|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-249 |
3.33e-138 |
|
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: 388.96 E-value: 3.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG--SGSALRQHRRR 87
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALANVLTGRLAFHNTLRSLF-PLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLER 246
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
...
gi 1393936756 247 IYA 249
Cdd:TIGR02315 241 IYG 243
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-254 |
6.79e-135 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 380.94 E-value: 6.79e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG--SGSALRQHRR 86
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLIERQSALANVLTGRLAFHNTLRSLFPL-PRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARA 165
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 166 LAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLE 245
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLR 240
|
....*....
gi 1393936756 246 RIYAGRSTT 254
Cdd:COG3638 241 EIYGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-248 |
1.73e-130 |
|
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: 369.59 E-value: 1.73e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGS--GSALRQHRRRT 88
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANVLTGRLAFHNTLRSLF-PLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERI 247
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 1393936756 248 Y 248
Cdd:cd03256 241 Y 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-248 |
2.25e-70 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 217.22 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSgsalRQHRR 86
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDLASLSR----RELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLIERQSALANVLTGRLAFHNTLRslfPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGRYPHLGLFG---RPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLE 245
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvLTPELLE 232
|
...
gi 1393936756 246 RIY 248
Cdd:COG1120 233 EVY 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-231 |
9.57e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.51 E-value: 9.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSAL 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgQDISSL-SEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRT-AMIFQHHQLIERQSALANVLTGrLAFHNTLRslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRV 160
Cdd:COG1136 81 ARLRRRHiGFVFQFFNLLPELTALENVALP-LLLAGVSR------KERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIV 231
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-247 |
1.08e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 204.84 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG-SGSALRQHRRRT 88
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANVLtgrLAfhntLRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVT---LA----PIKVKKMSKAEaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL-TDAQLER 246
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFfENPQHER 231
|
.
gi 1393936756 247 I 247
Cdd:COG1126 232 T 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-230 |
8.50e-64 |
|
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: 199.25 E-value: 8.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQH 84
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgTDISKL-SEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRT-AMIFQHHQLIERQSALANVLtgrLAFHntlrsLFPLPRADQ-EIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:cd03255 80 RRRHiGFVFQSFNLLPDLTALENVE---LPLL-----LAGVPKKERrERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQI 230
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-231 |
3.77e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.46 E-value: 3.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQH 84
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgVDLTAL-SERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLIERQSALANVLtgrlafhntlrslFPL-----PRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQ 158
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVA-------------LPLeiagvPKAEiRKRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-238 |
3.01e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 195.27 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHRR 86
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngQDLSRL-KRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLIERQSALANVLtgrlafhntlrslFPL------PRADQEIALSCLARVGLADKALSRVDKLSGGQQQRV 160
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVA-------------LPLrvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE 238
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-239 |
5.08e-60 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 189.85 E-value: 5.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAM 90
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQH--HQLIERqSALANVltgrlAFhnTLRSLfPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:COG1122 80 VFQNpdDQLFAP-TVEEDV-----AF--GPENL-GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-230 |
1.49e-59 |
|
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: 188.12 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGEL-GSGSALRQHRRRTAMIFQHHQLIER 100
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtDDKKNINELRQKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSALANVLTGrlafhntLRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:cd03262 91 LTVLENITLA-------PIKVKGMSKAEaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-251 |
6.48e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.60 E-value: 6.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 1 MMPHPiqdaVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSelgelgSGSA 80
Cdd:COG1121 1 MMMMP----AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRL------FGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHRRRTAMIFQHHQlIERQ---SALANVLTGRLAFHNTLRslfPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQ 157
Cdd:COG1121 70 PRRARRRIGYVPQRAE-VDWDfpiTVRDVVLMGRYGRRGLFR---RPSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPS 237
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEE 224
|
250
....*....|....
gi 1393936756 238 ELTDAQLERIYAGR 251
Cdd:COG1121 225 VLTPENLSRAYGGP 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-231 |
2.94e-58 |
|
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: 185.48 E-value: 2.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQ 83
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgTDLTLL-SGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLIERQSALANVLtgrlafhntlrslFPL-----PRADQ-EIALSCLARVGLADKALSRVDKLSGGQQ 157
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVA-------------LPLeiagvPKAEIeERVLELLELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-239 |
3.16e-57 |
|
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: 190.88 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYP----GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSA 80
Cdd:COG1123 258 EPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgKDLTKL-SRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHRRRTAMIFQH--HQLIERQSALANVLTGrlafhntLRSLFPLPRAD-QEIALSCLARVGLADKALSR-VDKLSGGQ 156
Cdd:COG1123 337 LRELRRRVQMVFQDpySSLNPRMTVGDIIAEP-------LRLHGLLSRAErRERVAELLERVGLPPDLADRyPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAP 236
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
...
gi 1393936756 237 SEL 239
Cdd:COG1123 490 EEV 492
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-248 |
1.59e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 181.42 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRTAM 90
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR--VLGEDVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERqsalanvLTGR--LAFHntlRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:COG1131 78 VPQEPALYPD-------LTVRenLRFF---ARLYGLPRKEaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERI 247
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDV 226
|
.
gi 1393936756 248 Y 248
Cdd:COG1131 227 F 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-247 |
3.37e-56 |
|
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: 180.56 E-value: 3.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQ 83
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgQDITGL-SEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQhhqlierQSALANVLTgrlAFHNT---LRSLFPLPRAD-QEIALSCLARVGLADKAlsrvDK----LSGG 155
Cdd:COG1127 80 LRRRIGMLFQ-------GGALFDSLT---VFENVafpLREHTDLSEAEiRELVLEKLELVGLPGAA----DKmpseLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 156 QQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAA 235
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
250
....*....|..
gi 1393936756 236 PSELTDAQLERI 247
Cdd:COG1127 226 PEELLASDDPWV 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-250 |
3.74e-55 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 178.67 E-value: 3.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVT--PTGGSVTSELG-----ELGSGSALR 82
Cdd:PRK09984 4 IIRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGSHIELLGrtvqrEGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHRRRTAMIFQHHQLIERQSALANVLTGRLAFHNTLRSLFP-LPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSwFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
....*....
gi 1393936756 242 AQLERIYAG 250
Cdd:PRK09984 243 ERFDHLYRS 251
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-227 |
1.11e-52 |
|
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: 169.68 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSA-LRQHRRRTA 89
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLIERQSALANVLTGrlafhntlrslfplpradqeialsclarvgladkalsrvdkLSGGQQQRVGIARALAQQ 169
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-229 |
1.31e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 168.03 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAM 90
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQH--HQLIerqsalANVLTGRLAFHntLRSLfPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:cd03225 80 VFQNpdDQFF------GPTVEEEVAFG--LENL-GLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQ 229
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-231 |
2.36e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.14 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHR 85
Cdd:PRK11153 3 ELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgQDLTAL-SEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHqlierqsalaNVLTGRLAFHNTLrslFPL-----PRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQR 159
Cdd:PRK11153 82 RQIGMIFQHF----------NLLSSRTVFDNVA---LPLelagtPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-247 |
2.66e-51 |
|
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: 167.68 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHRRRTAMIFQhhqli 98
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgEDISGL-SEAELYRLRRRMGMLFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 erQSALANVLTgrlAFHNT---LRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIIL 174
Cdd:cd03261 85 --SGALFDSLT---VFENVafpLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 175 ADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERI 247
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLV 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
7-223 |
3.48e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 165.65 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYP---GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQ 83
Cdd:COG1116 4 AAPALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------GKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLIERQSALANVLTGrlafhntLRsLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALG-------LE-LRGVPKAErRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVV 223
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVV 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-231 |
3.58e-50 |
|
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: 164.60 E-value: 3.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQ--H 84
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQhhqliERQSALANVLTGRLAFHNTLRSLFPLPRADQ--EIALSCLARVGLADKALSR-VDKLSGGQQQRVG 161
Cdd:cd03257 81 RKEIQMVFQ-----DPMSSLNPRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-231 |
3.94e-50 |
|
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: 162.99 E-value: 3.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgeLGsGSALRQHRRRtami 91
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----LD-GKDLASLSPK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 fqhhqlierqsALANvltgRLAFhntlrslfpLPRAdqeialscLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPA 171
Cdd:cd03214 70 -----------ELAR----KIAY---------VPQA--------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 172 IILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-223 |
1.68e-49 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 162.70 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSelgelgSGSALRQHRRRTAMI 91
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV------FGKPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQHHQlIERQ---SALANVLTGRLAFhntLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ 168
Cdd:cd03235 74 PQRRS-IDRDfpiSVRDVVLMGLYGH---KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVV 223
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-231 |
9.64e-49 |
|
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: 160.38 E-value: 9.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGsaLRQHRRRTAM 90
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-GRDVTG--VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVltgrlAFHNTLRSLfplPRADQEI-ALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:cd03259 77 VFQDYALFPHLTVAENI-----AFGLKLRGV---PKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-269 |
3.09e-48 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 160.67 E-value: 3.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRtAM 90
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR-AV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ-- 168
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSS-------AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 169 -----QPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDA 242
Cdd:COG4559 153 epvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEvLTDE 231
|
250 260
....*....|....*....|....*..
gi 1393936756 243 QLERIYAGRSTTQPANTPAEPPVMLEP 269
Cdd:COG4559 232 LLERVYGADLRVLAHPEGGCPQVLPRA 258
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-238 |
3.85e-47 |
|
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: 157.21 E-value: 3.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGsaLRQHRRRTAM 90
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITG--LPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 I---FQHHQLIERQSALANVLTGRLAFHNTLRSLFPLPRADQEI---ALSCLARVGLADKALSRVDKLSGGQQQRVGIAR 164
Cdd:cd03219 77 IgrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE 238
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-230 |
4.43e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 4.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAM 90
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-GKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQhhqlierQSALanvltgrlaFHNTLRSLFPLP------RADQEIALSCLARVGLADKALSR-VDKLSGGQQQRVGIA 163
Cdd:COG4619 79 VPQ-------EPAL---------WGGTVRDNLPFPfqlrerKFDRERALELLERLGLPPDILDKpVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-223 |
1.74e-46 |
|
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: 154.94 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQHRRR 87
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD------GEPVTGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALANVLTGrlafhntLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG-------LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVV 223
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-238 |
2.05e-46 |
|
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: 155.97 E-value: 2.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRR- 86
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPPHRIa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 -----RTamiFQHHQLIERQSALANVLTGRLAFHNT--LRSLFPLP------RADQEIALSCLARVGLADKALSRVDKLS 153
Cdd:COG0411 78 rlgiaRT---FQNPRLFPELTVLENVLVAAHARLGRglLAALLRLPrarreeREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
....*
gi 1393936756 234 AAPSE 238
Cdd:COG0411 235 GTPAE 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-272 |
2.74e-46 |
|
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: 161.99 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVtPTGGSVTSEL---GELGSGSALRQ 83
Cdd:COG1123 2 TPLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGEVlldGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQhhqliERQSALANVLTGR-LAFhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:COG1123 81 RGRRIGMVFQ-----DPMTQLNPVTVGDqIAE--ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDA 242
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260 270
....*....|....*....|....*....|
gi 1393936756 243 QlERIYAGRSTTQPANTPAEPPVMLEPSLE 272
Cdd:COG1123 234 P-QALAAVPRLGAARGRAAPAAAAAEPLLE 262
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-248 |
2.77e-46 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 155.70 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRt 88
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ 168
Cdd:PRK13548 79 AVLPQHSSLSFPFTVEEVVAMGRAPHGLS-------RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 169 ------QPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTD 241
Cdd:PRK13548 152 lwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEvLTP 231
|
....*..
gi 1393936756 242 AQLERIY 248
Cdd:PRK13548 232 ETLRRVY 238
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-239 |
3.67e-46 |
|
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: 155.88 E-value: 3.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG--SGSALRQHRRRT-AMIFQHHQLI 98
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRKKiSMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 ERQSALANVltgrlAFHNTLRSLFPLPRadQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:cd03294 115 PHRTVLENV-----AFGLEVQGVPRAER--EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-239 |
5.01e-46 |
|
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: 154.58 E-value: 5.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRR 87
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-GRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQH-------HQLIERqsalanVLTGRLAFHNtlrslfpLPRADQEIAlSCLARVGLADKALSR-VDKLSGGQQQR 159
Cdd:COG1124 81 VQMVFQDpyaslhpRHTVDR------ILAEPLRIHG-------LPDREERIA-ELLEQVGLPPSFLDRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-243 |
2.27e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.60 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpgGVTALR-DTSIAfrRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGElgSGSALRQHRRRTA 89
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRfDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-GQ--DLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLIERQSALANVLtgrLAFHNTLRslfpLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIG---LGLRPGLK----LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQ 243
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-241 |
5.36e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.78 E-value: 5.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGS-VTSELGELGSGSALRQHRRRTAMIFQHHQLIER 100
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSALANVLTGRLAFHNTLRSlfplprADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKE------EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 181 SLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-223 |
1.57e-44 |
|
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: 152.90 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYP---GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTP---TGGSVT---SELGELgSGSA 80
Cdd:COG0444 1 LLEVRNLKVYFPtrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgEDLLKL-SEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHR-RRTAMIFQhhqliERQSALANVLTGRLAFHNTLRSLFPLPRAD-QEIALSCLARVGLADkALSRVDK----LSG 154
Cdd:COG0444 80 LRKIRgREIQMIFQ-----DPMTSLNPVMTVGDQIAEPLRIHGGLSKAEaRERAIELLERVGLPD-PERRLDRypheLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 155 GQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVV 223
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-227 |
1.59e-44 |
|
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: 149.71 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGS---GSALRQHRR 86
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA-GEDVNrlrGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLIERQSALANVltgrlAFhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENV-----AL--PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-239 |
1.72e-44 |
|
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: 150.02 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLV-----TPTGGSVTSELGELGSGSALR-QH 84
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLIeRQSALANVLTGrLAFHNTLRSlfplpRADQEIALSCLARVGLADKALSRVD--KLSGGQQQRVGI 162
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYG-LRLHGIKLK-----EELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdgITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-239 |
3.11e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.94 E-value: 3.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgeLGsG---SALRQ 83
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-----LD-GrdvTGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLIERQSALANVltgrlAFHntLRSLfPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:COG3842 75 EKRNVGMVFQDYALFPHLTVAENV-----AFG--LRMR-GVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-239 |
6.81e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 147.60 E-value: 6.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG----VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGEL----GSGSALR 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVT--IDGRditaKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHRRRTAMIFQH--HQLIErqsalANVLTgRLAF--HNtlrslFPLPRAD-QEIALSCLARVGLADKALSRVD-KLSGGQ 156
Cdd:TIGR04521 79 DLRKKVGLVFQFpeHQLFE-----ETVYK-DIAFgpKN-----LGLSEEEaEERVKEALELVGLDEEYLERSPfELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAP 236
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
...
