 228
Cdd:TIGR04521 223 LD 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-178 |
7.10e-18 |
|
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: 79.97 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQ------ 87
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQIGLVSQdvflfn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 ---------APPLPPRQRVVSAVLAgrlgqwplwkslvslvypldrAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVG 156
Cdd:cd03251 90 dtvaeniayGRPGATREEVEEAARA---------------------ANAHEFIMELPEGydTVIGERGVKLSGGQRQRIA 148
|
170 180
....*....|....*....|..
gi 15598510 157 IARVLYQRAELILADEPVSAMD 178
Cdd:cd03251 149 IARALLKDPPILILDEATSALD 170
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-226 |
7.58e-18 |
|
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: 82.78 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPPRqrVVSAVLAgRLGQWPLWKSLVSLVyplDRAGAHDALQRL------DLGDklfqRCDQLSGGQLQRV 155
Cdd:TIGR01842 394 IGYLPQDVELFPG--TVAENIA-RFGENADPEKIIEAA---KLAGVHELILRLpdgydtVIGP----GGATLSGGQRQRI 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPvlAGHTlALLN--REAAARGSTLLASLHAVDLaLQHFPRVIGLRAGRIA 226
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDE--EGEQ-ALANaiKALKARGITVVVITHRPSL-LGCVDKILVLQDGRIA 532
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-181 |
1.07e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHaDGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalsaaarqrlrar 81
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 igLVHQappLPPRQRVVSAVLAgrlgQWPLWKSL-VS--LVYPLDRAGA---------HDALQRLDLGDKLFQRCDQLSG 149
Cdd:COG3839 66 --DVTD---LPPKDRNIAMVFQ----SYALYPHMtVYenIAFPLKLRKVpkaeidrrvREAAELLGLEDLLDRKPKQLSG 136
|
170 180 190
....*....|....*....|....*....|..
gi 15598510 150 GQLQRVGIARVLYQRAELILADEPVSAMDPVL 181
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKL 168
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-225 |
1.18e-17 |
|
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: 78.84 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsAAARQRLRARIGLVHQAPPLPP 93
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-----VTDLPPKDRDIAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGrlgqwplwksLVSLVYPLD--RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:cd03301 86 HMTVYDNIAFG----------LKLRKVPKDeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598510 172 EPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-192 |
1.39e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPPRQRV 97
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAV-LAGRLGQWPlwKSLV-SLVYPLdragahdaLQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVS 175
Cdd:PRK11153 100 FDNVaLPLELAGTP--KAEIkARVTEL--------LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180
....*....|....*....|
gi 15598510 176 AMDPVLAGHTLALL---NRE 192
Cdd:PRK11153 170 ALDPATTRSILELLkdiNRE 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-234 |
1.76e-17 |
|
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: 78.87 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrarI 82
Cdd:COG0410 4 LEVENLH-AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---------------I 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GlvhqapPLPPRQRV---VSAVLAGR-------------LGQWPLwkslvslvypLDRAGAHDALQRL-----DLGDKLF 141
Cdd:COG0410 68 T------GLPPHRIArlgIGYVPEGRrifpsltveenllLGAYAR----------RDRAEVRADLERVyelfpRLKERRR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 142 QRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLR 221
Cdd:COG0410 132 QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEII-RRLNREGVTILLVEQNARFALEIADRAYVLE 210
|
250
....*....|...
gi 15598510 222 AGRIAFDLPAGEV 234
Cdd:COG0410 211 RGRIVLEGTAAEL 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-178 |
2.37e-17 |
|
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: 78.92 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarqRLRARIGLVHQAPPLPPRQR 96
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-----VQERNVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAVLAGrlgqwpLWKSLVSLVYPLD--RAGAHDALQRLDLgDKLFQRC-DQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:cd03296 91 VFDNVAFG------LRVKPRSERPPEAeiRAKVHELLKLVQL-DWLADRYpAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
....*
gi 15598510 174 VSAMD 178
Cdd:cd03296 164 FGALD 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-226 |
4.10e-17 |
|
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: 76.31 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglvhqAPPLPPR 94
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---------------------VSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QrvvsavlAGRLGqwplwkslVSLVYpldragahdalqrldlgdklfqrcdQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:cd03216 71 D-------ARRAG--------IAMVY-------------------------QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 175 SAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:cd03216 111 AALTPAEVERLFKVI-RRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-243 |
4.54e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRARIGLVHQAPPLPPR 94
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQP--LESWSSKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRlgqWPlWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:PRK10575 100 MTVRELVAIGR---YP-WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 175 SAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR-IAFDLPAGEVDRAALDALY 243
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEmIAQGTPAELMRGETLEQIY 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-235 |
4.65e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.00 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADgQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaARQRLRAR 81
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-------LDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPPRQRVVSAVLA-GRL-GqwplwkslvslvypLDRAGAHDA----LQRLDLGDKLFQRCDQLSGGQLQRV 155
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYlARLkG--------------LSKAEAKRRadewLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 156 G-IARVLYQRAELILaDEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDlpaGEV 234
Cdd:COG4152 139 QlIAALLHDPELLIL-DEPFSGLDPVNVELLKDVI-RELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS---GSV 213
|
.
gi 15598510 235 D 235
Cdd:COG4152 214 D 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-226 |
5.25e-17 |
|
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: 77.91 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVH-ADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQ---------------APPLPPRQRVVSavlAGRLgqwplwkslvslvypldrAGAHDALQRLDLG--DKLFQRC 144
Cdd:cd03252 78 VGVVLQenvlfnrsirdnialADPGMSMERVIE---AAKL------------------AGAHDFISELPEGydTIVGEQG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 145 DQLSGGQLQRVGIARVLYQRAELILADEPVSAMDpvLAGHTLALLNREAAARGSTLLASLHAVDlALQHFPRVIGLRAGR 224
Cdd:cd03252 137 AGLSGGQRQRIAIARALIHNPRILIFDEATSALD--YESEHAIMRNMHDICAGRTVIIIAHRLS-TVKNADRIIVMEKGR 213
|
..
gi 15598510 225 IA 226
Cdd:cd03252 214 IV 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-181 |
7.63e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSaaARQRLRARIGLVHQAPPLPP 93
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LS--HVPPYQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGrLGQWPLWKSLVSlvypldrAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK11607 105 HMTVEQNIAFG-LKQDKLPKAEIA-------SRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
....*...
gi 15598510 174 VSAMDPVL 181
Cdd:PRK11607 177 MGALDKKL 184
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-225 |
8.24e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPPR 94
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAgrlgqwPLWKSLVSLVYPLDRAGAhdALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:PRK10908 94 RTVYDNVAI------PLIIAGASGDDIRRRVSA--ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 175 SAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK10908 166 GNLDDALSEGILRLF-EEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-225 |
8.33e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPlppRQRVVSAVLAgrlgqwplwkslvSLVYPLDRAG---------AHDALQRLDLGDKLFQRCDQLSGGQL 152
Cdd:PRK13635 83 VGMVFQNPD---NQFVGATVQD-------------DVAFGLENIGvpreemverVDQALRQVGMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 153 QRVGIARVLYQRAELILADEPVSAMDP-----VLAghTLALLNREaaaRGSTLLASLHAVDLALQHfPRVIGLRAGRI 225
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPrgrreVLE--TVRQLKEQ---KGITVLSITHDLDEAAQA-DRVIVMNKGEI 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-234 |
9.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 12 HADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPWALSAAARQRLRARIGLVHQAPPl 91
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLRESVGMVFQDPD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 pprQRVVSAVLAGRLGQWPLwkslvSLVYPLD--RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELIL 169
Cdd:PRK13636 93 ---NQLFSASVYQDVSFGAV-----NLKLPEDevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 170 ADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-183 |
2.53e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.35 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DL-VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVL--------------------ASQWRPSAGRVELLGEep 67
Cdd:PRK14239 10 DLsVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtitgsivyngHNIYSPRTDTVDLRKE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 68 walsaaarqrlrarIGLVHQAP-PLPprqrvvsavlagrlgqwplWKSLVSLVYPLDRAGAHDAlQRLD----------- 135
Cdd:PRK14239 88 --------------IGMVFQQPnPFP-------------------MSIYENVVYGLRLKGIKDK-QVLDeavekslkgas 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 136 ----LGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAG 183
Cdd:PRK14239 134 iwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
15-205 |
4.10e-16 |
|
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: 74.56 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsaAARQRLRARIGLVHQAPPLPPR 94
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRLGqwplwkslvslvYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:cd03268 87 LTARENLRLLARL------------LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190
....*....|....*....|....*....|.
gi 15598510 175 SAMDPVLAGHTLALLNREaAARGSTLLASLH 205
Cdd:cd03268 155 NGLDPDGIKELRELILSL-RDQGITVLISSH 184
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-226 |
4.17e-16 |
|
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: 76.76 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 34 LIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsAAARQRLRARIGLVHQAPPLPPRQRVVSAVLAGrLGQWPLWK 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGED-----VTNVPPHLRHINMVFQSYALFPHMTVEENVAFG-LKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 114 SLVslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVL---AGHTLALLN 190
Cdd:TIGR01187 75 AEI-------KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLrdqMQLELKTIQ 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598510 191 REAaarGSTLLASLHAVDLALQHFPRVIGLRAGRIA 226
Cdd:TIGR01187 148 EQL---GITFVFVTHDQEEAMTMSDRIAIMRKGKIA 180
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-225 |
5.19e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.22 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrarIGLVH----QAPPLPPR 94
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEE---------------IRLKPdrdgELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 Q--RVVSavlagRLG----QWPLWKSLVSL---------VYPLDRAGAHDA----LQRLDLGDKLFQRCDQLSGGQLQRV 155
Cdd:COG4598 89 QlqRIRT-----RLGmvfqSFNLWSHMTVLenvieapvhVLGRPKAEAIERaealLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVM-RDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-178 |
5.41e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 76.34 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPWALSaaarqrlra 80
Cdd:COG1118 1 MSIEVRNIS-KRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRDLFTN--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 riglvhqappLPPRQRVVsavlaGRLGQWP-LWKSL-----VSL---VYPLDRAGAHDALQRL-------DLGDklfQRC 144
Cdd:COG1118 70 ----------LPPRERRV-----GFVFQHYaLFPHMtvaenIAFglrVRPPSKAEIRARVEELlelvqleGLAD---RYP 131
|
170 180 190
....*....|....*....|....*....|....
gi 15598510 145 DQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:COG1118 132 SQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-225 |
8.02e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLV--HADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLaSQWRPSAGRVELLGEEpwaLSAAARQRLRA 80
Cdd:PRK11174 348 VTIEAEDLEilSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-LGFLPYQGSLKINGIE---LRELDPESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQAPPLPPrQRVVSAVLAGR--LGQWPLWKSlvslvypLDRAGAHDALQRLDLG-DKLFQrcDQ---LSGGQLQR 154
Cdd:PRK11174 424 HLSWVGQNPQLPH-GTLRDNVLLGNpdASDEQLQQA-------LENAWVSEFLPLLPQGlDTPIG--DQaagLSVGQAQR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNReaAARGSTLLASLHAVDlALQHFPRVIGLRAGRI 225
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVTHQLE-DLAQWDQIWVMQDGQI 561
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
9.25e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADG-QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRA 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQP--IADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQapplppRQRVVSAVLAGRLgqwplwkslvslvyPLDRAGAHD-----ALQRLDLGdKLFQRCD---------- 145
Cdd:PRK11160 415 AISVVSQ------RVHLFSATLRDNL--------------LLAAPNASDealieVLQQVGLE-KLLEDDKglnawlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 146 -QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNreAAARGSTLLASLHAVdLALQHFPRVIGLRAGR 224
Cdd:PRK11160 474 rQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRL-TGLEQFDRICVMDNGQ 550
|
.