gi 1393936756 237 SEL 239
Cdd:TIGR04521 228 REV 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-230 |
1.01e-42 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 145.24 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 19 VYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHRRRTAMIFQHH 95
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngQDVSDL-RGRAIPYLRRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 96 QLIERQSALANVltgrlAFhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:cd03292 88 RLLPDRNVYENV-----AF--ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-238 |
1.02e-42 |
|
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: 145.65 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 2 MPHPiQDAVLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGEL 75
Cdd:COG4181 1 MSSS-SAPIIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 76 GSGSALRQHRRRTAMIFQHHQLIERQSALANVLTgrlafhntlrslfPLPRA----DQEIALSCLARVGLADKALSRVDK 151
Cdd:COG4181 80 DEDARARLRARHVGFVFQSFQLLPTLTALENVML-------------PLELAgrrdARARARALLERVGLGHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIV 231
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 1393936756 232 FDAAPSE 238
Cdd:COG4181 226 EDTAATA 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-248 |
5.77e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.23 E-value: 5.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGElGSGSALRQHRRRTA 89
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GE-DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLIERQSALANvltgrLAFHNTLRSLFplPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:COG4555 78 VLPDERGLYDRLTVREN-----IRYFAELYGLF--DEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDiCKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD----AQLE 245
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeigeENLE 229
|
...
gi 1393936756 246 RIY 248
Cdd:COG4555 230 DAF 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-251 |
4.64e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 139.61 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRqhr 85
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 rrtAMIFQHHQLIERQSALANVltgrlAFHNTLRSLfplPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIAR 164
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNV-----AFGLRLRGV---PKAErRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITV--------------------------IVSLHQLEYARRF 218
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVflithsveealflatrlvvmspgpgrIVERLELDFSRRF 227
|
250 260 270
....*....|....*....|....*....|...
gi 1393936756 219 ADrvvGLADSQIVFDAAPSELTDAQLERIYAGR 251
Cdd:COG4525 228 LA---GEDARAIKSDPAFIALREELLDIIFAQE 257
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-239 |
6.28e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 139.49 E-value: 6.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTA 89
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQH--HQLIerqsalANVLTGRLAF--HNtlrslFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIAR 164
Cdd:TIGR04520 81 MVFQNpdNQFV------GATVEDDVAFglEN-----LGVPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-231 |
1.05e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 138.22 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV---------TSELGElgsgSALRQHRRRTAMIF 92
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdfSQKPSE----KAIRLLRQKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QHHQLIERQSALANVLTGrlafhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAI 172
Cdd:COG4161 89 QQYNLWPHLTVMENLIEA------PCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-248 |
5.41e-39 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 136.68 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAlRQHRRRTAM 90
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHH---------QLIERQSALANVLTGRLAfhntlrslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:PRK11231 81 LPQHHltpegitvrELVAYGRSPWLSLWGRLS------------AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LT 240
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvMT 227
|
....*...
gi 1393936756 241 DAQLERIY 248
Cdd:PRK11231 228 PGLLRTVF 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-239 |
7.25e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.47 E-value: 7.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 4 HPIQDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT----------SELG 73
Cdd:COG4598 2 TDTAPPALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRvggeeirlkpDRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 74 ELGSGSA--LRQHRRRTAMIFQHHQLIERQSALANVLTGRLafhNTLRslfpLPRAD-QEIALSCLARVGLADKALSRVD 150
Cdd:COG4598 81 ELVPADRrqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPV---HVLG----RPKAEaIERAEALLAKVGLADKRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
....*....
gi 1393936756 231 VFDAAPSEL 239
Cdd:COG4598 233 EEQGPPAEV 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-239 |
7.43e-39 |
|
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: 135.89 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAM 90
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQH-----HQLIERQSALANVLTGrlafhntlrslFPLPRADQEiALSCLARVGLADKALSR--VDKLSGGQQQRVGIA 163
Cdd:cd03295 80 VIQQiglfpHMTVEENIALVPKLLK-----------WPKEKIRER-ADELLALVGLDPAEFADryPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-229 |
1.11e-38 |
|
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: 132.75 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMI 91
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQhhqlierqsalanvltgrlafhntlrslfplpradqeialsclarvgladkalsrvdkLSGGQQQRVGIARALAQQPA 171
Cdd:cd00267 79 PQ----------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 172 IILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQ 229
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-248 |
1.11e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.60 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSgSALRQHRRRTAmi 91
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELAKRLA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 fqhhqlIERQSalaNVLTGRLafhnTLRSL-----FP-----LPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:COG4604 79 ------ILRQE---NHINSRL----TVRELvafgrFPyskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LT 240
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEiIT 225
|
....*...
gi 1393936756 241 DAQLERIY 248
Cdd:COG4604 226 PEVLSDIY 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-230 |
1.28e-38 |
|
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: 133.29 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLGElGSGSALRQHRRRTAM 90
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-LGK-DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVltgrlafhntlrslfplpradqeialsclarvgladkalsrvdKLSGGQQQRVGIARALAQQP 170
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-246 |
1.99e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.26 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAL-------RQHRRRTAMIFQHH 95
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkgliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 96 QLIERQSALANVLTGRLAFHNTLRSlfplprADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:PRK11264 95 NLFPHRTVLENIIEGPVIVKGEPKE------EATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEDGITVIVSlHQLEYARRFADRVVGLADSQIVFDAAPSEL-TDAQLER 246
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT-HEMSFARDVADRAIFMDQGRIVEQGPAKALfADPQQPR 239
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-184 |
3.68e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 137.93 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHRRRT-AMIFQHHQL 97
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLidgEDITKL-SKKELRELRRKKmSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IERQSALANVltgrlAFhntlrslfPL-----PRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPA 171
Cdd:COG4175 117 LPHRTVLENV-----AF--------GLeiqgvPKAErRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPD 183
|
170
....*....|...
gi 1393936756 172 IILADEPVASLDP 184
Cdd:COG4175 184 ILLMDEAFSALDP 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-231 |
6.96e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 6.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTS-----ELGELGSGSALRQHR 85
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfDFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHQLIERQSALANVLTGrlafhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARA 165
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEA------PCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 166 LAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-248 |
7.81e-38 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 133.67 E-value: 7.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRR 87
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 -----TAMifqHHQLIERQSALANVLTGrlaFHNTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:COG1119 80 iglvsPAL---QLRFPRDETVLDVVLSG---FFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVI-VSlHQLEYARRFADRVVGLADSQIVFDAAPSE-LT 240
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEvLT 232
|
....*...
gi 1393936756 241 DAQLERIY 248
Cdd:COG1119 233 SENLSEAF 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-265 |
5.86e-37 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 131.65 E-value: 5.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRT 88
Cdd:PRK10253 6 ARLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLD-GEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANVLTGRLAFhntlRSLFPLPRADQEIALSCLAR-VGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARGRYPH----QPLFTRWRKEDEEAVTKAMQaTGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQL-ER 246
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELiER 239
|
250 260
....*....|....*....|..
gi 1393936756 247 IYAGRSTT--QP-ANTPAEPPV 265
Cdd:PRK10253 240 IYGLRCMIidDPvAGTPLVVPL 261
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-239 |
7.96e-37 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 130.88 E-value: 7.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLV-----TPTGGSVTSElGE--LGSGSALR 82
Cdd:TIGR00972 1 AIEIENLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlvpgVRIEGKVLFD-GQdiYDKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHRRRTAMIFQHHQLIERqSALANVLTGrlafhntLRSLFPLPRAD-QEIALSCLARVGLADKALSRVDK----LSGGQQ 157
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFPM-SIYDNIAYG-------PRLHGIKDKKElDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSlHQLEYARRFADRVVGLADSQIVFDAAPS 237
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVT-HNMQQAARISDRTAFFYDGELVEYGPTE 228
|
..
gi 1393936756 238 EL 239
Cdd:TIGR00972 229 QI 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-243 |
2.07e-36 |
|
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: 136.04 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgsgsALRQ 83
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingVDLSDL----DPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLAD--KAL-----SRVD---- 150
Cdd:COG4988 409 WRRQIAWVPQNPYL----------------FAGTIREnlRLGRPDASDEELEAALEAAGLDEfvAALpdgldTPLGeggr 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEyARRFADRVVGLADSQI 230
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLA-LLAQADRILVLDDGRI 549
|
250
....*....|...
gi 1393936756 231 VFDAAPSELTDAQ 243
Cdd:COG4988 550 VEQGTHEELLAKN 562
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-247 |
6.45e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 130.62 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYP----------GGVTALRDTSIAFRRGEfTV-LLGLSGAGKSTLLRSLNRLVTPTGGSVT---SEL 72
Cdd:COG4608 4 AEPLLEVRDLKKHFPvrgglfgrtvGVVKAVDGVSFDIRRGE-TLgLVGESGCGKSTLGRLLLRLEEPTSGEILfdgQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 73 GELgSGSALRQHRRRTAMIFQHHQ--LIERQSaLANVLTGRLAFHNTLrslfplPRAD-QEIALSCLARVGLADKALSRV 149
Cdd:COG4608 83 TGL-SGRELRPLRRRMQMVFQDPYasLNPRMT-VGDIIAEPLRIHGLA------SKAErRERVAELLELVGLRPEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 150 DK-LSGGQQQRVGIARALAQQPAIILADEPVASLDpaTSVR--VLGLLRDICKEDGITVIVSLHQLEYARRFADRV---- 222
Cdd:COG4608 155 PHeFSGGQRQRIGIARALALNPKLIVCDEPVSALD--VSIQaqVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVavmy 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1393936756 223 ----VGLADSQIVFD------------AAPSELTDAQLERI 247
Cdd:COG4608 233 lgkiVEIAPRDELYArplhpytqallsAVPVPDPERRRERI 273
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-242 |
6.63e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.04 E-value: 6.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGELGSGSALRQHRRRTAM 90
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI--VLNGRDLFTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVltgrlAFHntLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQP 170
Cdd:COG1118 80 VFQHYALFPHMTVAENI-----AFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 171 AIILADEPVASLDpaTSVRVL--GLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDA 242
Cdd:COG1118 153 EVLLLDEPFGALD--AKVRKElrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-222 |
6.95e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.62 E-value: 6.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRL--VTPtGGSVTSEL---GE--L 75
Cdd:COG1117 4 PASTLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIP-GARVEGEIlldGEdiY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 76 GSGSALRQHRRRTAMIFQH-----HQLIErqsalaNVLTG-RLafhNTLRSlfplpRAD-QEIALSCLARVGL----ADK 144
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKpnpfpKSIYD------NVAYGlRL---HGIKS-----KSElDEIVEESLRKAALwdevKDR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 145 ----ALSrvdkLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGItVIVSlHQLEYARRFAD 220
Cdd:COG1117 148 lkksALG----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI-VIVT-HNMQQAARVSD 221
|
..
gi 1393936756 221 RV 222
Cdd:COG1117 222 YT 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-233 |
8.29e-36 |
|
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: 127.22 E-value: 8.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 29 DTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGsALRQHRRRTAMIFQHHQLIERQSALANVL 108
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL--INGVDVT-AAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TGRLAfhnTLRslfpLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSV 188
Cdd:cd03298 93 LGLSP---GLK----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1393936756 189 RVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-225 |
1.25e-35 |
|
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: 126.58 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV---TSELGELGSGSALRQHRRRTAMIFQHHQLI 98
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVylnGQETPPLNSKKASKFRREKLGYLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 ERQSALANVLTGrLAFHNtlrslfpLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADE 177
Cdd:TIGR03608 89 ENETVEENLDLG-LKYKK-------LSKKEkREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1393936756 178 PVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRfADRVVGL 225
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
22-239 |
1.48e-35 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 130.36 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGEL---GSGSALRQHRRRT-AMIFQHHQL 97
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFID-GENimkQSPVELREVRRKKiGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IERQSALANVLTGRlafhntlrSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILAD 176
Cdd:TIGR01186 83 FPHMTILQNTSLGP--------ELLGWPEQErKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 177 EPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-239 |
2.76e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgELGsG---SALRQHR 85
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-----LIG-GrdvTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHQLIERQSALANVLtgrlafhntlrslFPL-----PRAD-----QEIAlsclARVGLADKALSRVDKLSGG 155
Cdd:COG3839 75 RNIAMVFQSYALYPHMTVYENIA-------------FPLklrkvPKAEidrrvREAA----ELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 156 QQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLH-QLEyARRFADRVVGLADSQIVFDA 234
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVE-AMTLADRIAVMNDGRIQQVG 216
|
....*
gi 1393936756 235 APSEL 239
Cdd:COG3839 217 TPEEL 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-243 |
8.66e-35 |
|
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: 131.43 E-value: 8.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALR 82
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggVDLRDL-DEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHrrrTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLAD--KAL-----SRVD--- 150
Cdd:COG4987 409 RR---IAVVPQRPHL----------------FDTTLREnlRLARPDATDEELWAALERVGLGDwlAALpdgldTWLGegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 -KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDgiTVIVSLHQLEYARRFaDRVVGLADSQ 229
Cdd:COG4987 470 rRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGR 546
|
250
....*....|....
gi 1393936756 230 IVFDAAPSELTDAQ 243
Cdd:COG4987 547 IVEQGTHEELLAQN 560
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-241 |
1.62e-34 |
|
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: 124.08 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAM 90
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVLTGRLAFHNTLR--------SLFPLpradqeialsclarvgLADKALSRVDKLSGGQQQRVGI 162
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRkarlervyELFPR----------------LKERRKQLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
12-239 |
1.76e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 126.36 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMI 91
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILID-GEDIRDLDPVELRRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQH-----HQLIERQSALANVLTGRlafhntlrslfplPRAD-QEIALSCLARVGL-ADKALSRV-DKLSGGQQQRVGIA 163
Cdd:COG1125 82 IQQiglfpHMTVAENIATVPRLLGW-------------DKERiRARVDELLELVGLdPEEYRDRYpHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-268 |
2.21e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.37 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPGgVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRR 87
Cdd:COG1129 2 EPLLEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALANVLTGRLAfhntLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREP----RRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVI-VSlHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLER 246
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIyIS-HRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
250 260
....*....|....*....|....
gi 1393936756 247 IYAGRSTTQ--PANTPAEPPVMLE 268
Cdd:COG1129 235 LMVGRELEDlfPKRAAAPGEVVLE 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-257 |
3.49e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 127.65 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAlRQHRRRTAM 90
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-RAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVLTGRlafHNTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQP 170
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGR---TPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLERIYA 249
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADvLTADTLRAAFD 237
|
250
....*....|
gi 1393936756 250 GRS--TTQPA 257
Cdd:PRK09536 238 ARTavGTDPA 247
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-227 |
4.17e-34 |
|
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: 122.59 E-value: 4.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRT 88
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL--WNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANvltgrLAFHNTLRSLfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ 168
Cdd:COG4133 78 AYLGHADGLKPELTVREN-----LRFWAALYGL----RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYArrfADRVVGLAD 227
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA---AARVLDLGD 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-239 |
4.77e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 124.43 E-value: 4.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 25 TALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAMIFQH--HQLIerqs 102
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdNQIV---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 alANVLTGRLAFHNtlRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASL 182
Cdd:PRK13633 100 --ATIVEEDVAFGP--ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 183 DPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-241 |
9.47e-34 |
|
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: 122.35 E-value: 9.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRRRTAM 90
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVltgrlAFHNTLRSLfplPRADQEIALS-CLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:cd03300 77 VFQNYALFPHLTVFENI-----AFGLRLKKL---PKAEIKERVAeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-180 |
1.02e-33 |
|
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: 119.67 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSaLRQHRRRTAMIFQHHQLIERQSALAN 106
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 107 VLTGRLAFHNTLRSlfplPRADQEIALSCLARVGLADKALSRVDK-LSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:pfam00005 80 LRLGLLLKGLSKRE----KDARAEEALEKLGLGDLADRPVGERPGtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-239 |
5.24e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.05 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGE--LGSGSA---LRQHRRRTAMIFQ--HHQLI 98
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT--IGErvITAGKKnkkLKPLRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 ErQSALANVLTGRLAFHntlrslfpLPRAD-QEIALSCLARVGLADKALSRVD-KLSGGQQQRVGIARALAQQPAIILAD 176
Cdd:PRK13634 100 E-ETVEKDICFGPMNFG--------VSEEDaKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 177 EPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-230 |
1.10e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.54 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSGSALRQ 83
Cdd:PRK11629 5 LLQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLIERQSALANV----LTGRLAfhntlrslfplPRADQEIALSCLARVGLADKALSRVDKLSGGQQQR 159
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVamplLIGKKK-----------PAEINSRALEMLAAVGLEHRANHRPSELSGGERQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFaDRVVGLADSQI 230
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-234 |
1.60e-32 |
|
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: 118.55 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 37 GEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE---LGELGSGSALRQHRRRTAMIFQHHQLIERQSALANVLTGrla 113
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 114 fhntLRSLFPLPRADQEIALscLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGL 193
Cdd:cd03297 100 ----LKRKRNREDRISVDEL--LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1393936756 194 LRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDA 234
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-247 |
2.37e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.12 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgSGSALRQHR 85
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHqliERQSALANVlTGRLAF----HNTLRSLFpLPRADQeialsCLARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:PRK13635 81 RQVGMVFQNP---DNQFVGATV-QDDVAFglenIGVPREEM-VERVDQ-----ALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL-- 239
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfk 229
|
....*...
gi 1393936756 240 TDAQLERI 247
Cdd:PRK13635 230 SGHMLQEI 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-223 |
2.66e-32 |
|
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: 116.71 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLGELGSGSALRQHRRRTA 89
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLierqsalanvltgrlaFHNTLRSlfplpradqEIalsclarvgladkalsrvdkLSGGQQQRVGIARALAQQ 169
Cdd:cd03228 80 YVPQDPFL----------------FSGTIRE---------NI--------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVV 223
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRII 165
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-243 |
3.26e-32 |
|
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: 124.95 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGsgsaLRQHRR 86
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgIDLRQID----PASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLADKALSRVDK-----------LS 153
Cdd:COG2274 550 QIGVVLQDVFL----------------FSGTIREniTLGDPDATDEEIIEAARLAGLHDFIEALPMGydtvvgeggsnLS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIVFD 233
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVED 690
|
250
....*....|
gi 1393936756 234 AAPSELTDAQ 243
Cdd:COG2274 691 GTHEELLARK 700
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-233 |
6.44e-32 |
|
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: 116.91 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVtALRDTSIAFRRGeFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgELGSGSALRQH---RRR 87
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-----RIDGQDVLKQPqklRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALAnvltgRLAFHNTLRSLfPLPRADQEIALScLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:cd03264 74 IGYLPQEFGVYPNFTVRE-----FLDYIAWLKGI-PSKEVKARVDEV-LELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEDgiTVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-231 |
9.25e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.59 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 12 RVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelGSGSALRQHRRRTAMI 91
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN----GKPIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQH--HQLIErQSALANVLTGRlafhntlrslfPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:cd03226 77 MQDvdYQLFT-DSVREELLLGL-----------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-225 |
1.02e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.79 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgelgsgsalRQHRRRTAMIFQHHQLIERQ 101
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALAN--VLTGRLAFHNTLRslfPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:NF040873 71 PLTVRdlVAMGRWARRGLWR---RLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1393936756 180 ASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRfADRVVGL 225
Cdd:NF040873 148 TGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-239 |
1.08e-31 |
|
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: 116.70 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGG-------SVTSELGELgsgsalrqhR 85
Cdd:cd03265 3 VENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghDVVREPREV---------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQhhqlierQSALANVLTGR--LAFHNTLRSLfPLPRADQEIAlSCLARVGLADKALSRVDKLSGGQQQRVGIA 163
Cdd:cd03265 73 RRIGIVFQ-------DLSVDDELTGWenLYIHARLYGV-PGAERRERID-ELLDFVGLLEAADRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-215 |
1.29e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 115.60 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG-SGSALRQHRRRTAMIFQHHQli 98
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLLERRQRVGLVFQDPD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 erQSALANVLTGRLAFhntlrSLFPLPRADQEI------ALSCLARVGLADKALSrvdKLSGGQQQRVGIARALAQQPAI 172
Cdd:TIGR01166 79 --DQLFAADVDQDVAF-----GPLNLGLSEAEVerrvreALTAVGASGLRERPTH---CLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYA 215
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-231 |
1.32e-31 |
|
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: 114.83 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAM 90
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQhhqlierqsalanvltgrlafhntlrslfplpradqeialsclarvgladkalsrvdkLSGGQQQRVGIARALAQQP 170
Cdd:cd03216 80 VYQ----------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDIcKEDGITVI-VSlHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIfIS-HRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
27-239 |
1.34e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.38 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGS----------VTSELGEL--GSGSALRQHRRRTAMIFQH 94
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSivvngqtinlVRDKDGQLkvADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 95 HQLIERQSALANVLTGRLafhntlrSLFPLPRAD-QEIALSCLARVGLADKALSRVD-KLSGGQQQRVGIARALAQQPAI 172
Cdd:PRK10619 101 FNLWSHMTVLENVMEAPI-------QVLGLSKQEaRERAVKYLAKVGIDERAQGKYPvHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-248 |
2.45e-31 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 117.20 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 1 MMPHPIQ-DAVLRVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGS 79
Cdd:PRK10575 1 MQEYTNHsDTTFALRNVSFRVPGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 AlRQHRRRTAMIFQHHQLIERQSALANVLTGRLAFHNTLRSLfplPRADQEIALSCLARVGLADKALSRVDKLSGGQQQR 159
Cdd:PRK10575 80 S-KAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRF---GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
250
....*....|
gi 1393936756 240 TDAQ-LERIY 248
Cdd:PRK10575 236 MRGEtLEQIY 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
2.82e-31 |
|
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: 121.33 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 1 MMPHPIqdavLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKS----TLLRSLNRLVTPTGGSVT---S 70
Cdd:COG4172 1 MMSMPL----LSVEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 71 ELGELgSGSALRQHR-RRTAMIFQhhqliERQSALANVLT-GR-----LAFHNTLRslfplPRADQEIALSCLARVGLAD 143
Cdd:COG4172 77 DLLGL-SERELRRIRgNRIAMIFQ-----EPMTSLNPLHTiGKqiaevLRLHRGLS-----GAAARARALELLERVGIPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 144 KAlSRVDK----LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFA 219
Cdd:COG4172 146 PE-RRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFA 224
|
250
....*....|..
gi 1393936756 220 DRVVGLADSQIV 231
Cdd:COG4172 225 DRVAVMRQGEIV 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-240 |
5.44e-31 |
|
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: 114.91 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRTA 89
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY--INGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHhqlierqSALANVLTGR--LAFHNTLRSLfPLPRADQEIALSCLArVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:cd03263 79 YCPQF-------DALFDELTVRehLRFYARLKGL-PKSEIKEEVELLLRV-LGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELT 240
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-239 |
8.08e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSAL-RQHRRRt 88
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD------GEPLdPEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 amifqhhqlI-----ER----------QsalanvltgrLAFHNTLRSLfplPRAD-QEIALSCLARVGLADKALSRVDKL 152
Cdd:COG4152 73 ---------IgylpeERglypkmkvgeQ----------LVYLARLKGL---SKAEaKRRADEWLERLGLGDRANKKVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 153 SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVF 232
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
....*..
gi 1393936756 233 DAAPSEL 239
Cdd:COG4152 210 SGSVDEI 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-239 |
1.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG-SGSALRQHRRRT 88
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQhhqlierqsalanvltgrlafhNTLRSLFPlPRADQEIAL-----------------SCLARVGLADKALSRVDK 151
Cdd:PRK13639 81 GIVFQ----------------------NPDDQLFA-PTVEEDVAFgplnlglskeevekrvkEALKAVGMEGFENKPPHH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
....*...
gi 1393936756 232 FDAAPSEL 239
Cdd:PRK13639 217 KEGTPKEV 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-250 |
2.03e-30 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 114.98 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 6 IQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHR 85
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS--ILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 rrTAMIFQHHQLIERQSALAN--VLTGRLAFHNTLRSlfPLPRaDQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIA 163
Cdd:PRK15056 80 --VAYVPQSEEVDWSFPVLVEdvVMMGRYGHMGWLRR--AKKR-DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSqiVFDAAPSE--LTD 241
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGT--VLASGPTEttFTA 231
|
....*....
gi 1393936756 242 AQLERIYAG 250
Cdd:PRK15056 232 ENLELAFSG 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-239 |
2.37e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.44 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG--SGSALRQHRRRT-AMIFQHHQLIERQS 102
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRRKKiAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANVLTGRlafhntlrSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:PRK10070 123 VLDNTAFGM--------ELAGINAEErREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 182 LDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-239 |
2.55e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG-SGSALRQHR 85
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQH--HQLIErQSALANVLTGRLAFHntlrslfpLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:PRK13636 82 ESVGMVFQDpdNQLFS-ASVYQDVSFGAVNLK--------LPEDEvRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-231 |
2.68e-30 |
|
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: 112.73 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGsaLRQHRRRTAM 90
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTD--LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANvltgrLAFHNTLRSLfplPRADQEIALSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQQ 169
Cdd:cd03301 77 VFQNYALYPHMTVYDN-----IAFGLKLRKV---PKDEIDERVREVAELLQIEHLLDRkPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-238 |
2.89e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVY----PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSA-LRQHR 85
Cdd:PRK13637 3 IKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQH--HQLIErqsalaNVLTGRLAFHNTLRSLfplprADQEI---ALSCLARVGLADKALSrvDK----LSGGQ 156
Cdd:PRK13637 83 KKVGLVFQYpeYQLFE------ETIEKDIAFGPINLGL-----SEEEIenrVKRAMNIVGLDYEDYK--DKspfeLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAP 236
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
..