gi 15598510 225 I 225
Cdd:PRK11160 551 I 551
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-205 |
9.66e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaAARQRLRAR 81
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP------TRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQA-------PPLpprqrVVSAVLAGRLGQwplwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQR 154
Cdd:PRK15056 80 VAYVPQSeevdwsfPVL-----VEDVVMMGRYGH----MGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLH 205
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEGKTMLVSTH 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-210 |
1.90e-15 |
|
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: 72.78 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglVHQAPPLPP 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP------------------LAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKSLVSLVYPLDRA--GAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:TIGR01189 73 ENILYLGHLPGLKPELSALENLHFWAAIHGGAqrTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598510 172 EPVSAMDPvlAGHTL--ALLNREAAARGSTLLASLHAVDLA 210
Cdd:TIGR01189 153 EPTTALDK--AGVALlaGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-234 |
2.57e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLPPRQRVV 98
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT---INLVRDKDGQLKVADKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 savlagrLGQWPLWKSLVSL---------VYPLDRAGAHDA----LQRLDLGDKLFQRCD-QLSGGQLQRVGIARVLYQR 164
Cdd:PRK10619 98 -------FQHFNLWSHMTVLenvmeapiqVLGLSKQEARERavkyLAKVGIDERAQGKYPvHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 165 AELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
2.87e-15 |
|
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: 75.09 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaaRQRLRAR 81
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD---QDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPPRQrVVSAVLAGRLGQWP--LWKSlvslvypLDRAGAHDALQRLD--LGDKLFQRCDQLSGGQLQRVGI 157
Cdd:TIGR02868 411 VSVCAQDAHLFDTT-VRENLRLARPDATDeeLWAA-------LERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLNreAAARGSTLLASLH 205
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLL--AALSGRTVVLITH 528
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-226 |
2.91e-15 |
|
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: 73.03 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPL-- 91
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAIGVVPQDTVLfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 -------------PPRQRVVSAVLAGRLgqwplwkslvslvypldragaHDALQRLDLG--DKLFQRCDQLSGGQLQRVG 156
Cdd:cd03253 89 dtigynirygrpdATDEEVIEAAKAAQI---------------------HDKIMRFPDGydTIVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 157 IARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLA-SLHAV---DLalqhfprVIGLRAGRIA 226
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAhRLSTIvnaDK-------IIVLKDGRIV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-180 |
5.02e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 72.76 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLAsqwR-----PSA---GRVELLGEE-------P 67
Cdd:COG1117 12 IEVRNLN-VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN---RmndliPGArveGEILLDGEDiydpdvdV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 68 WALsaaarqrlRARIGLVHQAP-PLPprqrvvsavlagrlgqwplwKSL---VslVYPLDRAGAHD----------ALQR 133
Cdd:COG1117 88 VEL--------RRRVGMVFQKPnPFP--------------------KSIydnV--AYGLRLHGIKSkseldeiveeSLRK 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 134 LDL----GDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPV 180
Cdd:COG1117 138 AALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-178 |
6.53e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADGQrALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarqRLRA 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-----ARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 RIGLVHQ-----------------APPLPPRQRVVSAVLAGRLGQwplWKSLVSLVYPLDRAGAhdalqrldlgdklfqr 143
Cdd:PRK10851 75 KVGFVFQhyalfrhmtvfdniafgLTVLPRRERPNAAAIKAKVTQ---LLEMVQLAHLADRYPA---------------- 135
|
170 180 190
....*....|....*....|....*....|....*
gi 15598510 144 cdQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK10851 136 --QLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-234 |
7.58e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQwRPSAGRVELLGEEPWALSAAArqrlrarigLVHQAPPLPPRQRVV 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAE---------LARHRAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVlagrlgqwPLWKSLvSLVYP--LDRAGAHDAL----QRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ-------RA 165
Cdd:COG4138 82 FAM--------PVFQYL-ALHQPagASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 166 ELILADEPVSAMDpvlAGHTLALLN--REAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:COG4138 153 QLLLLDEPMNSLD---VAQQAALDRllRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-223 |
9.71e-15 |
|
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: 71.34 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARqrlrarigLVHQAPPLPP----R 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPwltvR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAgrlgqwplwkSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:TIGR01184 73 ENIALAVDR----------VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598510 175 SAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAG 223
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-225 |
1.03e-14 |
|
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: 73.57 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSL----LRVLasqwrPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAP--P 90
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPfgS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 LPPRQRVVSAVLAGrlgqwplwksLVSLVYPLDRAG----AHDALQRLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRA 165
Cdd:COG4172 375 LSPRMTVGQIIAEG----------LRVHGPGLSAAErrarVAEALEEVGLDPAARHRYpHEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 166 ELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHavDL----ALQHfpRVIGLRAGRI 225
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH--DLavvrALAH--RVMVMKDGKV 504
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-228 |
1.14e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrarigLVHqappLPP 93
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-----------------ITH----VPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAgrlgQWPLWKSLVslVY------------PLD--RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIAR 159
Cdd:PRK09452 84 ENRHVNTVFQ----SYALFPHMT--VFenvafglrmqktPAAeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 160 VLYQRAELILADEPVSAMDPVL---AGHTLALLNREAaarGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLrkqMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-247 |
1.25e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAP--PLPPR 94
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPlaSLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVvsavlaGRLGQWPLwkslvSLVYP-LDRAGAHDALQ----RLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK15079 115 MTI------GEIIAEPL-----RTYHPkLSRQEVKDRVKammlKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 169 LADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHavDLAL-QHFP-RVIGLRAGRiafdlpagEVDRAALDALYANE 246
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAVvKHISdRVLVMYLGH--------AVELGTYDEVYHNP 253
|
.
gi 15598510 247 Q 247
Cdd:PRK15079 254 L 254
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-224 |
1.26e-14 |
|
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: 70.58 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG------EEPWALSaaarqrlrariGLVHQ---- 87
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsiayvsQEPWIQN-----------GTIREnilf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 -APPLPPR-QRVVSAVLagrlgqwplwkslvslvypLDRagahDaLQRLDLGDKLF--QRCDQLSGGQLQRVGIARVLYQ 163
Cdd:cd03250 89 gKPFDEERyEKVIKACA-------------------LEP----D-LEILPDGDLTEigEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 164 RAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLaLQHFPRVIGLRAGR 224
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-225 |
1.60e-14 |
|
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: 72.91 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWA----LSAAARQRLRARIGLVHQAPPLP 92
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVdmtkPGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 PrQRVVSAVLAGRLG-QWPLWKSLVSLVYPLDRAGAHDALQRLDLgDKLfqrCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:TIGR03269 378 P-HRTVLDNLTEAIGlELPDELARMKAVITLKMVGFDEEKAEEIL-DKY---PDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 172 EPVSAMDPVLaghTLALLNREAAAR---GSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:TIGR03269 453 EPTGTMDPIT---KVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-225 |
2.23e-14 |
|
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: 72.44 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLPp 93
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD---LADYTLASLRRQVALVSQDVVLF- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKSLVSLVypldRAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:TIGR02203 419 NDTIANNIAYGRTEQADRAEIERALA----AAYAQDFVDKLPLGldTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598510 172 EPVSAMDPVLAGHTLALLnrEAAARGSTLLASLHAVDlALQHFPRVIGLRAGRI 225
Cdd:TIGR02203 495 EATSALDNESERLVQAAL--ERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-178 |
3.20e-14 |
|
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: 69.81 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRARIGLVHQAPPLPPRQrvV 98
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKP--ISQYEHKYLHSKVSLVGQEPVLFARS--L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQwplwKSLVSLVYPLDRAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:cd03248 105 QDNIAYGLQS----CSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
..
gi 15598510 177 MD 178
Cdd:cd03248 181 LD 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-210 |
3.41e-14 |
|
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: 69.44 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELlgeEPWALSAAARQRLRARIGLVHQAPplpp 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL---NGGPLDFQRDSIARGLLYLGHAPG---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 rqrvVSAVLAGRlgqwplwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:cd03231 84 ----IKTTLSVL-------ENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598510 174 VSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLA 210
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-225 |
3.56e-14 |
|
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: 70.06 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQrlrarIGLVHQAPPLPPRQRVV 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-----ISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGrlgqwpLWKSLVSlvYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:cd03299 90 KNIAYG------LKKRKVD--KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598510 179 PVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-205 |
4.67e-14 |
|
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: 69.39 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 12 HADGQR--ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPW-----ALSAAARQRLRARIGL 84
Cdd:COG4778 18 LQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqASPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 85 VHQAPPLPPRqrvVSA--VLAgrlgqwplwKSLVSLVYPLD--RAGAHDALQRLDLGDKLFqrcdQL-----SGGQLQRV 155
Cdd:COG4778 98 VSQFLRVIPR---VSAldVVA---------EPLLERGVDREeaRARARELLARLNLPERLW----DLppatfSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLH 205
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFH 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-233 |
6.37e-14 |
|
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: 68.94 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG----EEPwalsaaarQRLRARIGLVHQAP 89
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREP--------REVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 PLPP----RQRVvsaVLAGRLGQWPlWKSLvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRA 165
Cdd:cd03265 83 SVDDeltgWENL---YIHARLYGVP-GAER--------RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 166 ELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGE 233
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-262 |
7.67e-14 |
|
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: 70.87 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLR-ARIGLVHQAP- 89
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 ----PLPPRQRVVSAVLA--GRLGQWPLWKSLVSLvypLDRAGAHDALQRLDlgdklfQRCDQLSGGQLQRVGIARVLYQ 163
Cdd:COG4172 103 tslnPLHTIGKQIAEVLRlhRGLSGAAARARALEL---LERVGIPDPERRLD------AYPHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 164 RAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHavDLAL-QHFP-RVIGLRAGRIafdlpageVDRAALDA 241
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH--DLGVvRRFAdRVAVMRQGEI--------VEQGPTAE 243
|
250 260 270
....*....|....*....|....*....|...