gi 1393936756 237 SE 238
Cdd:PRK13637 230 RE 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-242 |
6.18e-30 |
|
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: 112.43 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQhrRRTAMIFQHHQLIERQ 101
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATDVPVQE--RNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVltgrlAFHNTLRSLFPLPRADQ--EIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:cd03296 90 TVFDNV-----AFGLRVKPRSERPPEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDA 242
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-233 |
1.42e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 112.08 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGsvtselgELGSGSA-LRQHRRRTAMIFQHHQLIER 100
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTApLAEAREDTRLMFQDARLLPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSALANVLTGrlafhntlrslfpLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:PRK11247 96 KKVIDNVGLG-------------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 181 SLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-226 |
1.56e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.10 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRqhrrrtAM 90
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVltgrlAFHNTLRSLfplPRADQE-IALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNV-----AFGLQLAGV---EKMQRLeIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLA 226
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-231 |
1.62e-29 |
|
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: 110.83 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelGSGSALrQHRRRTAMIFQHHQLIERQ 101
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD----GKPLDI-AARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTgrlafhntLRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:cd03269 86 KVIDQLVY--------LAQLKGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 181 SLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-251 |
2.15e-29 |
|
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: 113.66 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 29 DTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGEL----GSGSALRQHRRRTAMIFQHHQLIERQSAL 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVlqdsARGIFLPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 105 ANVLTGRlafHNTLRSLfPLPRADQEIALsclarVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDP 184
Cdd:COG4148 96 GNLLYGR---KRAPRAE-RRISFDEVVEL-----LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 185 ATSVRVLGLLRDICKEDGITVI-VSlHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLERIYAGR 251
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILyVS-HSLDEVARLADHVVLLEQGRVVASGPLAEvLSRPDLLPLAGGE 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-239 |
2.37e-29 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 113.59 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRRR 87
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI---TRLPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALANV---LTGRlafhntlrslfPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIA 163
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIaygLKNR-----------GMGRAEvAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:TIGR03265 147 RALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-231 |
3.19e-29 |
|
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: 115.55 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYP----------GGVTALRDTSIAFRRGEfTV-LLGLSGAGKSTLLRSLNRLVtPTGGSVT-- 69
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPikrglfrrtvGHVKAVDGVSLTLRRGE-TLgLVGESGSGKSTLGLALLRLI-PSEGEIRfd 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 70 -SELGELgSGSALRQHRRRTAMIFQ--HHQLIERQSALANVLTGrLAFHNTlrslfPLPRADQE-IALSCLARVGLADKA 145
Cdd:COG4172 346 gQDLDGL-SRRALRPLRRRMQVVFQdpFGSLSPRMTVGQIIAEG-LRVHGP-----GLSAAERRaRVAEALEEVGLDPAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 146 LSR-VDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVG 224
Cdd:COG4172 419 RHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMV 498
|
....*..
gi 1393936756 225 LADSQIV 231
Cdd:COG4172 499 MKDGKVV 505
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-239 |
3.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTP--TGGSVTSELGELGSGSALRQH 84
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHqliERQSALANVlTGRLAFHNTLRSLfplPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIA 163
Cdd:PRK13640 83 REKVGIVFQNP---DNQFVGATV-GDDVAFGLENRAV---PRPEmIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-231 |
7.33e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV---TSELGELGSgSALRQHRR 86
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsGHDITRLKN-REVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLierqsalanvLTGRLAFHNTLRSLFPLPRADQEI---ALSCLARVGLADKALSRVDKLSGGQQQRVGIA 163
Cdd:PRK10908 80 QIGMIFQDHHL----------LMDRTVYDNVAIPLIIAGASGDDIrrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 164 RALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-239 |
1.10e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.29 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQhrRRTAMIFQHHQLIERQSALANVltgRLAF 114
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-GQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNI---GLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 115 HNTLRSlfplpRADQEIALSCLA-RVGLADkALSRV-DKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLG 192
Cdd:PRK10771 97 NPGLKL-----NAAQREKLHAIArQMGIED-LLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1393936756 193 LLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-239 |
1.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGV----TALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGELGSGSA-----L 81
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV--TVDDITITHKtkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRTAMIFQ--HHQLIErQSALANVLTGRLAFHNTLRSLfplpradQEIALSCLARVGLADKALSRVD-KLSGGQQQ 158
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFE-DTVEREIIFGPKNFKMNLDEV-------KNYAHRLLMDLGFSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE 238
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
.
gi 1393936756 239 L 239
Cdd:PRK13646 233 L 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-234 |
1.66e-28 |
|
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: 108.07 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT----------SELGELGSgsa 80
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqkniEALRRIGA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 lrqhrrrtamifqhhqLIERQSALANvLTGRlafHNtLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRV 160
Cdd:cd03268 77 ----------------LIEAPGFYPN-LTAR---EN-LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDA 234
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-225 |
1.76e-28 |
|
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: 113.54 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAlRQHRRRTAM 90
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIErQSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLAD--KAL-----SRVDK----LSGGQQQR 159
Cdd:TIGR02857 401 VPQHPFLFA-GTIAENIRLAR-------------PDASDAEIREALERAGLDEfvAALpqgldTPIGEggagLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGL 225
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-240 |
2.01e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.39 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 25 TALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSALRQHRRRTAMIFQhhqliERQ 101
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgEPLAKL-NRAQRKAFRRDIQMVFQ-----DSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTGRLAFHNTLRSLFPLPRADQEI-ALSCLARVGLADKALSRV-DKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:PRK10419 100 SAVNPRKTVREIIREPLRHLLSLDKAERLArASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELT 240
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
2.24e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.33 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 1 MMPHPIQ-DAVLRVDRLSVVY----PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE---- 71
Cdd:PRK13631 11 KVPNPLSdDIILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 72 ----LGELGSGSAL-------RQHRRRTAMIFQ--HHQL----IERQSALANVLTGrlafhntlrslfpLPRAD-QEIAL 133
Cdd:PRK13631 91 gdkkNNHELITNPYskkiknfKELRRRVSMVFQfpEYQLfkdtIEKDIMFGPVALG-------------VKKSEaKKLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 134 SCLARVGLADKALSRVD-KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDiCKEDGITVIVSLHQL 212
Cdd:PRK13631 158 FYLNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTM 236
|
250 260
....*....|....*....|....*..
gi 1393936756 213 EYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13631 237 EHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-236 |
4.70e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.90 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGG---VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGS---VTSELGELGSGSALR 82
Cdd:PRK10535 3 ALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHRRRTAMIFQHHQLIERQSALANVLTGRLaFHNTLRslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAV-YAGLER------KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAP 236
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-225 |
6.51e-28 |
|
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: 107.17 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQhrrrtaMIFQHHQLIERQSALAN 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VLtgrLAFHNTLRSLfplPRADQE-IALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPA 185
Cdd:TIGR01184 75 IA---LAVDRVLPDL---SKSERRaIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1393936756 186 TSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGL 225
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVML 188
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-231 |
6.53e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT------SELgelg 76
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdiRDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 77 sgsALRQHRRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLAD--KAL-----S 147
Cdd:COG1132 408 ---TLESLRRQIGVVPQDTFL----------------FSGTIREniRYGRPDATDEEVEEAAKAAQAHEfiEALpdgydT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 148 RVD----KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVV 223
Cdd:COG1132 469 VVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRIL 545
|
....*...
gi 1393936756 224 GLADSQIV 231
Cdd:COG1132 546 VLDDGRIV 553
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
22-241 |
7.91e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 108.63 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSelgelgSG----SALRQHRRRTAMIFQHHQL 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV------AGydvvREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IERQSALAN-VLTGRLafhntlrslFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:TIGR01188 78 DEDLTGRENlEMMGRL---------YGLPKDEaEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-268 |
8.03e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQHRRR 87
Cdd:COG3845 3 PPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID------GKPVRIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TA------MIFQHHQLIERQSALANVLtgrLAFHNTLRSLFPLPRADQEI-ALSclARVGLADKALSRVDKLSGGQQQRV 160
Cdd:COG3845 76 DAialgigMVHQHFMLVPNLTVAENIV---LGLEPTKGGRLDRKAARARIrELS--ERYGLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELT 240
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETS 229
|
250 260 270
....*....|....*....|....*....|
gi 1393936756 241 DAQLERIYAGRSTTQPAN-TPAEP-PVMLE 268
Cdd:COG3845 230 EEELAELMVGREVLLRVEkAPAEPgEVVLE 259
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-230 |
9.50e-28 |
|
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: 106.10 E-value: 9.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 31 SIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSAlrQHRRRTAMIFQHHQLIERQSALANVltg 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVN-DQSHTGLA--PYQRPVSMLFQENNLFAHLTVRQNI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 111 RLAFHNTLRslfpLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRV 190
Cdd:TIGR01277 92 GLGLHPGLK----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1393936756 191 LGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:TIGR01277 168 LALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-239 |
1.24e-27 |
|
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: 108.35 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 42 LLGLSGAGKSTLLRSLNRLVTPTGGSVtselgeLGSGSALRQ---HRRRTAMIFQHHQLIERQSALANVltgrlAFHNTL 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSI------MLDGEDVTNvppHLRHINMVFQSYALFPHMTVEENV-----AFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 119 RSLfplPRAdqEIA---LSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLR 195
Cdd:TIGR01187 70 RKV---PRA--EIKprvLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1393936756 196 DICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-231 |
1.35e-27 |
|
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: 106.27 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRRRTAMIFQHHQLIERQSALAN 106
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VLTGrlaFHNTLRSLFPLPRADQEIAlsclARVGLaDKALSR-VDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPA 185
Cdd:cd03299 92 IAYG---LKKRKVDKKEIERKVLEIA----EMLGI-DHLLNRkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1393936756 186 TSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-221 |
1.44e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.78 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRL------VTPTGGSVTSELGELGSGSAL 81
Cdd:PRK14239 3 EPILQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRTAMIFQHHQLIErQSALANVLTG-RLafhNTLRSLFPLPRADQE--IALSCLARVG--LADKALSrvdkLSGGQ 156
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGlRL---KGIKDKQVLDEAVEKslKGASIWDEVKdrLHDSALG----LSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIckEDGITVIVSLHQLEYARRFADR 221
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-250 |
1.71e-27 |
|
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: 105.83 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGElgSGSALRQHRRR 87
Cdd:COG0410 1 MPMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-GE--DITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIF---QHHQLIERQSALANVLTGRLAfhntlRSLFPLPRADQEIALSCLARvgLADKALSRVDKLSGGQQQRVGIAR 164
Cdd:COG0410 77 RLGIGyvpEGRRIFPSLTVEENLLLGAYA-----RRDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL-TDAQ 243
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELlADPE 228
|
....*..
gi 1393936756 244 LERIYAG 250
Cdd:COG0410 229 VREAYLG 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-246 |
2.14e-27 |
|
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: 105.68 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAM 90
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVLTGrlafhntlrsLFPLPRADQEIALSCLARVGLADKALSRV-DKLSGGQQQRVGIARALAQQ 169
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTG----------LAALPRRSRKIPDEIYELFPVLKEMLGRRgGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLER 246
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRR 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-249 |
2.33e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 106.08 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 31 SIAFRRGEFTVLLGLSGAGKSTLLRSLNRLvTPTGGSVT---SELGELgSGSALRQHRrrtAMIFQHhqlierQSALANV 107
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILlngRPLSDW-SAAELARHR---AYLSQQ------QSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 108 LTGR-LAFHntLRSLFPLPRADQEIALSClARVGLADKaLSR-VDKLSGGQQQRVGIARALAQ-------QPAIILADEP 178
Cdd:COG4138 85 PVFQyLALH--QPAGASSEAVEQLLAQLA-EALGLEDK-LSRpLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 179 VASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLERIYA 249
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPENLSEVFG 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-231 |
4.39e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLV-----TPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQ 96
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLD-GQDIFKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 LIERQSALANVLTGRlafhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVD----KLSGGQQQRVGIARALAQQPAI 172
Cdd:PRK14247 93 PIPNLSIFENVALGL-----KLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLRDICKEdgITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-252 |
6.54e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.56 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALR-----QHRRRTAMIFQHHQ 96
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvlEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 LIErQSALANVLTGrlafhntLRSLFPLPRAD-QEIALSCLARVGLADKALSRVD----KLSGGQQQRVGIARALAQQPA 171
Cdd:PRK14271 112 PFP-MSIMDNVLAG-------VRAHKLVPRKEfRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 172 IILADEPVASLDPATSVRVLGLLRDICkeDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL----TDAQLERI 247
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLfsspKHAETARY 261
|
....*
gi 1393936756 248 YAGRS 252
Cdd:PRK14271 262 VAGLS 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-220 |
9.99e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRL--VTPTG---GSVTSELGEL-GSGSAL 81
Cdd:PRK14243 8 ETVLRTENLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLyAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRTAMIFQHHQLIERqSALANVLTGR--LAFHNTLRSLfpLPRADQEIALSCLARVGLADKALSrvdkLSGGQQQR 159
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPK-SIYDNIAYGAriNGYKGDMDEL--VERSLRQAALWDEVKDKLKQSGLS----LSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSlHQLEYARRFAD 220
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVT-HNMQQAARVSD 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-239 |
1.58e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVT----ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSGSALRQ 83
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQ--HHQLIErQSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVD-KLSGGQQQRV 160
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFE-NTVLKDVEFGPKNFGFS-------EDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-232 |
2.02e-26 |
|
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: 102.24 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLN--RLVTPTGGSVTSElgelGSGSALRQHRRRT 88
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLIN----GRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERqsalanvLTGR--LAFHNTLRSLfplpradqeialsclarvgladkalsrvdklSGGQQQRVGIARAL 166
Cdd:cd03213 85 GYVPQDDILHPT-------LTVRetLMFAAKLRGL-------------------------------SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDICKeDGITVIVSLHQLEYAR-RFADRVVGLADSQIVF 232
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIfELFDKLLLLSQGRVIY 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-267 |
2.12e-26 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 104.14 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTaLRDTSIAFRRGEFTVLLGLSGAGKSTLLRS----LNRLVTPTGGSVTSEL---GE-LGSGSAL 81
Cdd:PRK13547 1 MLTADHLHVARRHRAI-LRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGARVTGDVtlnGEpLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRtAMIFQHHQLIERQSALANVLTGRlafHNTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:PRK13547 80 RLARLR-AVLPQAAQPAFAFSAREIVLLGR---YPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQ---------QPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVF 232
Cdd:PRK13547 156 FARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393936756 233 DAAPSE-LTDAQLERIYAGRstTQPANTP-AEPPVML 267
Cdd:PRK13547 236 HGAPADvLTPAHIARCYGFA--VRLVDAGdGVPPVIV 270
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-227 |
2.12e-26 |
|
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: 102.90 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVT--ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGS--VTSELGELGSGSAL-RQ--HRRRTAMIF-- 92
Cdd:COG4778 20 GGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLAQASpREilALRRRTIGYvs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QHHQLIERQSALaNVLTGRLafhntLRSLFPLPRAdQEIALSCLARVGLADK--ALSRVdKLSGGQQQRVGIARALAQQP 170
Cdd:COG4778 100 QFLRVIPRVSAL-DVVAEPL-----LERGVDREEA-RARARELLARLNLPERlwDLPPA-TFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-233 |
4.85e-26 |
|
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: 101.68 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRTAMIFQHHQLIERQ 101
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT--VDGFDVVKEPAEARRRLGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLT-GRLafhntlrslFPLPRADQEIALSCLA-RVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:cd03266 94 TARENLEYfAGL---------YGLKGDELTARLEELAdRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:cd03266 165 TGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-239 |
6.89e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVY----PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGELGSGSALRQH- 84
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV--TVGDIVVSSTSKQKe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 ----RRRTAMIFQ--HHQLIErQSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVD-KLSGGQQ 157
Cdd:PRK13643 79 ikpvRKKVGVVFQfpESQLFE-ETVLKDVAFGPQNFGIP-------KEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPS 237
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS 229
|
..
gi 1393936756 238 EL 239
Cdd:PRK13643 230 DV 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
7.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.51 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLGELGSGSALRQHRRR 87
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV-MGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQH--HQLIErQSALANVLTG----RLAFHNTLRSLfplpradqEIALSCLARVGLADKALSRvdkLSGGQQQRVG 161
Cdd:PRK13647 81 VGLVFQDpdDQVFS-STVWDDVAFGpvnmGLDKDEVERRV--------EEALKAVRMWDFRDKPPYH---LSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLrDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
...
gi 1393936756 242 AQL 244
Cdd:PRK13647 228 EDI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
3.01e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 21 PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV-----------TSELGELGSGSA--------- 80
Cdd:PRK13651 17 PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKEKVLEKLviqktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 ---LRQHRRRTAMIFQ--HHQLIErQSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVD-KLSG 154
Cdd:PRK13651 97 ikkIKEIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVS-------KEEAKKRAAKYIELVGLDESYLQRSPfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 155 GQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDA 234
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
....
gi 1393936756 235 APSE 238
Cdd:PRK13651 248 DTYD 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-239 |
3.86e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSA---LRQHRRRTAMIFQ--HHQLIEr 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdIKQIRKKVGLVFQfpESQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSALANVLTGRLAFHNTlrslfplPRADQEIALSCLARVGLADKALSRVD-KLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVS-------QEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 180 ASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-222 |
3.93e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.71 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 21 PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLGE--LG-SGSALRQHRRRTAMIFQhhql 97
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW-LGKdlLGmKDDEWRAVRSDIQMIFQ---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 ierqSALANvLTGRLAFHNT----LRSLFP-LPRAD-QEIALSCLARVGLADKALSRV-DKLSGGQQQRVGIARALAQQP 170
Cdd:PRK15079 106 ----DPLAS-LNPRMTIGEIiaepLRTYHPkLSRQEvKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRV 222
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
26-227 |
1.05e-24 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 98.25 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSGSALRQHRRRTAMIFQHHQLIERQS 102
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTlagKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANV---LTGRlAFHNTLRslfpLPRADQEIALsclarVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:NF038007 100 IFDNValpLKYR-GVAKKER----IERVNQVLNL-----FGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1393936756 180 ASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEyARRFADRVVGLAD 227
Cdd:NF038007 170 GNLDSKNARAVLQQLKYI-NQKGTTIIMVTHSDE-ASTYGNRIINMKD 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-238 |
3.66e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVV-YPGGV---TALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsG---SALRQ 83
Cdd:COG1101 2 LELKNLSKTfNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID------GkdvTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRrTAMI---FQHHQL-------IERQSALAnvltgrlAFHNTLRSL-FPLPRADQEIALSCLARV--GLADKALSRVD 150
Cdd:COG1101 76 YKR-AKYIgrvFQDPMMgtapsmtIEENLALA-------YRRGKRRGLrRGLTKKRRELFRELLATLglGLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....*...
gi 1393936756 231 VFDAAPSE 238
Cdd:COG1101 228 ILDVSGEE 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-230 |
4.53e-24 |
|
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: 95.36 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTA-LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSgSALRQHRRRTA 89
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLierqsalanvLTGRLAfhntlrslfplpradQEIalsclarvgladkalsrvdkLSGGQQQRVGIARALAQQ 169
Cdd:cd03246 80 YLPQDDEL----------FSGSIA---------------ENI--------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRfADRVVGLADSQI 230
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-245 |
7.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTA 89
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQH--HQLIERqsalanVLTGRLAFHNTLRSLFPL---PRADQeialsCLARVGLADKALSRVDKLSGGQQQRVGIAR 164
Cdd:PRK13644 81 IVFQNpeTQFVGR------TVEEDLAFGPENLCLPPIeirKRVDR-----ALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEyARRFADRVVGLADSQIVFDAAP-SELTDAQ 243
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPeNVLSDVS 227
|
..
gi 1393936756 244 LE 245
Cdd:PRK13644 228 LQ 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-238 |
1.71e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAlrqHRRRTAMIFQHHQLIERQ 101
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHVNTVFQSYALFPHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVltgrlAFhnTLRsLFPLPRAdqEIA---LSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK09452 102 TVFENV-----AF--GLR-MQKTPAA--EITprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE 238
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-247 |
2.71e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.83 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 5 PIQDAVLRVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtSELGELGSGSALRQ 83
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI-KIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQH--HQLIErQSALANVltgrlAF--HNTLrslfpLPRAD-QEIALSCLARVGLaDKALSR-VDKLSGGQQ 157
Cdd:PRK13632 81 IRKKIGIIFQNpdNQFIG-ATVEDDI-----AFglENKK-----VPPKKmKDIIDDLAKKVGM-EDYLDKePQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPS 237
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
250
....*....|.
gi 1393936756 238 E-LTDAQLERI 247
Cdd:PRK13632 228 EiLNNKEILEK 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-241 |
2.91e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.38 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 1 MMPHPIqdavLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSEL--GELGSG 78
Cdd:PRK11701 1 MMDQPL----LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 79 SALRQHRRRTAM------IFQHHQ--LIERQSALANV---LTGRLAFH-NTLRslfplpradqEIALSCLARVGLAdkaL 146
Cdd:PRK11701 76 YALSEAERRRLLrtewgfVHQHPRdgLRMQVSAGGNIgerLMAVGARHyGDIR----------ATAGDWLERVEID---A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 147 SRVDKL----SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRV 222
Cdd:PRK11701 143 ARIDDLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRL 222
|
250
....*....|....*....
gi 1393936756 223 VGLADSQIVfdaaPSELTD 241
Cdd:PRK11701 223 LVMKQGRVV----ESGLTD 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-245 |
4.81e-23 |
|
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: 97.95 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRL--VTPTGGSVT---------------SELG 73
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 74 ELGS--GSAL---------------RQHRRRTAMIFQH-HQLIERQSALANVLtgrlafhNTLRSL-FPLPRADQEiALS 134
Cdd:TIGR03269 80 EPCPvcGGTLepeevdfwnlsdklrRRIRKRIAIMLQRtFALYGDDTVLDNVL-------EALEEIgYEGKEAVGR-AVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 135 CLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEY 214
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260 270
....*....|....*....|....*....|.
gi 1393936756 215 ARRFADRVVGLADSQIVFDAAPSELTDAQLE 245
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVAVFME 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-272 |
6.16e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.55 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT------SEL-----GELGSGsalrqhrrrtaM 90
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninyNKLdhklaAQLGIG-----------I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIERQSALANVLTGRLAfhntLRSLFPLPRAD----QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHL----TKKVCGVNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 167 AQQPAIILADEPVASLDPAtSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLER 246
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
250 260
....*....|....*....|....*...
gi 1393936756 247 IYAGRSTTQ--PANTPAEPPVMLEPSLE 272
Cdd:PRK09700 240 LMVGRELQNrfNAMKENVSNLAHETVFE 267
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-222 |
8.22e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYP---------GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGEL-- 75
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 76 GSGSALRQHRRRTAMIFQ--HHQLIERQSaLANVLTGRLAFhNTlrslfPLPRADQ-EIALSCLARVGLADKALSRVDKL 152
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQnpYGSLNPRKK-VGQILEEPLLI-NT-----SLSAAERrEKALAMMAKVGLRPEHYDRYPHM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 153 -SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRV 222
Cdd:PRK11308 155 fSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEV 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-233 |
2.31e-22 |
|
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: 92.40 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGELGSGSALRQHRRRTAMIF-QHHQLIERQS 102
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV--RVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANvltgrlafHNTLRSLFPLP--RADQEIA-LSCLARVG-LADKAlsrVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:cd03267 112 VIDS--------FYLLAAIYDLPpaRFKKRLDeLSELLDLEeLLDTP---VRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-239 |
3.15e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRRRTAMIFQHHQLIERQS 102
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---SHVPPYQRPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANVLTGrlafhntLRSlFPLPRAdqEIALSC---LARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:PRK11607 108 VEQNIAFG-------LKQ-DKLPKA--EIASRVnemLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-212 |
3.49e-22 |
|
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: 95.51 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALR 82
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT--LDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 QHRRRTAMIFQHHQLIERQSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLADKALSRVD-----------K 151
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLRLAR-------------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIckEDGITVIVSLHQL 212
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-222 |
3.79e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 91.69 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsgsalrQHRRRTAM 90
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFD-----------GHPWTRKD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIErQSALANVLTGR--LAFHNTLRSLfplprADQEIaLSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ 168
Cdd:TIGR03740 69 LHKIGSLIE-SPPLYENLTARenLKVHTTLLGL-----PDSRI-DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLN 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 169 QPAIILADEPVASLDPatsvrvLGL--LRDICK---EDGITVIVSLHQLEYARRFADRV 222
Cdd:TIGR03740 142 HPKLLILDEPTNGLDP------IGIqeLRELIRsfpEQGITVILSSHILSEVQQLADHI 194
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
9-231 |
4.37e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.21 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGG--------VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSa 80
Cdd:COG4167 3 ALLEVRNLSKTFKYRtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 lRQHR-RRTAMIFQH--HQLIERQSaLANVLTGRLAFhNTlrSLFPLPRADQEIALscLARVGL-ADKALSRVDKLSGGQ 156
Cdd:COG4167 82 -YKYRcKHIRMIFQDpnTSLNPRLN-IGQILEEPLRL-NT--DLTAEEREERIFAT--LRLVGLlPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-239 |
5.90e-22 |
|
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: 91.45 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPG--GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgsgsALRQHRRRTAMIFQH 94
Cdd:cd03249 10 YPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgVDIRDL----NLRWLRSQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 95 HQLIERqSALANVLTGRLafhntlrslfplPRADQEIALSCLAR------VGLADKALSRV----DKLSGGQQQRVGIAR 164
Cdd:cd03249 86 PVLFDG-TIAENIRYGKP------------DATDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
27-239 |
1.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.72 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHqliERQSALAN 106
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-GDLLTEENVWDIRHKIGMVFQNP---DNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VlTGRLAF--------HNTLRSlfplpRADQEIALsclarVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK13650 99 V-EDDVAFglenkgipHEEMKE-----RVNEALEL-----VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQL-EYArrFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLdEVA--LSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-231 |
1.64e-21 |
|
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: 89.86 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVY-PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT------SELGelgsgsaLRQ 83
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiSKIG-------LHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS-LFPLPRADQEIALSCLARVGLADKALSRVDKL---------- 152
Cdd:cd03244 76 LRSRISIIPQDPVL----------------FSGTIRSnLDPFGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggen 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 153 -SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLE----YarrfaDRVVGLAD 227
Cdd:cd03244 140 lSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDtiidS-----DRILVLDK 212
|
....
gi 1393936756 228 SQIV 231
Cdd:cd03244 213 GRVV 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-245 |
1.82e-21 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 90.27 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALR---QHR 85
Cdd:TIGR02323 2 PLLQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQlseAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTA-----MIFQHHQ--LIERQSALANVLTGRLAF----HNTLRslfplpradqEIALSCLARVGLAdkaLSRVDKL-- 152
Cdd:TIGR02323 81 RRLMrtewgFVHQNPRdgLRMRVSAGANIGERLMAIgarhYGNIR----------ATAQDWLEEVEID---PTRIDDLpr 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 153 --SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:TIGR02323 148 afSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
250
....*....|....*
gi 1393936756 231 VfdaaPSELTDAQLE 245
Cdd:TIGR02323 228 V----ESGLTDQVLD 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-239 |
1.98e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.09 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQhrRRTAMIFQHHQLIERQ 101
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-GEDVTHRSIQQ--RDICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTGrlafhntlrsLFPLPRADQEIAL---SCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK11432 94 SLGENVGYG----------LKMLGVPKEERKQrvkEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-239 |
2.12e-21 |
|
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: 92.10 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 38 EFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE---LGELGSGSALRQHRRRTAMIFQHHQLIERQSALANVLTGRLaf 114
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 115 hntlRSLFPLPRADQEIALSCLARVGLADKalsRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLL 194
Cdd:TIGR02142 102 ----RARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1393936756 195 RDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-227 |
3.02e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.95 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 4 HPIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPtggsvtselgelGSGSALRQ 83
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY------------GSGRIARP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHHQLIErqsalanvltGrlafhnTLRS--LFPLP--RADQEIALSCLARVGLADKAlSRVDK-------L 152
Cdd:COG4178 424 AGARVLFLPQRPYLPL----------G------TLREalLYPATaeAFSDAELREALEAVGLGHLA-ERLDEeadwdqvL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 153 SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYArRFADRVVGLAD 227
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGHRSTLA-AFHDRVLELTG 558
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-241 |
3.86e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLsVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQ-----H 84
Cdd:PRK14246 10 VFNISRL-YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidaikL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLIERQSALANVLtgrlafhntlrslFPLP-------RADQEIALSCLARVGLADKALSRVD----KLS 153
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIA-------------YPLKshgikekREIKKIVEECLRKVGLWKEVYDRLNspasQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdgITVIVSLHQLEYARRFADRVVGLADSQIV-- 231
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVew 233
|
250
....*....|....*.