gi 15598510 242 LYANEQ-------LQAE-----RASPAGEPAVM 262
Cdd:COG4172 244 LFAAPQhpytrklLAAEprgdpRPVPPDAPPLL 276
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-178 |
1.13e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAP--PLPPR 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPygSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRvVSAVLAGrlgqwPLwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQL-SGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK11308 109 KK-VGQILEE-----PL-LINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEP 181
|
....*
gi 15598510 174 VSAMD 178
Cdd:PRK11308 182 VSALD 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-228 |
1.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARI 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLAgrLGQWPLWKSLVSLVYPLDRagahdALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:PRK13644 80 GIVFQNPETQFVGRTVEEDLA--FGPENLCLPPIEIRKRVDR-----ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 163 QRAELILADEPVSAMDPVlAGHTLALLNREAAARGSTLLASLHAVDlALQHFPRVIGLRAGRIAFD 228
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLE 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-239 |
1.35e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PW-ALSaaarqrlrARIGLVHQAPP 90
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsPRdAIA--------LGIGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 LPPRQRVVSAVLAGRLGQWPLWkslvslvypLDRAGAHDALQRL--------DLGDKLfqrcDQLSGGQLQRVGIARVLY 162
Cdd:COG3845 91 LVPNLTVAENIVLGLEPTKGGR---------LDRKAARARIRELserygldvDPDAKV----EDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAE-LILaDEPVSAMDPVLAGHTLALLNREAAARGSTLLAS--LHAVdLALQHfpRVIGLRAGRIAFDLPAGEVDRAAL 239
Cdd:COG3845 158 RGARiLIL-DEPTAVLTPQEADELFEILRRLAAEGKSIIFIThkLREV-MAIAD--RVTVLRRGKVVGTVDTAETSEEEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-218 |
1.99e-13 |
|
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: 69.45 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVL--ASQWRPSAGRV----------------ELLGE---------E 66
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 67 P-----WALSAAARQRLRARIGLVHQAP-PLPPRQRVVSAVLagrlgqwplwKSLVSLVYPLDRA--GAHDALQRLDLGD 138
Cdd:TIGR03269 91 PeevdfWNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVL----------EALEEIGYEGKEAvgRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 139 KLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASlhavdlalQHFPRVI 218
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT--------SHWPEVI 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-260 |
2.70e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLPPR 94
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS--PRDAQAAGIAIIHQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLagrLGQWPLWKSLVSlvYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:COG1129 94 LSVAENIF---LGREPRRGGLID--WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 175 SAMDPVLAGHTLALLnREAAARG-STLLASlHAVDLALQHFPRVIGLRAGRIAFDLPAGEVDRAAL------DALyanEQ 247
Cdd:COG1129 169 ASLTEREVERLFRII-RRLKAQGvAIIYIS-HRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELvrlmvgREL---ED 243
|
250
....*....|...
gi 15598510 248 LQAERASPAGEPA 260
Cdd:COG1129 244 LFPKRAAAPGEVV 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-173 |
4.64e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVElLGEEpwalsaaarqrlrARI 82
Cdd:COG0488 316 LELEGLS-KSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGET-------------VKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAP-PLPPRQRVVSAVLAGRLGqwplwkslvslvypLDRAGAHDALQRLDL-GDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:COG0488 381 GYFDQHQeELDPDKTVLDELRDGAPG--------------GTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKL 446
|
170
....*....|...
gi 15598510 161 LYQRAELILADEP 173
Cdd:COG0488 447 LLSPPNVLLLDEP 459
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-229 |
4.73e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLR-ARIGLVHQAPPLPPRQRV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAVlagrlgQWPLwksLVSLVYPLD-RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:PRK11629 105 LENV------AMPL---LIGKKKPAEiNSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 177 MDPVLAGHTLALLNREAAARGSTLLASLHAVDLAlQHFPRVIGLRAGRIAFDL 229
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA-KRMSRQLEMRDGRLTAEL 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-228 |
5.55e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarQRLRARIGLVhqapplpprqr 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR----KEFARRIGVV----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 vvsavlagrLGQ-----W--PLWKS--LVSLVYPLDRAGAHDAL----QRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ 163
Cdd:COG4586 101 ---------FGQrsqlwWdlPAIDSfrLLKAIYRIPDAEYKKRLdelvELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 164 RAELILADEPVSAMDpVLAGHT----LALLNREaaaRGSTLLASLHAVD----LAlqhfPRVIGLRAGRIAFD 228
Cdd:COG4586 172 RPKILFLDEPTIGLD-VVSKEAirefLKEYNRE---RGTTILLTSHDMDdieaLC----DRVIVIDHGRIIYD 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-180 |
6.41e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVL--ASQWRPSA---GRVELLGEEPWAlSAAARQRLRARIGLVHQAP-PL 91
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPnPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 P----------PR----QRVVSAVLAGRLGQWPLWKslvslvypldragahdalqrlDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:PRK14243 104 PksiydniaygARingyKGDMDELVERSLRQAALWD---------------------EVKDKLKQSGLSLSGGQQQRLCI 162
|
170 180
....*....|....*....|...
gi 15598510 158 ARVLYQRAELILADEPVSAMDPV 180
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPI 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-210 |
6.79e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRAR-IGLVHQA----PPLPP 93
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSfmliPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRV-VSAVLAGRLGQWplwkslvslvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK10584 106 LENVeLPALLRGESSRQ-------------SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598510 173 PVSAMDPVLAGHTLALL---NREAAargSTLLASLHAVDLA 210
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLfslNREHG---TTLILVTHDLQLA 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-234 |
1.13e-12 |
|
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: 65.22 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalSAAARQRLRAR 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLP----PRQRVVsavLAGRLGQWPLWKslvslvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGI 157
Cdd:cd03263 77 LGYCPQFDALFdeltVREHLR---FYARLKGLPKSE---------IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARgSTLLASlhavdlalqHFPRVIGLRAGRIAFdLPAGEV 234
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR-SIILTT---------HSMDEAEALCDRIAI-MSDGKL 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-178 |
1.31e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.67 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQrlrarIGLVHQAPPLPPRQRVVSA 100
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-----ICMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 101 VLAGrlgqwplwksLVSLVYPLD--RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK11432 99 VGYG----------LKMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-205 |
2.20e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 5 LDGVDLVHADGQRAL-ADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwalsaaarqRLRARIG 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---------DDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPPRQRVVSAV-----LAGRLGQwplwkslvslvyplDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIA 158
Cdd:PRK13539 74 ACHYLGHRNAMKPALTVAenlefWAAFLGG--------------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598510 159 RVLYQRAELILADEPVSAMDPvlagHTLAL---LNREAAARGSTLLASLH 205
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDA----AAVALfaeLIRAHLAQGGIVIAATH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-227 |
2.85e-12 |
|
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: 63.72 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSA--GRVeLLGEEPwalsaAARQRLRARIGLVHQAPPLPPRQR 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEV-LINGRP-----LDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAvlagrlgqwpLWKSLvslvypldragahdalqrldlgdklfqRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:cd03213 99 VRET----------LMFAA---------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 177 MDPVLAGHTLALLnREAAARGSTLLASLHAV-DLALQHFPRVIGLRAGRIAF 227
Cdd:cd03213 142 LDSSSALQVMSLL-RRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIY 192
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-227 |
3.02e-12 |
|
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: 64.21 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSA---GRVELLGEEPwalsaaARQRLRARIGLVHQ----AP 89
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR------KPDQFQKCVAYVRQddilLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 PLPPRQRVV-SAVLAGRLGQWPLWKSLVSLVYPLDRAgahdALQRLdlGDKLFQrcdQLSGGQLQRVGIARVLYQRAELI 168
Cdd:cd03234 95 GLTVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDL----ALTRI--GGNLVK---GISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 169 LADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHA--VDLaLQHFPRVIGLRAGRIAF 227
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTL-SQLARRNRIVILTIHQprSDL-FRLFDRILLLSSGEIVY 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-197 |
3.46e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLvHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRP---SAGRVELLGEEPWALSAAARQrl 78
Cdd:COG4136 1 MLSLENLTI-TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 rarIGLVHQAPPLPPRQRVVSAV---LAGRLGQwplwkslvslvyPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRV 155
Cdd:COG4136 78 ---IGILFQDDLLFPHLSVGENLafaLPPTIGR------------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARG 197
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRG 184
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-225 |
3.64e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADG----QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWA-LSAAAR 75
Cdd:PRK13641 1 MSIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 76 QRLRARIGLVHQappLPPRQRVVSAVLAG-RLGqwPLwkslvSLVYPLDRA--GAHDALQRLDLGDKLFQRCD-QLSGGQ 151
Cdd:PRK13641 81 KKLRKKVSLVFQ---FPEAQLFENTVLKDvEFG--PK-----NFGFSEDEAkeKALKWLKKVGLSEDLISKSPfELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 152 LQRVGIARVLYQRAELILADEPVSAMDPvLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDP-EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-225 |
4.54e-12 |
|
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: 64.10 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPL------- 91
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRSQIGLVSQEPVLfdgtiae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 ------PPRQrVVSAVLAGRLgqwplwkslvslvypldrAGAHDALQRL-DLGDKLF-QRCDQLSGGQLQRVGIARVLYQ 163
Cdd:cd03249 96 nirygkPDAT-DEEVEEAAKK------------------ANIHDFIMSLpDGYDTLVgERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 164 RAELILADEPVSAMDPVLAGHTLALLNReaAARGSTLLASLHAVdLALQHFPRVIGLRAGRI 225
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNGQV 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-228 |
4.91e-12 |
|
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: 64.37 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPwaLSAAARQRLRAR 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPP--------------------LPP---RQRVvsavlagrlgqwplwkslvslvypldragaHDALQRLDLGD 138
Cdd:TIGR04520 79 VGMVFQNPDnqfvgatveddvafglenlgVPReemRKRV------------------------------DEALKLVGMED 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 139 KLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDP-----VLAghTLALLNREaaaRGSTLLASLHAVDLALQH 213
Cdd:TIGR04520 129 FRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPkgrkeVLE--TIRKLNKE---EGITVISITHDMEEAVLA 203
|
250
....*....|....*
gi 15598510 214 fPRVIGLRAGRIAFD 228
Cdd:TIGR04520 204 -DRVIVMNKGKIVAE 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-207 |
4.98e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRAL-ADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPP 93
Cdd:PRK11831 18 GNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVlagrlgQWPLwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK11831 98 DMNVFDNV------AYPL-REHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|....
gi 15598510 174 VSAMDPVLAGHTLALLNREAAARGSTLLASLHAV 207
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-177 |
5.63e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHAdGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE-----PWAlsaaarqR 77
Cdd:PRK10762 5 LQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtfngPKS-------S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 78 LRARIGLVHQAPPLPPRQRVVSAVLAGR--LGQWP--LWKSLvslvypldRAGAHDALQRLDLGDKLFQRCDQLSGGQLQ 153
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQLTIAENIFLGRefVNRFGriDWKKM--------YAEADKLLARLNLRFSSDKLVGELSIGEQQ 148
|
170 180
....*....|....*....|....
gi 15598510 154 RVGIARVLYQRAELILADEPVSAM 177
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-201 |
6.26e-12 |
|
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: 62.45 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 8 VDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglvhq 87
Cdd:cd03215 5 LEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVvsavlagRLGqwplwkslVSLVyPLDRAGaHDALQRLDLGDKLFQRCdQLSGGQLQRVGIARVLYQRAEL 167
Cdd:cd03215 64 VTRRSPRDAI-------RAG--------IAYV-PEDRKR-EGLVLDLSVAENIALSS-LLSGGNQQKVVLARWLARDPRV 125
|
170 180 190
....*....|....*....|....*....|....
gi 15598510 168 ILADEPVSAMDpVLAGHTLALLNREAAARGSTLL 201
Cdd:cd03215 126 LILDEPTRGVD-VGAKAEIYRLIRELADAGKAVL 158
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-173 |
6.85e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.70 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLvHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgeepwalsaaarqrlrari 82
Cdd:cd03221 1 IELENLSK-TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 glvhqapplpprqrvvsavlagrlgqwplWKSLVSLVYpldragahdalqrldlgdklFqrcDQLSGGQLQRVGIARVLY 162
Cdd:cd03221 59 -----------------------------WGSTVKIGY--------------------F---EQLSGGEKMRLALAKLLL 86
|
170
....*....|.
gi 15598510 163 QRAELILADEP 173
Cdd:cd03221 87 ENPNLLLLDEP 97
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-178 |
7.75e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLvHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALsaaarqrlrari 82
Cdd:PRK10247 8 LQLQNVGY-LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 glvhqaPPLPPRQRVVSAVlagrlgQWP-LWKSLV--SLVYPL-------DRAGAHDALQRLDLGDKLFQ-RCDQLSGGQ 151
Cdd:PRK10247 75 ------KPEIYRQQVSYCA------QTPtLFGDTVydNLIFPWqirnqqpDPAIFLDDLERFALPDTILTkNIAELSGGE 142
|
170 180
....*....|....*....|....*..