gi 1393936756 232 ------FDAAPSELTD 241
Cdd:PRK14246 234 gssneiFTSPKNELTE 249
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-211 |
4.22e-21 |
|
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: 88.87 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTptGGSVTSelGE-LGSGSALRQH--RRRTAMIFQHHQLIERqsa 103
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTS--GQiLFNGQPRKPDqfQKCVAYVRQDDILLPG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 104 lanvLTGR--LAFHNTLRS--LFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:cd03234 96 ----LTVRetLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGItVIVSLHQ 211
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRI-VILTIHQ 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-241 |
4.64e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 19 VYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVT-PTGGSVTSELGELGSGSALR-----QHRRRTAMIF 92
Cdd:PRK14267 12 VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElNEEARVEGEVRLFGRNIYSPdvdpiEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QHHQLIERQSALANVLTGrLAFHNTLRSLFPLPradqEIALSCLARVGLADKALSRVD----KLSGGQQQRVGIARALAQ 168
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD----ERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKEdgITVIVSLHQLEYARRFADRV--------VGLADSQIVFDAAPSELT 240
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVaflylgklIEVGPTRKVFENPEHELT 244
|
.
gi 1393936756 241 D 241
Cdd:PRK14267 245 E 245
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-239 |
6.17e-21 |
|
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: 88.44 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLIE 99
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID-GQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 rQSALANVLTGRlafhntlrslfplPRA-DQEIALSCLAR------VGLADKALSRVD----KLSGGQQQRVGIARALAQ 168
Cdd:cd03253 89 -DTIGYNIRYGR-------------PDAtDEEVIEAAKAAqihdkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-268 |
6.81e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.77 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlVTPTG---GSVTSElGELGSGSALRQHRRRTAMIFqhHQ-- 96
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFD-GEVCRFKDIRDSEALGIVII--HQel 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 -LIERQSALANVLTGRlafHNTLRSLFPLPRADQEiALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:NF040905 88 aLIPYLSIAENIFLGN---ERAKRGVIDWNETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIV--FDAAPSELTDAQLERIYAGRST 253
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIetLDCRADEVTEDRIIRGMVGRDL 242
|
250
....*....|....*..
gi 1393936756 254 TQ--PANTPAEPPVMLE 268
Cdd:NF040905 243 EDryPERTPKIGEVVFE 259
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-220 |
7.16e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLvtptgGSVTSELGELGSGSALRQH------ 84
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-----NELESEVRVEGRVEFFNQNiyerrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 -----RRRTAMIFQHHQLIErQSALANVltgrlAFHNTLRSLFPLPRADqEIALSCLARVGLADKALSRVDK----LSGG 155
Cdd:PRK14258 82 nlnrlRRQVSMVHPKPNLFP-MSVYDNV-----AYGVKIVGWRPKLEID-DIVESALKDADLWDEIKHKIHKsaldLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 156 QQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFAD 220
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-241 |
8.76e-21 |
|
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: 88.05 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLIE 99
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-GIDIRDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 RqSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLAD--KAL---------SRVDKLSGGQQQRVGIARALAQ 168
Cdd:cd03254 91 G-TIMENIRLGR-------------PNATDEEVIEAAKEAGAHDfiMKLpngydtvlgENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYArRFADRVVGLADSQIVFDAAPSELTD 241
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-242 |
9.07e-21 |
|
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: 88.31 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 21 PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSgSALRQHRRRTAMIFQHHQLIER 100
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL-ADPAWLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 qSALANVLTGRLAFhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:cd03252 91 -SIRDNIALADPGM--SMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 181 SLDPATSVRVLGLLRDICkeDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTDA 242
Cdd:cd03252 168 ALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-223 |
1.66e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELgsgSALRQHRRRTAMIFQHHQLIERQSALAN 106
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VltgrlAFHNTLrslfpLPR-------ADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:PRK10851 95 I-----AFGLTV-----LPRrerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVV 223
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-239 |
2.04e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 16 LSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQhh 95
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR-GEPITKENIREVRKFVGLVFQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 96 qlierqsalanvltgrlafhNTLRSLFPlPRADQEIAL-----------------SCLARVGLADkALSRV-DKLSGGQQ 157
Cdd:PRK13652 86 --------------------NPDDQIFS-PTVEQDIAFgpinlgldeetvahrvsSALHMLGLEE-LRDRVpHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPS 237
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
..
gi 1393936756 238 EL 239
Cdd:PRK13652 224 EI 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-263 |
2.13e-20 |
|
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: 90.27 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlVTPTG---GSVTSELGELGSGSALRQHRRRTAMIFQHHQLI 98
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 ERQSALANVLTGRLAFHNTLRSlfplprADQEIALSC---LARVGLADKALSR-VDKLSGGQQQRVGIARALAQQPAIIL 174
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPGGRM------AYNAMYLRAknlLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 175 ADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAGRSTT 254
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREIT 243
|
....*....
gi 1393936756 255 qpANTPAEP 263
Cdd:TIGR02633 244 --SLYPHEP 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-233 |
2.43e-20 |
|
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: 86.49 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgeLGSGSALRQH-----RR 86
Cdd:cd03245 5 FRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV------LLDGTDIRQLdpadlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLADKAL-----------SRVDKLS 153
Cdd:cd03245 79 NIGYVPQDVTL----------------FYGTLRDniTLGAPLADDERILRAAELAGVTDFVNkhpngldlqigERGRGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDgiTVIVSLHQLEyARRFADRVVGLADSQIVFD 233
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-242 |
3.99e-20 |
|
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: 89.54 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQH----- 84
Cdd:TIGR03375 464 IEFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLD------GVDIRQIdpadl 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSCLARVGLADKA-----------LSRVDK 151
Cdd:TIGR03375 538 RRNIGYVPQDPRL----------------FYGTLRDniALGAPYADDEEILRAAELAGVTEFVrrhpdgldmqiGERGRS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEyARRFADRVVGLADSQIV 231
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTS-LLDLVDRIIVMDNGRIV 678
|
250
....*....|.
gi 1393936756 232 FDAAPSELTDA 242
Cdd:TIGR03375 679 ADGPKDQVLEA 689
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-213 |
4.26e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.17 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 25 TALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLV--TPTGGSVTSELGELGSGSALrqhrrrtamifqhhqlIERQS 102
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASL----------------IDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANVLTgrlafhntlrslfplpradqeiALSCLARVGLADKAL--SRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:COG2401 108 RKGDFKD----------------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|...
gi 1393936756 181 SLDPATSVRVLGLLRDICKEDGITVIVSLHQLE 213
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-223 |
5.40e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.58 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSGSALRQHRRR 87
Cdd:PRK11300 6 LSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TamiFQHHQLIERQSALANVLtgrLAFH-----NTLRSLFPLP---RADQEI---ALSCLARVGLADKALSRVDKLSGGQ 156
Cdd:PRK11300 85 T---FQHVRLFREMTVIENLL---VAQHqqlktGLFSGLLKTPafrRAESEAldrAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVV 223
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-229 |
8.83e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVvYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTP---TGGSVTSELGELgsgSALRQHRRR 87
Cdd:COG4136 2 LSLENLTI-TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL---TALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIERQSALANVLtgrlafhntlrslFPLPR-----ADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLA-------------FALPPtigraQRRARVEQALEEAGLAGFADRDPATLSGGQRARVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEyARRFADRVVGLADSQ 229
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDLGNWQ 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-231 |
1.20e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT------SELGElgsgSALRQ 83
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqpiADYSE----AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 hrrrtAMIfqhhqlierqsalanVLTGRL-AFHNTLRS--LFPLPRADQEIALSCLARVGLA-----DKALS-------R 148
Cdd:PRK11160 415 -----AIS---------------VVSQRVhLFSATLRDnlLLAAPNASDEALIEVLQQVGLEklledDKGLNawlgeggR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 149 vdKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRFaDRVVGLADS 228
Cdd:PRK11160 475 --QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNG 549
|
...
gi 1393936756 229 QIV 231
Cdd:PRK11160 550 QII 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-231 |
1.39e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVY-PGGV--TALRDTSIAFRRGEFTVLLGLSGAGKS-TLLRSLNRLVTP----TGGSVTSELGEL--GSG 78
Cdd:PRK15134 4 PLLAIENLSVAFrQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 79 SALRQHR-RRTAMIFQHHQL-------IERQsaLANVLtgrlAFHNTLRSlfplPRADQEIaLSCLARVGLADKALSRVD 150
Cdd:PRK15134 84 QTLRGVRgNKIAMIFQEPMVslnplhtLEKQ--LYEVL----SLHRGMRR----EAARGEI-LNCLDRVGIRQAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 ---KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:PRK15134 153 yphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
....
gi 1393936756 228 SQIV 231
Cdd:PRK15134 233 GRCV 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-252 |
1.46e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.66 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPGgVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRR 86
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFQHHQLIERQSALANVLTGRLAFhntlRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGQLPH----KGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIV--FDAApSELTDAQL 244
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVatFDDM-AQVDRDQL 233
|
....*...
gi 1393936756 245 ERIYAGRS 252
Cdd:PRK11288 234 VQAMVGRE 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-231 |
1.56e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT--SELGELGSGSALRQHRRRTAMIFQ--HHQLIE 99
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfnGQRIDTLSPGKLQALRRDIQFIFQdpYASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 RQSALANVLTgRLAFHNTLRSlfplpRADQEIALSCLARVGL-ADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK10261 417 RQTVGDSIME-PLRVHGLLPG-----KAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-255 |
1.65e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlVTPTGgsvTSElGE-LGSGSALR-QHRRRT-----AMIFQH 94
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHG---TYE-GEiIFEGEELQaSNIRDTeragiAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 95 HQLIERQSALANVLTGRLAFHNTLRSLFPLPRADQEIalscLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIIL 174
Cdd:PRK13549 91 LALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKL----LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 175 ADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAGRSTT 254
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGRELT 245
|
.
gi 1393936756 255 Q 255
Cdd:PRK13549 246 A 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-239 |
2.20e-19 |
|
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: 87.55 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 6 IQDAVLRVDRLSVVY----PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV----------TSE 71
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 72 LGELGSGSAlrqhRRRTAMIFQHHQLIERQSALANvLTGRLAFHntlrslFPLPRADQEiALSCLARVGLAD-KALSRVD 150
Cdd:TIGR03269 355 PGPDGRGRA----KRYIGILHQEYDLYPHRTVLDN-LTEAIGLE------LPDELARMK-AVITLKMVGFDEeKAEEILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 K----LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLA 226
Cdd:TIGR03269 423 KypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|...
gi 1393936756 227 DSQIVFDAAPSEL 239
Cdd:TIGR03269 503 DGKIVKIGDPEEI 515
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-250 |
3.66e-19 |
|
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: 83.75 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGELgSGSALRQHRR-RTA 89
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI--LLDGQ-DITKLPMHKRaRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIF--QHHQLIERQSALANVLtgrLAFHntlrsLFPLPRADQEIAL-SCLARVGLADKALSRVDKLSGGQQQRVGIARAL 166
Cdd:cd03218 77 IGYlpQEASIFRKLTVEENIL---AVLE-----IRGLSKKEREEKLeELLEEFHITHLRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 167 AQQPAIILADEPVASLDPaTSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL-TDAQLE 245
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDP-IAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIaANELVR 227
|
....*
gi 1393936756 246 RIYAG 250
Cdd:cd03218 228 KVYLG 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-250 |
4.94e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLGELGSGSAlRQHRRRTAMIFQHHQLIERQ 101
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV-LGVPVPARA-RLARARIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLT-GRLAFHNTlrslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:PRK13536 130 TVRENLLVfGRYFGMST--------REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 181 SLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLE----RIYAG 250
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGcqviEIYGG 274
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-239 |
5.17e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELG-SGSALRQHRRRTAMIFQHHQlierQSALA 105
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGLLALRQQVATVFQDPE----QQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NVLTGRLAFhntlrSLFPLPRADQEIAlsclARVglaDKALSRVDK----------LSGGQQQRVGIARALAQQPAIILA 175
Cdd:PRK13638 93 TDIDSDIAF-----SLRNLGVPEAEIT----RRV---DEALTLVDAqhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-249 |
6.41e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 30 TSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLvTPTGGSVTSELGELGSGSALRQHRRRTamifqhhQLIERQSALANVLT 109
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRA-------YLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 110 grlaFHNTLRSLFPLPR-ADQEIALSCLA-RVGLADKALSRVDKLSGGQQQRVGIARALAQ-QPAI------ILADEPVA 180
Cdd:PRK03695 87 ----FQYLTLHQPDKTRtEAVASALNEVAeALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 181 SLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLERIYA 249
Cdd:PRK03695 163 SLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPENLAQVFG 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-230 |
1.20e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT------SELGELGSgSALRQhrRRTAMIFQHHQLIERQSALANVL 108
Cdd:PRK10584 34 KRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplHQMDEEAR-AKLRA--KHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TGRLafhntLRSLFPLPRADQEIALscLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSV 188
Cdd:PRK10584 111 LPAL-----LRGESSRQSRNGAKAL--LEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1393936756 189 RVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQI 230
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-227 |
2.58e-18 |
|
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: 80.59 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtptggsvtseLGELGSGSALRQHRRRTAMIFQhhqlierQSALA 105
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--------------LGELEKLSGSVSVPGSIAYVSQ-------EPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NvltgrlafhNTLRS--LFPLP----RADQEIALSCLARvglaD-KALSRVDK---------LSGGQQQRVGIARALAQQ 169
Cdd:cd03250 79 N---------GTIREniLFGKPfdeeRYEKVIKACALEP----DlEILPDGDLteigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 170 PAIILADEPVASLDPATSVR-----VLGLLRdickeDGITVIVSLHQLEYARRfADRVVGLAD 227
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHifencILGLLL-----NNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-244 |
2.86e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 5 PIQDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtSELGELGSGSAlRQH 84
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-SLCGEPVPSRA-RHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLIERQSALANVLT-GRLafhntlrslFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGI 162
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVfGRY---------FGLSAAAaRALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDA 242
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
..