gi 15598510 152 LQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-239 |
9.16e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrarI 82
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED---------------I 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GlvhqapPLPPRQRV---VSAVLAGRLGQ-----WPLWKSLVSLVY---PLDRAG----------AHDALQRLDL-GDKL 140
Cdd:COG3845 323 T------GLSPRERRrlgVAYIPEDRLGRglvpdMSVAENLILGRYrrpPFSRGGfldrkairafAEELIEEFDVrTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 141 FQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDpvlAGHTLALLNR--EAAARGST-LLASlhaVDL--ALQHFP 215
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRllELRDAGAAvLLIS---EDLdeILALSD 470
|
250 260
....*....|....*....|....
gi 15598510 216 RVIGLRAGRIAFDLPAGEVDRAAL 239
Cdd:COG3845 471 RIAVMYEGRIVGEVPAAEATREEI 494
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-225 |
1.06e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALS-AAARQRLRARIGLVHQAPPLPPRQR 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAVLAGRlgqwplwkSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:PRK10070 123 VLDNTAFGM--------ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598510 177 MDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-212 |
1.12e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQ--WRPSAGRVELlgeepwalsaaarqrlrariglvhQAPPLPP 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDV------------------------PDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVlagrlgqwPLWKSLVSLVYPLDRAGAHDALqrldlgdkLFQRC-DQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:COG2401 99 EASLIDAI--------GRKGDFKDAVELLNAVGLSDAV--------LWLRRfKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDL--ALQ 212
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVidDLQ 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-178 |
1.17e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRAL-ADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPplpp 93
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP---IRRQRDEYHQDLLYLGHQPG---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 rqrvvsavLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK13538 85 --------IKTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
....*
gi 15598510 174 VSAMD 178
Cdd:PRK13538 157 FTAID 161
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
1.41e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpWALSAAARQRLRARIGLVHQapplPPRQR 96
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKD-EKNKKKTKEKEKVLEKLVIQ----KTRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAV--LAGRLG------QWPLWKSL---------VSLVYPLDRAG--AHDALQRLDLGDKLFQRCD-QLSGGQLQRVG 156
Cdd:PRK13651 96 KIKKIkeIRRRVGvvfqfaEYQLFEQTiekdiifgpVSMGVSKEEAKkrAAKYIELVGLDESYLQRSPfELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 157 IARVLYQRAELILADEPVSAMDPVLAGHTLALLNrEAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD-NLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKD 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-228 |
1.70e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.16 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaarqrlrARIGLVhqaPPLPPRQR 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG--------LGGGFN---PELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVsavlagrlgqwplwksLVSLVYPLDRAGAHDALQRL----DLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03220 105 IY----------------LNGRLLGLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLASlHAVDLALQHFPRVIGLRAGRIAFD 228
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-224 |
1.79e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHAD----GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalSAAARQ 76
Cdd:PRK13536 35 GSMSTVAIDLAGVSksygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP----VPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 RLRARIGLVHQAPPLPPRQRVVSAVLA-GRLgqWPLWKSLVSLVYPldragahDALQRLDLGDKLFQRCDQLSGGQLQRV 155
Cdd:PRK13536 111 LARARIGVVPQFDNLDLEFTVRENLLVfGRY--FGMSTREIEAVIP-------SLLEFARLESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPvLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDP-HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-209 |
1.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.90 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPlpprQRV 97
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP---ITKENIREVRKFVGLVFQNPD----DQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAVLAGRLGQWPLWKSLVslvyplDRAGAH---DALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPV 174
Cdd:PRK13652 92 FSPTVEQDIAFGPINLGLD------EETVAHrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190
....*....|....*....|....*....|....*
gi 15598510 175 SAMDPVLAGHTLALLNREAAARGSTLLASLHAVDL 209
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-178 |
2.93e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLP 92
Cdd:PRK13657 345 DNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD---IRTVTRASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 PRQrVVSAVLAGRLGqwplwKSLVSLVYPLDRAGAHDALQRLDLGDKLF--QRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK13657 422 NRS-IEDNIRVGRPD-----ATDEEMRAAAERAQAHDFIERKPDGYDTVvgERGRQLSGGERQRLAIARALLKDPPILIL 495
|
....*...
gi 15598510 171 DEPVSAMD 178
Cdd:PRK13657 496 DEATSALD 503
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-180 |
3.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVL------ASQWRPSaGRVELLGEEPWAlSAAARQRLRARIGLVHQ 87
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVE-GRVEFFNQNIYE-RRVNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVVSAVLAGRLGQWPLWKSLVSLVypldragaHDALQRLDLGD----KLFQRCDQLSGGQLQRVGIARVLYQ 163
Cdd:PRK14258 96 KPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIV--------ESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARALAV 167
|
170
....*....|....*..
gi 15598510 164 RAELILADEPVSAMDPV 180
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPI 184
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-179 |
3.92e-11 |
|
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: 61.09 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAP-------- 89
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID---IRDISRKSLRSMIGVVLQDTflfsgtim 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 -------PLPPRQRVVSAvlagrlgqwplwkslvslvypLDRAGAHDALQRL--DLGDKLFQRCDQLSGGQLQRVGIARV 160
Cdd:cd03254 95 enirlgrPNATDEEVIEA---------------------AKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARA 153
|
170
....*....|....*....
gi 15598510 161 LYQRAELILADEPVSAMDP 179
Cdd:cd03254 154 MLRDPKILILDEATSNIDT 172
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-178 |
4.18e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRARIGLVHQAPPLppRQRVV 98
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-LLDGVP--LVQYDHHYLHRQVALVGQEPVL--FSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQWPLWKSLVSLVypldRAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAK----AANAHDFIMEFPNGydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
..
gi 15598510 177 MD 178
Cdd:TIGR00958 648 LD 649
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-244 |
5.17e-11 |
|
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: 61.00 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrari 82
Cdd:TIGR03410 1 LEVSNLN-VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGED---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 glvhqAPPLPPRQRV---VSAVLAGR--LGQWPLWKSLVSLVYPLDRAGAH---DALQRLD-LGDKLFQRCDQLSGGQLQ 153
Cdd:TIGR03410 64 -----ITKLPPHERAragIAYVPQGReiFPRLTVEENLLTGLAALPRRSRKipdEIYELFPvLKEMLGRRGGDLSGGQQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 154 RVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGE 233
Cdd:TIGR03410 139 QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
250
....*....|.
gi 15598510 234 VDRAALDALYA 244
Cdd:TIGR03410 219 LDEDKVRRYLA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-180 |
6.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLAS--QWRPSA---GRVELLGEEPWALSAAARQRLrarIGLVHQAP-PLP 92
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIELRRR---VQMVFQIPnPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 PRQRVVSAVLAGRLGQwpLWKSLVSLvypldRAGAHDALQRLDLGDKLFQRCD----QLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK14247 96 NLSIFENVALGLKLNR--LVKSKKEL-----QERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVL 168
|
170
....*....|..
gi 15598510 169 LADEPVSAMDPV 180
Cdd:PRK14247 169 LADEPTANLDPE 180
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-225 |
7.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.29 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQR-LRARIGLVHQAPPLPP 93
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKSLVSLVypldragAHDALQRLDLGDKLFQRCD-QLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKEKAEKI-------AAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 173 PVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK13643 171 PTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-177 |
7.99e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLPPR 94
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD--HKLAAQLGIGIIYQELSVIDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRLgqwPLWKSL-VSLV-YPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK09700 95 LTVLENLYIGRH---LTKKVCgVNIIdWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
....*
gi 15598510 173 PVSAM 177
Cdd:PRK09700 172 PTSSL 176
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-225 |
8.25e-11 |
|
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: 60.25 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrarigLVHqappLPPRQR 96
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-----------------ITK----LPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 vvsAVLA-GRLGQWP-LWKSL--------VSLVYPLDRAGAHDA----LQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:cd03218 73 ---ARLGiGYLPQEAsIFRKLtveenilaVLEIRGLSKKEREEKleelLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 163 QRAELILADEPVSAMDPvLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:cd03218 150 TNPKFLLLDEPFAGVDP-IAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-211 |
1.12e-10 |
|
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: 60.46 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DLVHADGQRALADIRLRLAA-GERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllGEEPW----------ALSAAARQR 77
Cdd:cd03236 5 EPVHRYGPNSFKLHRLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPDWdeildefrgsELQNYFTKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 78 LRARIGLVH--QAPPLPPRQrvvsavLAGRLGQwplwkslvsLVYPLDRAGAHDAL-QRLDLGDKLFQRCDQLSGGQLQR 154
Cdd:cd03236 83 LEGDVKVIVkpQYVDLIPKA------VKGKVGE---------LLKKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDpVLAGHTLALLNREAAARGSTLLASLHavDLAL 211
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLD-IKQRLNAARLIRELAEDDNYVLVVEH--DLAV 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-180 |
1.67e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDL-VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLAS--QWRPSA---GRVELLGEEPWAlSAAA 74
Cdd:PRK14267 1 MKFAIETVNLrVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNIYS-PDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 75 RQRLRARIGLVHQAPPLPPRQRVVSAVLAGrLGQWPLWKSLVSLVYPLDRAGAHDALQRlDLGDKLFQRCDQLSGGQLQR 154
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELDERVEWALKKAALWD-EVKDRLNDYPSNLSGGQRQR 157
|
170 180
....*....|....*....|....*.
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDPV 180
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPV 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-179 |
1.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADGQ----RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSA-AAR 75
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 76 QRLRARIGLVHQAP-------------PLPPRQRVVSAVLAGRLgqwplwkslvslvypldragAHDALQRLDLGDKLFQ 142
Cdd:PRK13649 81 KQIRKKVGLVFQFPesqlfeetvlkdvAFGPQNFGVSQEEAEAL--------------------AREKLALVGISESLFE 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598510 143 RCD-QLSGGQLQRVGIARVLYQRAELILADEPVSAMDP 179
Cdd:PRK13649 141 KNPfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-177 |
2.81e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPWALSaAARQRLRARI 82
Cdd:PRK11288 5 LSFDGIG-KTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-LIDGQEMRFA-STTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQAPPLPPRQRVVSAVLagrLGQWPLWKSLVSlvYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLY 162
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLY---LGQLPHKGGIVN--RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170
....*....|....*
gi 15598510 163 QRAELILADEPVSAM 177
Cdd:PRK11288 157 RNARVIAFDEPTSSL 171
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-251 |
2.82e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPlpprQRVV 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNLRRKIGMVFQNPD----NQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SA-----VLAGRLGQWPLWKSLVSLVypldragaHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK13642 96 GAtveddVAFGMENQGIPREEMIKRV--------DEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 174 VSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHfPRVIGLRAGRIafdlpageVDRAALDALYANEQLQAE 251
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS-DRILVMKAGEI--------IKEAAPSELFATSEDMVE 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-259 |
3.36e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASqwrPSA----GRVELLGEEPW-ALSAAARQRLRARIGLVH 86
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS---PPVvypsGDIRFHGESLLhASEQTLRGVRGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 87 QAP-----PLPPRQRVVSAVLAGRLG--QWPLWKSLVSLvypLDRAGAHDALQRLDlgdklfQRCDQLSGGQLQRVGIAR 159
Cdd:PRK15134 99 QEPmvslnPLHTLEKQLYEVLSLHRGmrREAARGEILNC---LDRVGIRQAAKRLT------DYPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 160 VLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIafdlpageVDRAAL 239
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC--------VEQNRA 241
|
250 260
....*....|....*....|....
gi 15598510 240 DALYANEQLQAER----ASPAGEP 259
Cdd:PRK15134 242 ATLFSAPTHPYTQkllnSEPSGDP 265
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-186 |
5.80e-10 |
|
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: 57.73 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRA-RIGLVHQAPPLpprqrV 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPWL-----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAVLAGRLGQWPLWKSLVSLVypLDRAGAHDALQRLDLGDK--LFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVS 175
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAV--TDACSLQPDIDLLPFGDQteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170
....*....|.
gi 15598510 176 AMDPVLAGHTL 186
Cdd:cd03290 170 ALDIHLSDHLM 180
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-178 |
7.34e-10 |
|
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: 57.80 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGE----EPWALSaaarqrlrariglvhqapplPPRQRVVSAVLAG 104
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtvsyKPQYIK--------------------ADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 105 ---RLGQWPLWKSlvslvypldragahDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:cd03237 85 itkDFYTHPYFKT--------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-224 |
9.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalSAAARQRLRARIGLVHQAPPLPPRQRVVSA 100
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP----VPSRARHARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 101 VLagrlgqwplwksLVSLVYPLDRAGAHDALQRLDLGDKLFQRCD----QLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:PRK13537 101 LL------------VFGRYFGLSAAAARALVPPLLEFAKLENKADakvgELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598510 177 MDPvLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:PRK13537 169 LDP-QARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-197 |
1.01e-09 |
|
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: 58.30 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPP 93
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVVSAVLAGRLGQWPLWKslvsLVYPLDRAGAHDALQRLDLGDKLFQR-CDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:TIGR02633 92 ELSVAENIFLGNEITLPGGR----MAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180
....*....|....*....|....*..
gi 15598510 173 PVSAMDpvlAGHTLALLN--REAAARG 197
Cdd:TIGR02633 168 PSSSLT---EKETEILLDiiRDLKAHG 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
1.24e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 57.31 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPlppRQRV 97
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT---ISKENLKEIRKKIGIIFQNPD---NQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAV-------LAGRLGQWPLWKSLVSlvypldragahDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK13632 98 GATVeddiafgLENKKVPPKKMKDIID-----------DLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 171 DEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHfPRVIGLRAGRI 225
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILA-DKVIVFSEGKL 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-181 |
1.74e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEpwalsaaarqrlrariglvhQAPPLPPRQRVVSA 100
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEK--------------------RMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 101 VLAgrlgQWPLWKSL-----VSLVYPLDRAGAHDALQR-------LDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK11000 80 VFQ----SYALYPHLsvaenMSFGLKLAGAKKEEINQRvnqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170
....*....|...
gi 15598510 169 LADEPVSAMDPVL 181
Cdd:PRK11000 156 LLDEPLSNLDAAL 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-68 |
1.88e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.63 E-value: 1.88e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPW 68
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSA 91
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-180 |
1.97e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLA-------SQWRPSaGRVELLGEEPWALSAAARQRLrarIG 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVD-GKVLYFGKDIFQIDAIKLRKE---VG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPPRQRVVSavlagrlgqwplwkslvSLVYPLDRAGAHD----------ALQRLDLGDKLFQRCD----QLSG 149
Cdd:PRK14246 94 MVFQQPNPFPHLSIYD-----------------NIAYPLKSHGIKEkreikkiveeCLRKVGLWKEVYDRLNspasQLSG 156
|
170 180 190
....*....|....*....|....*....|.
gi 15598510 150 GQLQRVGIARVLYQRAELILADEPVSAMDPV 180
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-224 |
2.26e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 26 LAAGERVALIGPSGAGKTSLLRVLASQWrPSAGRVELLGE--EPWALSaaarqrlrariGLVHQAPPLPPRQRVVSAVla 103
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQplEAWSAA-----------ELARHRAYLSQQQTPPFAM-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 104 grlgqwPLWKSLVSLVYPLDRAGA-----HDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ-------RAELILAD 171
Cdd:PRK03695 85 ------PVFQYLTLHQPDKTRTEAvasalNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598510 172 EPVSAMDpVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGR 224
Cdd:PRK03695 159 EPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-179 |
3.44e-09 |
|
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: 57.07 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 5 LDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgeepwalsaaarqrlrarigl 84
Cdd:TIGR00954 454 FENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT----------------------- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 85 vhqappLPPRQRVVSavlagrLGQWPlWKSLVSL----VYP-----LDRAGAHDA-----LQRLDLGDkLFQR------- 143
Cdd:TIGR00954 511 ------KPAKGKLFY------VPQRP-YMTLGTLrdqiIYPdssedMKRRGLSDKdleqiLDNVQLTH-ILEReggwsav 576
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598510 144 ---CDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDP 179
Cdd:TIGR00954 577 qdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-179 |
3.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVElLGEEpwalsaaarqrlraRIGLVHQAPPLPP-R 94
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGER--------------VITAGKKNKKLKPlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVvsavlaGRLGQWP---LWKSLVS---LVYPLD--------RAGAHDALQRLDLGDKLFQRCD-QLSGGQLQRVGIAR 159
Cdd:PRK13634 85 KKV------GIVFQFPehqLFEETVEkdiCFGPMNfgvseedaKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAG 158
|
170 180
....*....|....*....|
gi 15598510 160 VLYQRAELILADEPVSAMDP 179
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDP 178
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-234 |
3.73e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 34 LIGPSGAGKTSLLRVLASQWRPSAGRVELLGEePWALSAAARQRLRARIGLVHQapplPPRQRVVSAVLAGRLGqwplwK 113
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGLLALRQQVATVFQ----DPEQQIFYTDIDSDIA-----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 114 SLVSLVYPLDRAG--AHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNR 191
Cdd:PRK13638 102 SLRNLGVPEAEITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598510 192 eAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAGEV 234
Cdd:PRK13638 182 -IVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-178 |
4.10e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.51 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRA-LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgeepwalsaaarQRLRARIGLVHQAPPLPP 93
Cdd:PRK09544 15 GQRRvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 rqrvvsavlagrlgQWPLWKSLVSLVYP-LDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK09544 81 --------------TLPLTVNRFLRLRPgTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
....*.
gi 15598510 173 PVSAMD 178
Cdd:PRK09544 147 PTQGVD 152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-179 |
4.79e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVL------ASQWRPSaGRVELLGEEpwALSAAARQRLRARIGLVHQA 88
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYS-GDVLLGGRS--IFNYRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 89 P---PLPPRQRVVSAVLAGRLGQWPLWKSLVSLvyPLDRAGAHDALQrldlgDKLFQRCDQLSGGQLQRVGIARVLYQRA 165
Cdd:PRK14271 110 PnpfPMSIMDNVLAGVRAHKLVPRKEFRGVAQA--RLTEVGLWDAVK-----DRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170
....*....|....
gi 15598510 166 ELILADEPVSAMDP 179
Cdd:PRK14271 183 EVLLLDEPTSALDP 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-234 |
4.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.82 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADG----QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWAlSAAARQ 76
Cdd:PRK13637 1 MSIKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 RLRARIGLVHQAPPLPPRQRVVSAVLA---GRLGqwpLWKSLVSL-VYpldRAGAHDALQRLDLGDKL-FqrcdQLSGGQ 151
Cdd:PRK13637 80 DIRKKVGLVFQYPEYQLFEETIEKDIAfgpINLG---LSEEEIENrVK---RAMNIVGLDYEDYKDKSpF----ELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 152 LQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPA 231
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
...
gi 15598510 232 GEV 234
Cdd:PRK13637 230 REV 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-178 |
5.27e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARI----- 82
Cdd:PRK11701 11 GLTKLYGPRkGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 -GLVHQApplpPRQRVVSAVLAG-----RL---GqwplWKSlvslvYPLDRAGAHDALQRLDLGDKlfqRCDQL----SG 149
Cdd:PRK11701 91 wGFVHQH----PRDGLRMQVSAGgnigeRLmavG----ARH-----YGDIRATAGDWLERVEIDAA---RIDDLpttfSG 154
|
170 180
....*....|....*....|....*....
gi 15598510 150 GQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-182 |
6.82e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLrvlasqwrpSAgrveLLGEEPWALSAAARQRlrariGLVHQAPPLP--PRQR 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLI---------SA----MLGELSHAETSSVVIR-----GSVAYVPQVSwiFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 97 VVSAVLAG-RLGQWPLWKSL--VSLVYPLDRAGAHDalqRLDLGdklfQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PLN03232 695 VRENILFGsDFESERYWRAIdvTALQHDLDLLPGRD---LTEIG----ERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
....*....
gi 15598510 174 VSAMDPVLA 182
Cdd:PLN03232 768 LSALDAHVA 776
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-181 |
8.09e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDlVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEE--PWALSAaarqrlra 80
Cdd:PRK11614 6 LSFDKVS-AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitDWQTAK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 81 rigLVHQAPPLPPRQRVVSAVLAgrlgqwpLWKSLVSLVYPLDRAGAHDALQRL-DLGDKLF----QRCDQLSGGQLQRV 155
Cdd:PRK11614 77 ---IMREAVAIVPEGRRVFSRMT-------VEENLAMGGFFAERDQFQERIKWVyELFPRLHerriQRAGTMSGGEQQML 146
|
170 180
....*....|....*....|....*.
gi 15598510 156 GIARVLYQRAELILADEPVSAMDPVL 181
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPII 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-184 |
9.97e-09 |
|
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: 55.72 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPPRQRVV 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAgrlgqwplwkslvsLVYPLDRAGAHDalqRLDLGDKLFQrcdqLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:TIGR00957 734 LEACA--------------LLPDLEILPSGD---RTEIGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
....*.
gi 15598510 179 PVLAGH 184
Cdd:TIGR00957 793 AHVGKH 798
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-189 |
9.97e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTS----LLRVLASQwrpsaGRVELLGEEPWALSAAARQRLRARIGLVHQAP 89
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 --PLPPRQRVVSAVLAGRLGQWPlwkslvSLVYPLDRAGAHDALQRLDLGDKLFQRC-DQLSGGQLQRVGIARVLYQRAE 166
Cdd:PRK15134 372 nsSLNPRLNVLQIIEEGLRVHQP------TLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPS 445
|
170 180
....*....|....*....|...
gi 15598510 167 LILADEPVSAMDPVLAGHTLALL 189
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALL 468
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-241 |
1.02e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 11 VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSA--------GRVELLGEEPWALSAAARQRLRARI 82
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 GLVHQ-APPLPPRQRVVsavlagrLGQWPLWKSLVSLVYPlDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVL 161
Cdd:PRK13547 89 PQAAQpAFAFSAREIVL-------LGRYPHARRAGALTHR-DGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 162 YQ---------RAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDLPAG 232
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....*....