gi 1393936756 243 QL 244
Cdd:PRK13537 229 EI 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
29-247 |
2.89e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 29 DTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtptGGSVTSELGELG---------SGSALRQHRRRTAMIFQHHQLIE 99
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLI-------GGQIAPDHGEILfdgenipamSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 RQSALANVltgrlAFhnTLRSLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK11831 98 DMNVFDNV-----AY--PLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERI 247
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRV 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-233 |
2.99e-18 |
|
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: 80.05 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRTA 89
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT--LDGVPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLierqsalanvltgrlaFHNTLRSlfplpradqeialsclaRVGLadkalsrvdKLSGGQQQRVGIARALAQQ 169
Cdd:cd03247 79 VLNQRPYL----------------FDTTLRN-----------------NLGR---------RFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDgiTVIVSLHQLEYARRFaDRVVGLADSQIVFD 233
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-212 |
3.80e-18 |
|
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: 80.10 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQhrrrtam 90
Cdd:TIGR01189 1 LAARNLACSR-GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPH------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 ifQHHQLIERQSALANVLTgrlAFHNtLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQP 170
Cdd:TIGR01189 73 --ENILYLGHLPGLKPELS---ALEN-LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQL 212
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-251 |
3.82e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYP---------------------GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV 68
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 69 TSElGELGSgsalrqhrrrtamifqhhqLIERQSALANVLTGR-LAFHNTLrsLFPLPRADQE------IALSclarvGL 141
Cdd:COG1134 84 EVN-GRVSA-------------------LLELGAGFHPELTGReNIYLNGR--LLGLSRKEIDekfdeiVEFA-----EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 142 ADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEpvasldpATSV-------RVLGLLRDICKEDGITVIVSlHQLEY 214
Cdd:COG1134 137 GDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-------VLAVgdaafqkKCLARIRELRESGRTVIFVS-HSMGA 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 1393936756 215 ARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAGR 251
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGRE 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-242 |
3.94e-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: 80.74 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTA 89
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-GHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQEIALSClARVGLADKALSRVD------------KLSGG 155
Cdd:cd03251 80 LVSQDVFL----------------FNDTVAEniAYGRPGATREEVEEA-ARAANAHEFIMELPegydtvigergvKLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 156 QQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIVFDAA 235
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
....*..
gi 1393936756 236 PSELTDA 242
Cdd:cd03251 220 HEELLAQ 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-207 |
4.81e-18 |
|
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: 83.64 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 2 MPHPIQDAVLRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgeLGsGSA 80
Cdd:COG4618 322 MPLPRPKGRLSVENLTVVPPGSkRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR-----LD-GAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHRRRTamiFQHH-----QLIErqsalanVLTGRLAfHNTLRslFPLPRADQEIALSCLARV-----GLADKALSRVD 150
Cdd:COG4618 396 LSQWDREE---LGRHigylpQDVE-------LFDGTIA-ENIAR--FGDADPEKVVAAAKLAGVhemilRLPDGYDTRIG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 151 ----KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIV 207
Cdd:COG4618 463 eggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVV 522
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-231 |
4.86e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.28 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 28 RDTSIAFRRGEFTVLLGLSGAGKS-TLLRSLNRL---VTPTGGSVTSElGELGSGSALRQhrRRTAMIFQHhqlieRQSA 103
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLD-GKPVAPCALRG--RKIATIMQN-----PRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 104 LANVLTGRLAFHNTLRSLFPLPRADQeiALSCLARVGLADKAlsRVDKL-----SGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAA--RVLKLypfemSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-239 |
5.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.68 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYP--GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHR 85
Cdd:PRK13642 2 NKILEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID-GELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHqliERQSALANVlTGRLAFHNTLRSLfPLPRADQEIALSCLArVGLADKALSRVDKLSGGQQQRVGIARA 165
Cdd:PRK13642 81 RKIGMVFQNP---DNQFVGATV-EDDVAFGMENQGI-PREEMIKRVDEALLA-VNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 166 LAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSEL 239
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-231 |
8.09e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgeLGSG---SALRQHrr 86
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-----LGETvkiGYFDQH-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 rtamifqHHQLIERQSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLA-DKALSRVDKLSGGQQQRVGIARA 165
Cdd:COG0488 387 -------QEELDPDKTVLDELRDGA-------------PGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 166 LAQQPAIILADEPVASLDPATsVRVLgllrdickEDGI-----TVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET-LEAL--------EEALddfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-211 |
1.01e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQHRRRTA 89
Cdd:PRK13539 2 MLEGEDLACVR-GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD------GGDIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQlierqSALANVLTGR--LAFHNTLRslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALA 167
Cdd:PRK13539 75 CHYLGHR-----NAMKPALTVAenLEFWAAFL------GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1393936756 168 QQPAIILADEPVASLDPATSVRVLGLLRDICKEDGItVIVSLHQ 211
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATHI 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-241 |
1.41e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSL-NRLVTPTGGSVTSELGelGSGSALRQHRRRTAMIFQHHQLIerqsala 105
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKGSGSVLLN--GMPIDAKEMRAISAYVQQDDLFI------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NVLTGR--LAFHNTLRslfpLPRAD-----QEIALSCLARVGLADKA------LSRVDKLSGGQQQRVGIARALAQQPAI 172
Cdd:TIGR00955 112 PTLTVRehLMFQAHLR----MPRRVtkkekRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQ--LEYARRFaDRVVGLADSQIVFDAAPSELTD 241
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpsSELFELF-DKIILMAEGRVAYLGSPDQAVP 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-250 |
1.64e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 6 IQDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHR 85
Cdd:PRK11614 1 MEKVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHQLIERQSALANVLTG-----RLAFHNTLRSLFPL-PRadqeialsclarvgLADKALSRVDKLSGGQQQR 159
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGgffaeRDQFQERIKWVYELfPR--------------LHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVF-DAAPSE 238
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLeDTGDAL 224
|
250
....*....|..
gi 1393936756 239 LTDAQLERIYAG 250
Cdd:PRK11614 225 LANEAVRSAYLG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-233 |
2.00e-17 |
|
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: 78.73 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 4 HPIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSelgelgsgsalrq 83
Cdd:cd03220 15 GGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAmifqhhqLIERQSALANVLTGRlafHNTLR--SLFPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRV 160
Cdd:cd03220 82 RGRVSS-------LLGLGGGFNPELTGR---ENIYLngRLLGLSRKEiDEKIDEIIEFSELGDFIDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSlHQLEYARRFADRVVGLADSQIVFD 233
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-242 |
2.44e-17 |
|
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: 81.30 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPG-GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSaLRQHRRRTA 89
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIFQHHQLIERQSAlANVLTGRLAfhntlrslfPLPRADQEIALSCLARVGLADKALSRVD--------KLSGGQQQRVG 161
Cdd:TIGR02203 410 LVSQDVVLFNDTIA-NNIAYGRTE---------QADRAEIERALAAAYAQDFVDKLPLGLDtpigengvLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTD 241
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 1393936756 242 A 242
Cdd:TIGR02203 557 R 557
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-223 |
2.77e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 2 MPH----PIQDaVLRVDRLSVVY---PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE--- 71
Cdd:PRK10261 1 MPHsdelDARD-VLAVENLNIAFmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkml 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 72 -------LGELGSGSALRQHRRR---TAMIFQhhqliERQSALANVLTGRLAFHNTLRSLFPLPRAD---QEIALSCLAR 138
Cdd:PRK10261 80 lrrrsrqVIELSEQSAAQMRHVRgadMAMIFQ-----EPMTSLNPVFTVGEQIAESIRLHQGASREEamvEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 139 VGLADKALSRV-DKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARR 217
Cdd:PRK10261 155 IPEAQTILSRYpHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
....*.
gi 1393936756 218 FADRVV 223
Cdd:PRK10261 235 IADRVL 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-231 |
3.97e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGS-ALRQHRRRtaMIFQ--HHQLIER 100
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDySYRSQRIR--MIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSaLANVLTGRLAFHNTLRslfplPRADQEIALSCLARVGL-ADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:PRK15112 104 QR-ISQILDFPLRLNTDLE-----PEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-230 |
4.74e-17 |
|
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: 76.70 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpggvtALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRR 87
Cdd:cd03215 2 EPVLEVRGLSVKG-----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMI---FQHHQLIERQSALANVLTGRLafhntlrslfplpradqeialsclarvgladkalsrvdkLSGGQQQRVGIAR 164
Cdd:cd03215 77 IAYVpedRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 165 ALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-239 |
5.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVY----PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRL-VTPTGGSVTSEL---GELGSGSALRQH 84
Cdd:PRK13645 9 LDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYaipANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQ--HHQL----IERQSALANVLTGrlafhntlrslfplprADQEIAL----SCLARVGLADKALSRVD-KLS 153
Cdd:PRK13645 89 RKEIGLVFQfpEYQLfqetIEKDIAFGPVNLG----------------ENKQEAYkkvpELLKLVQLPEDYVKRSPfELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
....*.
gi 1393936756 234 AAPSEL 239
Cdd:PRK13645 233 GSPFEI 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-231 |
6.30e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYP----------GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVtPTGGSVTSElgelgsGS 79
Cdd:PRK15134 275 LLDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFD------GQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 ALRQHRRRTAMIFQHHQLIERQ---SALANVLTGRLAFHNTLRSLFPLPRADQEIA--LSCLARVGLADKALSRV-DKLS 153
Cdd:PRK15134 348 PLHNLNRRQLLPVRHRIQVVFQdpnSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQqvIAVMEEVGLDPETRHRYpAEFS 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-250 |
7.18e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgelgsgsalRQHRRRTAMIF 92
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QHHQLIERQSALANVLTGR------LAFHNTLRSLFPLPRADQEI-------------------ALSCLARVGLADKALS 147
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDaelralEAELEELEAKLAEPDEDLERlaelqeefealggweaearAEEILSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 148 R-VDKLSGGQQQRVGIARALAQQPAIILADEPVASLDpATSVRVL-GLLRDickEDGITVIVSlHQleyaRRFADRVVGl 225
Cdd:COG0488 148 RpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEWLeEFLKN---YPGTVLVVS-HD----RYFLDRVAT- 217
|
250 260
....*....|....*....|....*
gi 1393936756 226 adsQIVfdaapsELTDAQLeRIYAG 250
Cdd:COG0488 218 ---RIL------ELDRGKL-TLYPG 232
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-230 |
8.39e-17 |
|
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: 79.70 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 2 MPHPIQDAVLRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSA 80
Cdd:TIGR01842 308 MPLPEPEGHLSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD------GAD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHRRRTamiFQHH-----QLIErqsalanVLTGRLAfHNTLRsLFPLPRADQEIALSCLARV-----GLADKALSRV- 149
Cdd:TIGR01842 382 LKQWDRET---FGKHigylpQDVE-------LFPGTVA-ENIAR-FGENADPEKIIEAAKLAGVhelilRLPDGYDTVIg 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 150 ---DKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEyARRFADRVVGLA 226
Cdd:TIGR01842 450 pggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQ 527
|
....
gi 1393936756 227 DSQI 230
Cdd:TIGR01842 528 DGRI 531
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-231 |
3.00e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 40 TVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGSGSALRQHRRRTAMIFQHHQLIERQSALANVLTGrlaFHN 116
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVlngRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG---MAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 117 TLRSLFplpraDQEIALsclarVGLaDKALSRVD-KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLR 195
Cdd:PRK11144 104 SMVAQF-----DKIVAL-----LGI-EPLLDRYPgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1393936756 196 DICKEDGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-236 |
4.16e-16 |
|
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: 78.13 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 16 LSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELGSGSALRQHRRRTAMIFQHH 95
Cdd:TIGR01257 935 VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL--VGGKDIETNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 96 QLIERQSALANVLtgrlaFHNTLRSlfplpRADQEIAL---SCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAI 172
Cdd:TIGR01257 1013 ILFHHLTVAEHIL-----FYAQLKG-----RSWEEAQLemeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 173 ILADEPVASLDPATSVRVLGLLrdICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAP 236
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-250 |
4.30e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTseLGELgSGSALRQHRR-- 86
Cdd:COG1137 2 MTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF--LDGE-DITHLPMHKRar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 -------RTAMIFQhhQLIERQSALAnVLtgrlafhntlrSLFPLPRADQEIAL-SCLARVGLADKALSRVDKLSGGQQQ 158
Cdd:COG1137 78 lgigylpQEASIFR--KLTVEDNILA-VL-----------ELRKLSKKEREERLeELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE 238
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
250
....*....|...
gi 1393936756 239 LT-DAQLERIYAG 250
Cdd:COG1137 223 ILnNPLVRKVYLG 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-243 |
4.53e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 16 LSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLrslNRLV--TPTGGSVT---SELGELgsgsALRQHRRRTAM 90
Cdd:PRK11174 355 LEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKingIELREL----DPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIErQSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLAD--KALS---------RVDKLSGGQQQR 159
Cdd:PRK11174 428 VGQNPQLPH-GTLRDNVLLGN-------------PDASDEQLQQALENAWVSEflPLLPqgldtpigdQAAGLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 160 VGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRFaDRVVGLADSQIVFDAAPSEL 239
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
....