gi 15598510 233 EVDRAALDA 241
Cdd:PRK13547 241 DVLTPAHIA 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-178 |
1.11e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 4 SLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGrvellgeEPWAlsaaarqRLRARIG 83
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARP-------QPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPPRQRVVSAVLAG---------RLGQW------------PLWKSLVSLVYPLDRAGAHDALQRLDLG-DKLf 141
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGvaeikdaldRFNEIsakyaepdadfdKLAAEQAELQEIIDAADAWDLDSQLEIAmDAL- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598510 142 qRC---DQ----LSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:TIGR03719 151 -RCppwDAdvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-230 |
1.39e-08 |
|
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: 53.65 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLpprqrv 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVD---ISKIGLHDLRSRISIIPQDPVL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 vsavLAG--R-----LGQWP---LWKSlvslvypLDRAGAHDALQRLD--LGDKLFQRCDQLSGGQLQRVGIARVLYQRA 165
Cdd:cd03244 90 ----FSGtiRsnldpFGEYSdeeLWQA-------LERVGLKEFVESLPggLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 166 ELILADEPVSAMDPvlagHTLALLNR--EAAARGSTLLASLHAVDlALQHFPRVIGLRAGRIA-FDLP 230
Cdd:cd03244 159 KILVLDEATASVDP----ETDALIQKtiREAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVeFDSP 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-178 |
1.74e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DLVHADGQRALADIRL-RLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgEEP-W----------ALSAAARQ 76
Cdd:PRK13409 78 EPVHRYGVNGFKLYGLpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE---EEPsWdevlkrfrgtELQNYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 RLRARIGLVHQApplpprQRV--VSAVLAGRLGQwplwkslvsLVYPLDRAGAHDAL-QRLDLGDKLFQRCDQLSGGQLQ 153
Cdd:PRK13409 155 LYNGEIKVVHKP------QYVdlIPKVFKGKVRE---------LLKKVDERGKLDEVvERLGLENILDRDISELSGGELQ 219
|
170 180
....*....|....*....|....*
gi 15598510 154 RVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-180 |
2.22e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLPPR 94
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP--LHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAgrlgqwplwksLVSLVYPLDRAGAHDALQRL-------DLGDKLFQrcdQLSGGQLQRVGIARVLYQRAEL 167
Cdd:PRK10895 93 LSVYDNLMA-----------VLQIRDDLSAEQREDRANELmeefhieHLRDSMGQ---SLSGGERRRVEIARALAANPKF 158
|
170
....*....|...
gi 15598510 168 ILADEPVSAMDPV 180
Cdd:PRK10895 159 ILLDEPFAGVDPI 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-226 |
2.74e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.33 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwALSAAARQRLRARIGLVHQAPPLpprqrv 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSRLAVVSQTPFL------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAVLAGR--LGQWPLWKSLVSLVYPLdrAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK10789 401 FSDTVANNiaLGRPDATQQEIEHVARL--ASVHDDILRLPQGydTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 174 VSAMDpvlaGHT--LALLNREAAARGSTLLASLHAVDlALQHFPRVIGLRAGRIA 226
Cdd:PRK10789 479 LSAVD----GRTehQILHNLRQWGEGRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-227 |
2.79e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.63 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 1 MSLSLDGVDLVHADG----QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGeepwalsaaarq 76
Cdd:PRK13646 1 MTIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 rlrarIGLVHQAPP---LPPRQRVvsavlaGRLGQWP---LWKSLV---------SLVYPLD--RAGAHDALqrLDLG-- 137
Cdd:PRK13646 69 -----ITITHKTKDkyiRPVRKRI------GMVFQFPesqLFEDTVereiifgpkNFKMNLDevKNYAHRLL--MDLGfs 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 138 -DKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPR 216
Cdd:PRK13646 136 rDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADE 215
|
250
....*....|.
gi 15598510 217 VIGLRAGRIAF 227
Cdd:PRK13646 216 VIVMKEGSIVS 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-238 |
3.81e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPS---AGRVELLGE--EPWALSAAArqrlrariGLVHQ----APPLPPRQR-VV 98
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpiDAKEMRAIS--------AYVQQddlfIPTLTVREHlMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLagRLGQwplwkslvSLVYPLDRAGAHDALQRLDLGD------KLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:TIGR00955 123 QAHL--RMPR--------RVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 173 PVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLAL-QHFPRVIGLRAGRIAFdlpAGEVDRAA 238
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVL-KGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAY---LGSPDQAV 255
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-60 |
4.19e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 4.19e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRV 60
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-178 |
6.01e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRARIGLVHQAP--PLPPRQ 95
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHP--LHFGDYSYRSQRIRMIFQDPstSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 96 RVvsavlaGRLGQWPLwkSLVSLVYPLDRAGA-HDALQRLDL-GDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK15112 105 RI------SQILDFPL--RLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
....*
gi 15598510 174 VSAMD 178
Cdd:PRK15112 177 LASLD 181
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-64 |
6.63e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 6.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 4 SLDGVDLVHADgQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG 64
Cdd:NF033858 3 RLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-241 |
7.95e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 20 ADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQWRPSAGRVELLGEEpwalsAAARQRLRARIGLVHQAP-----P 90
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKP-----VAPCALRGRKIATIMQNPrsafnP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 LPP-RQRVVSAVLA-GRLGqwplwkSLVSLVYPLDRAGAHDALQRLDLgdklfqRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK10418 95 LHTmHTHARETCLAlGKPA------DDATLTAALEAVGLENAARVLKL------YPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 169 LADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIA--------FDLPAGEVDRAALD 240
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVeqgdvetlFNAPKHAVTRSLVS 242
|
.
gi 15598510 241 A 241
Cdd:PRK10418 243 A 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-179 |
1.19e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPlpprQRVV 98
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNPD----NQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SA-----VLAGRLGQWPLWKSLVSLVypldragaHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK13650 96 GAtveddVAFGLENKGIPHEEMKERV--------NEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
....*.
gi 15598510 174 VSAMDP 179
Cdd:PRK13650 168 TSMLDP 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-178 |
1.28e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwALSAaarqrlrariglVHQAPPLPPRQRVVSA 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFD------------AEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 101 VLA-GRLgqWPLWKSLVSLVY---PLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:PRK11144 81 VFQdARL--FPHYKVRGNLRYgmaKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
..
gi 15598510 177 MD 178
Cdd:PRK11144 159 LD 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-178 |
1.41e-07 |
|
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: 52.22 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPS------AGRVELLGEEPWALSaaARQRLRARIGLVHQapplp 92
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSegkikhSGRISFSPQTSWIMP--GTIKDNIIFGLSYD----- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 pRQRVVSAVLAGRLgqwplwkslvslvypldragaHDALQRLDLGDK--LFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:TIGR01271 515 -EYRYTSVIKACQL---------------------EEDIALFPEKDKtvLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
....*...
gi 15598510 171 DEPVSAMD 178
Cdd:TIGR01271 573 DSPFTHLD 580
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-228 |
1.48e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLG------EEPWALSAAArqrlrariGLVHQAPPl 91
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKA--------GMVFQNPD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 pprQRVVSAVLAGRLGQWPlwKSLVslVYPLD-RAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK13633 96 ---NQIVATIVEEDVAFGP--ENLG--IPPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598510 171 DEPVSAMDP-----VLagHTLALLNREAaarGSTLLASLHAVDLALQHfPRVIGLRAGRIAFD 228
Cdd:PRK13633 169 DEPTAMLDPsgrreVV--NTIKELNKKY---GITIILITHYMEEAVEA-DRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-225 |
2.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQR-ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSA---GRVELLGEEpwaLSAAARQRL 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGIT---LTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 79 RARIGLVHQAPPlppRQRVVSAV-------LAGRLGQWPLWKSLVslvypldragaHDALQRLDLGDKLFQRCDQLSGGQ 151
Cdd:PRK13640 83 REKVGIVFQNPD---NQFVGATVgddvafgLENRAVPRPEMIKIV-----------RDVLADVGMLDYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 152 LQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLAlQHFPRVIGLRAGRI 225
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-189 |
2.16e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQwrpsAGRVELLGEEPWALSAAARQRLRARIGLVHQAP--PL 91
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSttgrALLRLVESQ----GGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPyaSL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 PPRQRVVSAVLAgrlgqwPLwksLVSLVYPLDRAGAHDA--LQRLDL-GDKLFQRCDQLSGGQLQRVGIARVLYQRAELI 168
Cdd:PRK10261 415 DPRQTVGDSIME------PL---RVHGLLPGKAAAARVAwlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180
....*....|....*....|.
gi 15598510 169 LADEPVSAMDPVLAGHTLALL 189
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLL 506
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-239 |
2.61e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLV-----HQ-- 87
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--PRDAIRAGIAYVpedrkGEgl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APPLPPRQRVVSAVLAgRLGQWPLwkslvslvypLDRAGAHDALQRL--DLGDK---LFQRCDQLSGGQLQRVGIARVLY 162
Cdd:COG1129 342 VLDLSIRENITLASLD-RLSRGGL----------LDRRRERALAEEYikRLRIKtpsPEQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 163 QRAELILADEP-----VSAMDPVlagHTLAllnREAAARG-STLLAS------LHAVDlalqhfpRVIGLRAGRIAFDLP 230
Cdd:COG1129 411 TDPKVLILDEPtrgidVGAKAEI---YRLI---RELAAEGkAVIVISselpelLGLSD-------RILVMREGRIVGELD 477
|
....*....
gi 15598510 231 AGEVDRAAL 239
Cdd:COG1129 478 REEATEEAI 486
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-179 |
2.63e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLrariGLVH--QAPPL---- 91
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM----GVVRtfQHVRLfrem 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 --------PPRQRVVSAVLAGrLGQWPLWKSlvSLVYPLDRAgAHdALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ 163
Cdd:PRK11300 96 tvienllvAQHQQLKTGLFSG-LLKTPAFRR--AESEALDRA-AT-WLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170
....*....|....*.
gi 15598510 164 RAELILADEPVSAMDP 179
Cdd:PRK11300 171 QPEILMLDEPAAGLNP 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-178 |
3.37e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLrvlasqwrpSAgrveLLGEepwalsaaarqrlrariglvhqappLPPRQRVv 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLI---------SA----MLGE-------------------------LPPRSDA- 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQWPLwkslVSLVY------------PLD-----RAGAHDALQR-LDL---GD--KLFQRCDQLSGGQLQRV 155
Cdd:PLN03130 674 SVVIRGTVAYVPQ----VSWIFnatvrdnilfgsPFDperyeRAIDVTALQHdLDLlpgGDltEIGERGVNISGGQKQRV 749
|
170 180
....*....|....*....|...
gi 15598510 156 GIARVLYQRAELILADEPVSAMD 178
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-177 |
3.38e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWrPSA---GRVELLGEEPWALSaaARQRLRARIGLVHQAPP 90
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASN--IRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 LPPRQRVVSAVLagrLGQWPLWKSLVSlvYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK13549 93 LVKELSVLENIF---LGNEITPGGIMD--YDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
....*..
gi 15598510 171 DEPVSAM 177
Cdd:PRK13549 168 DEPTASL 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-212 |
3.73e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 13 ADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVeLLGEEPwaLSAAARQRLRARIGLVHQAPPlp 92
Cdd:PRK13648 19 SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQA--ITDDNFEKLRKHIGIVFQNPD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 pRQRVVSAVlagrlgQWPLWKSLVSLVYPLDRAG--AHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILA 170
Cdd:PRK13648 94 -NQFVGSIV------KYDVAFGLENHAVPYDEMHrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598510 171 DEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQ 212
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-203 |
3.73e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 16 QRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwALSAAARQRLRARIGLVHQA---PPLP 92
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTYQKQLCFVGHRSginPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 PRQrvvsavlagrlgqwplwKSLVSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:PRK13540 91 LRE-----------------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|.
gi 15598510 173 PVSAMDPVLAGHTLALLNREAAARGSTLLAS 203
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTS 184
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
131-225 |
4.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.23 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 131 LQRLDLGDKLFQRCD-QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPvlAG-HTLALLNREAAARGSTLLASLHAVD 208
Cdd:PRK13631 160 LNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP--KGeHEMMQLILDAKANNKTVFVITHTME 237
|
90
....*....|....*..
gi 15598510 209 LALQHFPRVIGLRAGRI 225
Cdd:PRK13631 238 HVLEVADEVIVMDKGKI 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-178 |
5.59e-07 |
|
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: 50.32 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 21 DIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVElLGEepwalsaaarqrlRARIGLVHQA-PPLPPRQRVVS 99
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGE-------------TVKLAYVDQSrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 100 AVLAGrlgqwplwkslvslvypLD--RAGAHDALQRLDLGDKLF------QRCDQLSGGQLQRVGIARVLYQRAELILAD 171
Cdd:TIGR03719 406 EISGG-----------------LDiiKLGKREIPSRAYVGRFNFkgsdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 15598510 172 EPVSAMD 178
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-180 |
6.45e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.26 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrariglVHQappLPPR 94
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED------------------ITH---LPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRvvsavlaGRLG-----QWP--LWK-------SLVSLVYPLDRAGAHDALQRL----DLGDKLFQRCDQLSGGQLQRVG 156
Cdd:COG1137 74 KR-------ARLGigylpQEAsiFRKltvedniLAVLELRKLSKKEREERLEELleefGITHLRKSKAYSLSGGERRRVE 146
|
170 180
....*....|....*....|....
gi 15598510 157 IARVLYQRAELILADEPVSAMDPV 180
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPI 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-176 |
9.75e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgeepWALSaaarqrlrariglVHQAPplpprQRV-------VSAV 101
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELK-------------ISYKP-----QYIkpdydgtVEDL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598510 102 L---AGRLGQWPLWkslvslvypldragaHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPvSA 176
Cdd:PRK13409 421 LrsiTDDLGSSYYK---------------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-178 |
1.03e-06 |
|
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: 47.91 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DL-VHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLA--SQWRPSAGRVELLGEEpwalsaaarqrlrarigLV 85
Cdd:cd03217 5 DLhVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGED-----------------IT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 86 HqappLPPRQRVvsavlagRLGQWPLWKslvslvYPLDRAGAH--DALQRLDLGdklfqrcdqLSGGQLQRVGIARVLYQ 163
Cdd:cd03217 68 D----LPPEERA-------RLGIFLAFQ------YPPEIPGVKnaDFLRYVNEG---------FSGGEKKRNEILQLLLL 121
|
170
....*....|....*
gi 15598510 164 RAELILADEPVSAMD 178
Cdd:cd03217 122 EPDLAILDEPDSGLD 136
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-203 |
1.09e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRAR-IGLVHQAPP- 90
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIGReIAMIFQEPSs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 -LPPRQRV--------VSAVLAGRLGQWPLWKslvslvypldRAGAHDALQRLdlGDKLFQRC-----DQLSGGQLQRVG 156
Cdd:COG4170 101 cLDPSAKIgdqlieaiPSWTFKGKWWQRFKWR----------KKRAIELLHRV--GIKDHKDImnsypHELTEGECQKVM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598510 157 IARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGST-LLAS 203
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSiLLIS 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-190 |
1.31e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKT----SLLRVLASQWRPSaGRVELLGEEPWALSAAAR-QRLRARIGLVHQAP--P 90
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPEKELnKLRAEQISMIFQDPmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 91 LPPRQRVVSAV-----LAGRLGQWPLWKSLVSLvypLDRAGAHDALQRLDLGDKLFqrcdqlSGGQLQRVGIARVLYQRA 165
Cdd:PRK09473 110 LNPYMRVGEQLmevlmLHKGMSKAEAFEESVRM---LDAVKMPEARKRMKMYPHEF------SGGMRQRVMIAMALLCRP 180
|
170 180
....*....|....*....|....*
gi 15598510 166 ELILADEPVSAMDPVLAGHTLALLN 190
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLN 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-242 |
1.58e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 3 LSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrlrari 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 83 glVHQAPPLPPRQRvVSAVLAGRlgqWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKL-----FQRCDQLSGGQLQRVGI 157
Cdd:PRK10522 387 --VTAEQPEDYRKL-FSAVFTDF---HLFDQLLGPEGKPANPALVEKWLERLKMAHKLeledgRISNLKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 158 ARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAvDLALQHFPRVIGLRAGRIAfDLPAGEVDRA 237
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS-ELTGEERDAA 538
|
....*
gi 15598510 238 ALDAL 242
Cdd:PRK10522 539 SRDAV 543
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-223 |
1.62e-06 |
|
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: 47.24 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLRVLASqwRPSAGRVE---LLGEEPwalsaaARQRLRARIGLVHQAPPLPP 93
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeiLINGRP------LDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 94 RQRVV-----SAVLAGrlgqwplwkslvslvypldragahdalqrldlgdklfqrcdqLSGGQLQRVGIARVLYQRAELI 168
Cdd:cd03232 93 NLTVRealrfSALLRG------------------------------------------LSVEQRKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 169 LADEPVSAMDPVLAGHTLALLNREAAArGSTLLASLH--AVDLaLQHFPRVIGLRAG 223
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHqpSASI-FEKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-178 |
3.31e-06 |
|
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: 47.86 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVEL---LGEEPWALSaaarqrlrariglvhqapplPPRQRVVSAVLAGR 105
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEdlkISYKPQYIS--------------------PDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 106 LGQwplwKSLVSLVYpldragaHDALQRLDLgDKLFQR-CDQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:COG1245 426 NTD----DFGSSYYK-------TEIIKPLGL-EKLLDKnVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-178 |
3.87e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.16 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalsaaarqrlrarIGLVHQAPPLPPrQRVV 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------------ISFSSQFSWIMP-GTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQWPLWKSLVSLVYPLDRAGAHDALQRLDLGDKLFqrcdQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGI----TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-178 |
4.30e-06 |
|
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: 47.47 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 9 DLVHADGQRALADIRL-RLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVEllgEEP-W----------ALSAAARQ 76
Cdd:COG1245 78 DPVHRYGENGFRLYGLpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---EEPsWdevlkrfrgtELQDYFKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 RLRARIGLVHQapplpPrQRV--VSAVLAGRLGQwplwkslvsLVYPLDRAGAHDAL-QRLDLGDKLFQRCDQLSGGQLQ 153
Cdd:COG1245 155 LANGEIKVAHK-----P-QYVdlIPKVFKGTVRE---------LLEKVDERGKLDELaEKLGLENILDRDISELSGGELQ 219
|
170 180
....*....|....*....|....*
gi 15598510 154 RVGIARVLYQRAELILADEPVSAMD 178
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-227 |
5.33e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPS--AGRVELLGEEPwalsaaaRQRLRARIGLVHQAPPLPPRQRVVSAVLAGRL 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP-------TKQILKRTGFVTQDDILYPHLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 107 GQWPlwKSLVSLVYPLdraGAHDALQRLDLgdklfQRCDQ----------LSGGQLQRVGIARVLYQRAELILADEPVSA 176
Cdd:PLN03211 167 LRLP--KSLTKQEKIL---VAESVISELGL-----TKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598510 177 MDPVlAGHTLALLNREAAARGSTLLASLH-AVDLALQHFPRVIGLRAGRIAF 227
Cdd:PLN03211 237 LDAT-AAYRLVLTLGSLAQKGKTIVTSMHqPSSRVYQMFDSVLVLSEGRCLF 287
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-203 |
6.07e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLRARIGLVHQAPPLPPRQRVV 98
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLGQWPlwKSLVSLVyplDRAGAHDALQRldlgdklfqrcdQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK13543 107 CGLHGRRAKQMP--GSALAIV---GLAGYEDTLVR------------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*....
gi 15598510 179 PvlagHTLALLNREAAAR----GSTLLAS 203
Cdd:PRK13543 170 L----EGITLVNRMISAHlrggGAALVTT 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
13-230 |
6.44e-06 |
|
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: 45.87 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 13 ADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLp 92
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID---ISTIPLEDLRSSLTIIPQDPTL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 93 prqrvvsavLAGrlgqwplwkSLVSLVYPLDRAGAHDALQRLdlgdKLFQRCDQLSGGQLQRVGIARVLYQRAELILADE 172
Cdd:cd03369 94 ---------FSG---------TIRSNLDPFDEYSDEEIYGAL----RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 173 PVSAMDPvlagHTLALLNR--EAAARGSTLLASLHAVDlALQHFPRVIGLRAGRIA-FDLP 230
Cdd:cd03369 152 ATASIDY----ATDALIQKtiREEFTNSTILTIAHRLR-TIIDYDKILVMDAGEVKeYDHP 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-227 |
9.94e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVellgeepWAlsaaarqrlRARIGLVHQAPplpprqRVV 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------WA---------ERSIAYVPQQA------WIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 99 SAVLAGRLgqwplwkslvsLVY-PLDRAGAHDALQRLDLGDKLFQ-----------RCDQLSGGQLQRVGIARVLYQRAE 166
Cdd:PTZ00243 734 NATVRGNI-----------LFFdEEDAARLADAVRVSQLEADLAQlgggleteigeKGVNLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598510 167 LILADEPVSAMDpvlaGHTLALLNRE---AAARGSTLLASLHAVDLaLQHFPRVIGLRAGRIAF 227
Cdd:PTZ00243 803 VYLLDDPLSALD----AHVGERVVEEcflGALAGKTRVLATHQVHV-VPRADYVVALGDGRVEF 861
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-178 |
1.52e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGE-----EPwalsaaarq 76
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelEP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 77 rLRARIGLVHQAPPLPPRQRVvsavlAGRLGqwplwkslvslvYPLDRAG---AH------DALQRLDLGDKLFQRCDQL 147
Cdd:PRK11650 74 -ADRDIAMVFQNYALYPHMSV-----RENMA------------YGLKIRGmpkAEieervaEAARILELEPLLDRKPREL 135
|
170 180 190
....*....|....*....|....*....|.
gi 15598510 148 SGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-60 |
2.10e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 2.10e-05
10 20 30
....*....|....*....|....*....|..
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRV 60
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-173 |
2.26e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 4 SLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGrvellgeEPWAlsaaarqRLRARIG 83
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARP-------APGIKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPP----RQRVVSAV--------------------------LAGRLGQwplwkslvsLVYPLDRAGAHDALQR 133
Cdd:PRK11819 74 YLPQEPQLDPektvRENVEEGVaevkaaldrfneiyaayaepdadfdaLAAEQGE---------LQEIIDAADAWDLDSQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598510 134 LDLG-DKLfqRC-------DQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK11819 145 LEIAmDAL--RCppwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-177 |
2.55e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLpPR 94
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKS--SKEALENGISMVHQELNL-VL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAgrLGQWPLWKSLVSlvypldragaHDALQR--------LDLGDKLFQRCDQLSGGQLQRVGIARVLYQRAE 166
Cdd:PRK10982 87 QRSVMDNMW--LGRYPTKGMFVD----------QDKMYRdtkaifdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170
....*....|.
gi 15598510 167 LILADEPVSAM 177
Cdd:PRK10982 155 IVIMDEPTSSL 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-178 |
2.56e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELlgeepwalsaaarqrlRARIGL----VHQAPPLppr 94
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----------------AKGIKLgyfaQHQLEFL--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 qrvvsavlagRLGQWPLwKSLVSLVYPLDRAGAHDALQRLDL-GDKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEP 173
Cdd:PRK10636 389 ----------RADESPL-QHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
....*
gi 15598510 174 VSAMD 178
Cdd:PRK10636 458 TNHLD 462
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-178 |
3.48e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 20 ADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSAAARQRLrariGLVH-----QAPPL--- 91
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR----GLVYlpedrQSSGLyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 PPRQRVVSAVLAGRLGQWplwkslvslvypLDRAGAHDALQRL--DLGDKlFQRCDQ----LSGGQLQRVGIARVLYQRA 165
Cdd:PRK15439 356 APLAWNVCALTHNRRGFW------------IKPARENAVLERYrrALNIK-FNHAEQaartLSGGNQQKVLIAKCLEASP 422
|
170
....*....|...
gi 15598510 166 ELILADEPVSAMD 178
Cdd:PRK15439 423 QLLIVDEPTRGVD 435
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-214 |
3.59e-05 |
|
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: 44.90 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 14 DGQRALADIRLRLAAGERVALIGPSGAGKTSLL----RVLASQwrpsaGRVELLGEEpWalSAAARQRLRARIGLVhqap 89
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTE-----GEIQIDGVS-W--NSVTLQTWRKAFGVI---- 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 90 plPPRQRVVSAVLAGRL---GQWP---LWKSLvslvyplDRAGAHDALQRLDlgDKL-FQRCDQ---LSGGQLQRVGIAR 159
Cdd:TIGR01271 1298 --PQKVFIFSGTFRKNLdpyEQWSdeeIWKVA-------EEVGLKSVIEQFP--DKLdFVLVDGgyvLSNGHKQLMCLAR 1366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 160 VLYQRAELILADEPVSAMDPVlaghTLALLNR--EAAARGSTLLASLHAVD--LALQHF 214
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPV----TLQIIRKtlKQSFSNCTVILSEHRVEalLECQQF 1421
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
146-237 |
6.53e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 146 QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90
....*....|..
gi 15598510 226 AFDLPAGEVDRA 237
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-180 |
1.03e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEPWALSaaARQRLRARIGLVHQAPPLPPR 94
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 95 QRVVSAVLAGRLGQWPLWKSLVSLVYPLdraGAHdalQRLDLGDKLFQRCDQlsggqlQRVGIARVLYQRAELILADEPV 174
Cdd:PRK15439 101 LSVKENILFGLPKRQASMQKMKQLLAAL---GCQ---LDLDSSAGSLEVADR------QIVEILRGLMRDSRILILDEPT 168
|
....*.
gi 15598510 175 SAMDPV 180
Cdd:PRK15439 169 ASLTPA 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-178 |
1.07e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.17 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 2 SLSLDGVDLVHADGQRALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRAR 81
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP---LSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 82 IGLVHQAPPLPPRQRVVSAVLAGRLGQWPLWKSL--VSLVyPLDRA---GAHdalqrldlgDKLFQRCDQLSGGQLQRVG 156
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRDISEEQVWQALetVQLA-ELARSlpdGLY---------TPLGEQGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 15598510 157 IARVLYQRAELILADEPVSAMD 178
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-178 |
1.15e-04 |
|
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: 43.27 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQ----------- 87
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD---IRDVTQASLRAAIGIVPQdtvlfndtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 ----APPLPPRQRVVSAVLAGRLgqwplwkslvslvypldragaHDALQRLDLGdklFQ-----RCDQLSGGQLQRVGIA 158
Cdd:COG5265 451 niayGRPDASEEEVEAAARAAQI---------------------HDFIESLPDG---YDtrvgeRGLKLSGGEKQRVAIA 506
|
170 180
....*....|....*....|
gi 15598510 159 RVLYQRAELILADEPVSAMD 178
Cdd:COG5265 507 RTLLKNPPILIFDEATSALD 526
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-178 |
2.09e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.31 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 18 ALADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLPpRQRV 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 98 VSAVLAGRLGQWplwkSLVSLVYPLDRAGAHDALQRLDLG-DKLF-QRCDQLSGGQLQRVGIARVLYQRAELILADEPVS 175
Cdd:PRK11176 434 ANNIAYARTEQY----SREQIEEAARMAYAMDFINKMDNGlDTVIgENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
...
gi 15598510 176 AMD 178
Cdd:PRK11176 510 ALD 512
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-205 |
2.84e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 17 RALADIRLRLAAGERVALIGPSGAGKTSLLR----VLASQWRPSAGR-----VELLGEEPwalsAAARQRLRARIGLVHQ 87
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaicgVTKDNWRVTADRmrfddIDLLRLSP----RERRKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 88 APP--LPPRQRVVSAVL--------AGRLGQWPLWKslvslvypldRAGAHDALQRLDLGD-KLFQRC--DQLSGGQLQR 154
Cdd:PRK15093 97 EPQscLDPSERVGRQLMqnipgwtyKGRWWQRFGWR----------KRRAIELLHRVGIKDhKDAMRSfpYELTEGECQK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598510 155 VGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLH 205
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-231 |
2.86e-04 |
|
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: 42.24 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 6 DGVDLVhadgqraLADIRLRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLV 85
Cdd:TIGR00957 1296 EDLDLV-------LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN---IAKIGLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 86 HQAPPLPPRQRVVSAVLAGRLGQWPLWKSlvslvypLDRAGAHDALQRLDlgDKLFQRC----DQLSGGQLQRVGIARVL 161
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLDPFSQYSDEEVWWA-------LELAHLKTFVSALP--DKLDHECaeggENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598510 162 YQRAELILADEPVSAMDpvLAGHTLALLNREAAARGSTLLASLHAVDlALQHFPRVIGLRAGRIA-FDLPA 231
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVD--LETDNLIQSTIRTQFEDCTVLTIAHRLN-TIMDYTRVIVLDKGEVAeFGAPS 1504
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
146-248 |
3.46e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.15 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 146 QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRI 225
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
90 100
....*....|....*....|...
gi 15598510 226 afdlpageVDRAALDALYANEQL 248
Cdd:PRK13645 230 --------ISIGSPFEIFSNQEL 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-178 |
4.76e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 30 ERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwaLSAAARQRLRARIGLVHQAPPLpprqrvVSAVLAGRLGQW 109
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD---VAKFGLTDLRRVLSIIPQSPVL------FSGTVRFNIDPF 1333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598510 110 P------LWKSlvslvypLDRAGAHDALQRLDLG--DKLFQRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PLN03232 1334 SehndadLWEA-------LERAHIKDVIDRNPFGldAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-63 |
8.94e-04 |
|
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: 38.89 E-value: 8.94e-04
10 20 30
....*....|....*....|....*....|....*
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVELL 63
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI 36
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-178 |
1.23e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|..
gi 15598510 147 LSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-227 |
1.38e-03 |
|
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: 38.78 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 19 LADIRLRLAAGERVALIGPSGAGKTSLLRVLASQwRPSAGRVEllgeepwalsaaarqrlrariGLVH-------QAPPL 91
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVE---------------------GDIHyngipykEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 92 PPRQrvvsavlagrlgqwplwkslVSLVYPLDRagaHDAL----QRLDLGDKLfqRCDQ----LSGGQLQRVGIARVLYQ 163
Cdd:cd03233 81 YPGE--------------------IIYVSEEDV---HFPTltvrETLDFALRC--KGNEfvrgISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598510 164 RAELILADEPVSAMDPVLAGHTLALLNREAAARGSTLLASL-HAVDLALQHFPRVIGLRAGRIAF 227
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLyQASDEIYDLFDKVLVLYEGRQIY 200
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-178 |
1.46e-03 |
|
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: 38.71 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVELlgeepwalsaaarqrlrariglvhqapplpPRQRVVsavlagrlgq 108
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------DGITPV---------- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 109 wplwkslvslVYPldragahdalQRLDLgdklfqrcdqlSGGQLQRVGIARVLYQRAELILADEPVSAMD 178
Cdd:cd03222 65 ----------YKP----------QYIDL-----------SGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
146-190 |
1.70e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 1.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 15598510 146 QLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVLAGHTLALLN 190
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-178 |
2.32e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.16 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 24 LRLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEepwalsaaarqrlrARIGLVHQAPPLPPRQRVVSAVLA 103
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD--------------LIVARLQQDPPRNVEGTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 104 G----------------RLGQWP---LWKSLVSLVYPLDRAGA-------HDALQRLDL-GDKLFQrcdQLSGGQLQRVG 156
Cdd:PRK11147 90 GieeqaeylkryhdishLVETDPsekNLNELAKLQEQLDHHNLwqlenriNEVLAQLGLdPDAALS---SLSGGWLRKAA 166
|
170 180
....*....|....*....|..
gi 15598510 157 IARVLYQRAELILADEPVSAMD 178
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLD 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-49 |
2.49e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....*
gi 15598510 15 GQRALADIRLRLAAGERVALIGPSGAGKTSLLRVL 49
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL 47
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
114-253 |
2.60e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 114 SLVSLVYPLDRAGA--HDAlQRLDLGD--KLF--------QRCDQLSGGQLQRVGIARVLYQRAELILADEPVSAMDPVL 181
Cdd:PRK10762 352 SLTALRYFSRAGGSlkHAD-EQQAVSDfiRLFniktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 182 AGHTLALLNREAAARGSTLLASlhavdlalQHFPRVIG-------LRAGRIAFDLPAGEVDRAALDALYANEQLQAERA 253
Cdd:PRK10762 431 KKEIYQLINQFKAEGLSIILVS--------SEMPEVLGmsdrilvMHEGRISGEFTREQATQEKLMAAAVGKLNRVNQE 501
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-179 |
2.60e-03 |
|
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: 39.23 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 29 GERVALIGPSGAGKTSLLRVLASQWRPSAGRVELLGEEpwalsaaarqrLRARIGLVHQAPPLPPRQRVVSAVLAGRLGQ 108
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-----------ILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598510 109 WplwkslvslVYPLDRAGAHDALQRL------DLGDKLFQRC--DQLSGGQLQRVGIARVLYQRAELILADEPVSAMDP 179
Cdd:TIGR01257 2034 Y---------LYARLRGVPAEEIEKVanwsiqSLGLSLYADRlaGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
16-52 |
3.00e-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: 38.23 E-value: 3.00e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15598510 16 QRALADIRLRLAAGERVALI-GPSGAGKTSLLRVLASQ 52
Cdd:COG3267 29 REALARLEYALAQGGGFVVLtGEVGTGKTTLLRRLLER 66
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-235 |
5.22e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 37.79 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 4 SLDGVDLvhadgqralaDIRlrlaAGERVALIGPSGAGKTSLlRVLASQWRPSAGRvellgeEPWALSAAARQRLRARIG 83
Cdd:NF000106 28 AVDGVDL----------DVR----EGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR------RPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598510 84 LVHQAPPLPPRQRVVSavlaGRLGQWPLWKSLvSLVYPLDRAGAHDALQRLDLGDKLFQRCDQLSGGQLQRVGIARVLYQ 163
Cdd:NF000106 87 IG*HRPVR*GRRESFS----GRENLYMIGR*L-DLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598510 164 RAELILADEPVSAMDPVLAGHTLALLnREAAARGSTLLASLHAVDLALQHFPRVIGLRAGRIAFDlpaGEVD 235
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD---GKVD 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-65 |
5.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 5.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 15598510 25 RLAAGERVALIGPSGAGKTSLLRVLASQWRPSAGRVElLGE 65
Cdd:PRK11819 346 SLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGE 385
|
|
| |