gi 1393936756 240 TDAQ 243
Cdd:PRK11174 571 SQAG 574
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-246 |
6.86e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLierq 101
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKPEIYRQQVSYCAQTPTL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 saLANVLTGRLAFHNTLRSLFPlpraDQEIALSCLARVGLADKALS-RVDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:PRK10247 93 --FGDTVYDNLIFPWQIRNQQP----DPAIFLDDLERFALPDTILTkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 181 SLDPATSVRVLGLLRDICKEDGITVIVSLHQleyarrfADRvVGLADSQIVFDAAPSELTDAQLER 246
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHD-------KDE-INHADKVITLQPHAGEMQEARYEL 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-211 |
8.90e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 31 SIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgeLGSGSALRQHR--RRTAMIFQHHQlierqSALANVL 108
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV------LWQGEPIRRQRdeYHQDLLYLGHQ-----PGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TgrlAFHNtLRSLFPLPR-ADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIAR-ALAQQPAIILaDEPVASLDPAT 186
Cdd:PRK13538 90 T---ALEN-LRFYQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQG 164
|
170 180
....*....|....*....|....*
gi 1393936756 187 SVRVLGLLRDICKEDGItVIVSLHQ 211
Cdd:PRK13538 165 VARLEALLAQHAEQGGM-VILTTHQ 188
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-243 |
1.16e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALRQhrrrtamiFQHHQLiERQSALAN 106
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD------GVPLVQ--------YDHHYL-HRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 ---VLTGRLAFHNTLRSLFPLPRADQEIAlsclARVGLADKALSRVDK------------LSGGQQQRVGIARALAQQPA 171
Cdd:TIGR00958 562 qepVLFSGSVRENIAYGLTDTPDEEIMAA----AKAANAHDFIMEFPNgydtevgekgsqLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 172 IILADEPVASLDpatsVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTDAQ 243
Cdd:TIGR00958 638 VLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-206 |
1.22e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.57 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNrlvtptggsvtsELGELGSGSALRQHRRRTAM 90
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA------------GLWPWGSGRIGMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 IFQHHQLIerqsalanvlTGrlafhnTLRSLFPLPRADqeialsclarvgladkalsrvdKLSGGQQQRVGIARALAQQP 170
Cdd:cd03223 69 LPQRPYLP----------LG------TLREQLIYPWDD----------------------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 1393936756 171 AIILADEPVASLDPATsvrvLGLLRDICKEDGITVI 206
Cdd:cd03223 111 KFVFLDEATSALDEES----EDRLYQLLKELGITVI 142
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-223 |
1.33e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgELGSG--SALRQHRRRTAMIFQHHQL 97
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-----WIGGRvvNELEPADRDIAMVFQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IERQSALANvltgrLAFHNTLRSlfpLPRAdqEIAlsclARVGLADKALS-------RVDKLSGGQQQRVGIARALAQQP 170
Cdd:PRK11650 88 YPHMSVREN-----MAYGLKIRG---MPKA--EIE----ERVAEAARILEleplldrKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLH-QLEyARRFADRVV 223
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdQVE-AMTLADRVV 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-243 |
1.48e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQlierqsala 105
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN-NQAITDDNFEKLRKHIGIVFQNPD--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NVLTGRLAFHNTLRSL--FPLPRAD-QEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASL 182
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLenHAVPYDEmHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 183 DPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTDAQ 243
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-231 |
1.53e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLIE 99
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID-GTDIRTVTRASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 RqSALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLADKALSRVDK-----------LSGGQQQRVGIARALAQ 168
Cdd:PRK13657 423 R-SIEDNIRVGR-------------PDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLADSQIV 231
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-250 |
1.61e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTptggsVTSelGELGSGSALRQH----RRRTAMIFQHHQL 97
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED-----ITS--GDLFIGEKRMNDvppaERGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IERQSALANVLTG-RLAFHNtlrslfplpRADQEIALSCLARVGLADKALSRVDK-LSGGQQQRVGIARALAQQPAIILA 175
Cdd:PRK11000 87 YPHLSVAENMSFGlKLAGAK---------KEEINQRVNQVAEVLQLAHLLDRKPKaLSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEDGITVIVSLH-QLEyARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAG 250
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAG 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-250 |
2.03e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGsgs 79
Cdd:COG3845 250 PAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgEDITGLS--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 alRQHRRRTAMIF-----QHHQLIERQSALANVLTGRLAFHNTLRSLFPLPRADQEIALSCLARVGL-ADKALSRVDKLS 153
Cdd:COG3845 327 --PRERRRLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVrTPGPDTPARSLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 154 GGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
|
250
....*....|....*..
gi 1393936756 234 AAPSELTDAQLERIYAG 250
Cdd:COG3845 484 VPAAEATREEIGLLMAG 500
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-250 |
2.12e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGGvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRT 88
Cdd:PRK10895 2 ATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANvLTGRLAFHNTLRSLFPLPRADQeialsCLARVGLADKALSRVDKLSGGQQQRVGIARALAQ 168
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDN-LMAVLQIRDDLSAEQREDRANE-----LMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 169 QPAIILADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSE-LTDAQLERI 247
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEiLQDEHVKRV 233
|
...
gi 1393936756 248 YAG 250
Cdd:PRK10895 234 YLG 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-233 |
4.67e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLG------ElgsgsalRQHRRRTAMIF-QHHQ 96
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-LGyvpfkrR-------KEFARRIGVVFgQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 L------IErqsalanvlTGRLafhntLRSLFPLPRADQEIALSCLARV-GLADKALSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:COG4586 107 LwwdlpaID---------SFRL-----LKAIYRIPDAEYKKRLDELVELlDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 170 PAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFD 233
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-244 |
5.89e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVvyPGGVtalRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGS--- 79
Cdd:COG1129 249 AAAPGEVVLEVEGLSV--GGVV---RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 ALRQH-------RRRTAmifqhhqLIERQSALANVLtgrLAFHNTLRSLFPL-PRADQEIALSCLARVGLadKALS---R 148
Cdd:COG1129 324 AIRAGiayvpedRKGEG-------LVLDLSIRENIT---LASLDRLSRGGLLdRRRERALAEEYIKRLRI--KTPSpeqP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 149 VDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADS 228
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREG 470
|
250
....*....|....*.
gi 1393936756 229 QIVFDAAPSELTDAQL 244
Cdd:COG1129 471 RIVGELDREEATEEAI 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-232 |
6.05e-15 |
|
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: 71.52 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNrLVTPTGGSVTSEL--GELGSGSALRQHRRRTAMIFQHHqlierqsal 104
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA-NRTEGNVSVEGDIhyNGIPYKEFAEKYPGEIIYVSEED--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 105 anvltgrlaFHN---TLRSLFplpradqEIALSClarvgladKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:cd03233 93 ---------VHFptlTVRETL-------DFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 182 LDPATSVRVLGLLRDICKEDGITVIVSLHQ--LEYARRFaDRVVGLADSQIVF 232
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFVSLYQasDEIYDLF-DKVLVLYEGRQIY 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-211 |
6.26e-15 |
|
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: 71.37 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelGSGSALRQHRRRTAMIFQHHQlierq 101
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN----GGPLDFQRDSIARGLLYLGHA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 salaNVLTGRLAFHNTLRslFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:cd03231 82 ----PGIKTTLSVLENLR--FWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 1393936756 182 LDPATSVRVLGLLRDICKEDGItVIVSLHQ 211
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGM-VVLTTHQ 184
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-242 |
3.13e-14 |
|
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: 70.51 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 34 FRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGsgsalrqhrrrtamiFQHHQLIERQSAlanvlTGRLA 113
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------------YKPQYIKADYEG-----TVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 114 FHNTLRSLFPLPRADQEIAlSCLARVGLADkalSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGL 193
Cdd:cd03237 82 LSSITKDFYTHPYFKTEIA-KPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1393936756 194 LRDICKEDGITVIVSLHQLEYARRFADRVvgladsqIVFDAAPSELTDA 242
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRL-------IVFEGEPSVNGVA 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-225 |
4.79e-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: 69.42 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYPG--GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgeLGSGSALRQH- 84
Cdd:cd03248 9 KGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV------LLDGKPISQYe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 ----RRRTAMIFQHHQLIERqSALANVLTGrLAFHNTLRSLFPLPRADQEIALSCLARvGLADKALSRVDKLSGGQQQRV 160
Cdd:cd03248 83 hkylHSKVSLVGQEPVLFAR-SLQDNIAYG-LQSCSFECVKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDiCKEDGiTVIVSLHQLEYARRfADRVVGL 225
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERR-TVLVIAHRLSTVER-ADQILVL 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-239 |
6.88e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.60 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlVTPTGGSVTSELGELGSGSALR---QHRRR-----TAMIFQ 93
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRlspRERRKlvghnVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 94 H------------HQLIerQSALANVLTGRL--AFHNTLRSlfplpradqeiALSCLARVGLAD-KALSRV--DKLSGGQ 156
Cdd:PRK15093 97 EpqscldpservgRQLM--QNIPGWTYKGRWwqRFGWRKRR-----------AIELLHRVGIKDhKDAMRSfpYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAP 236
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
...
gi 1393936756 237 SEL 239
Cdd:PRK15093 244 KEL 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-244 |
1.53e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAMIFQHHQLIERQ 101
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTGrlafhntlrslFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:PRK15439 102 SVKENILFG-----------LPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 182 LDPATSVRVLGLLRDICKEDGITVIVSlHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQL 244
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQGVGIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-224 |
4.04e-13 |
|
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: 68.81 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 14 DRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTggsvtselgelgSGSALRQHRRRTAMIFQ 93
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF------------NGEARPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 94 HHQLIERQSALANVLTG------RLAFHNTLRSLFPLPRAD-----------QEIALSCLA-----RVGLADKAL----- 146
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGvaeikdALDRFNEISAKYAEPDADfdklaaeqaelQEIIDAADAwdldsQLEIAMDALrcppw 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 147 -SRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDpATSVrvlGLLRDICKEDGITVIVSLHQleyaRRFADRVVG 224
Cdd:TIGR03719 156 dADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESV---AWLERHLQEYPGTVVAVTHD----RYFLDNVAG 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-227 |
1.11e-12 |
|
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: 65.43 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRS-LNRLVTPTGGSVTSELGELGSGSALRQHRRRTAMIFQHHQLIERQ 101
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAiLGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTGRLAFhNTLR--------SLFP----LPRADQeialsclARVGladkalSRVDKLSGGQQQRVGIARALAQQ 169
Cdd:cd03290 93 ATVEENITFGSPF-NKQRykavtdacSLQPdidlLPFGDQ-------TEIG------ERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 170 PAIILADEPVASLDPATSVRVL--GLLRdICKEDGITVIVSLHQLEYARRfADRVVGLAD 227
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMqeGILK-FLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-236 |
1.93e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.74 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVY-PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHR 85
Cdd:cd03369 3 EHGEIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-GIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 86 RRTAMIFQHHQLierqsalanvltgrlaFHNTLRS-LFPLPR-ADQEI--ALScLARVGLadkalsrvdKLSGGQQQRVG 161
Cdd:cd03369 82 SSLTIIPQDPTL----------------FSGTIRSnLDPFDEySDEEIygALR-VSEGGL---------NLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 162 IARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRFaDRVVGLADSQIVFDAAP 236
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-268 |
2.44e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAMIFQHHQLIERQS 102
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANVLTGRLAfhntLRSLF----PLPRADQEIalscLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PRK10982 90 VMDNMWLGRYP----TKGMFvdqdKMYRDTKAI----FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 179 VASLdpaTSVRVLGLLRDI--CKEDGITVIVSLHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAGRSTTQ- 255
Cdd:PRK10982 162 TSSL---TEKEVNHLFTIIrkLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQr 238
|
250
....*....|....*.
gi 1393936756 256 ---PANTPAEppVMLE 268
Cdd:PRK10982 239 fpdKENKPGE--VILE 252
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-231 |
8.04e-12 |
|
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: 64.84 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 5 PIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsGSALR-- 82
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID------GQDIRdv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 -QH--RRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS--LFPLPRADQE--IALSCLARV-----GLADKALSRVD 150
Cdd:COG5265 426 tQAslRAAIGIVPQDTVL----------------FNDTIAYniAYGRPDASEEevEAAARAAQIhdfieSLPDGYDTRVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 ----KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQLEYARRfADRVVGLA 226
Cdd:COG5265 490 erglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLE 566
|
....*
gi 1393936756 227 DSQIV 231
Cdd:COG5265 567 AGRIV 571
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-238 |
1.07e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlVTPTGGSVTS--------ELGELgSGSALRQ-HRRRTAMIF 92
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTAdrfrwngiDLLKL-SPRERRKiIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QH------------HQLIErqSALANVLTGRLafhntlrslFPLPRADQEIALSCLARVGLAD-KAL--SRVDKLSGGQQ 157
Cdd:COG4170 96 QEpsscldpsakigDQLIE--AIPSWTFKGKW---------WQRFKWRKKRAIELLHRVGIKDhKDImnSYPHELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 158 QRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGLADSQIVfDAAPS 237
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV-ESGPT 243
|
.
gi 1393936756 238 E 238
Cdd:COG4170 244 E 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-222 |
1.23e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.03 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgeLGSGSALRQhrrrT 88
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT-----VAGKSILTN----I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 89 AMIFQHHQLIERQSALANVLTGR--LAFHNTLRSLfplPRADQE-IALSCLARVGLADKALSRVDKLSGGQQQRVGIARA 165
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGRehLYLYARLRGV---PAEEIEkVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 166 LAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRV 222
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRL 2140
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
27-225 |
2.26e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTggsvtselgelgSGSALRQHRRRTAMIFQhhqlierqsalan 106
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD------------EGVIKRNGKLRIGYVPQ------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 vltgRLAFHNTL-----RSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:PRK09544 75 ----KLYLDTTLpltvnRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1393936756 182 LDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVVGL 225
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-211 |
3.65e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 37 GEFTVLLGLSGAGKSTLLRSL-NRLvtpTGGSVTselgelgsGSALRQHRRRTAMIFQHHQLIERQSALANVLTGR--LA 113
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALaGRI---QGNNFT--------GTILANNRKPTKQILKRTGFVTQDDILYPHLTVRetLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 114 FHNTLRSLFPLPRADQ-EIALSCLARVGLAD-----KALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATS 187
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKiLVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....
gi 1393936756 188 VRVLGLLRDICKEdGITVIVSLHQ 211
Cdd:PLN03211 243 YRLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-222 |
4.73e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYP---GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTP---TGGSVTSELGELGSGSA 80
Cdd:PRK09473 9 ADALLDVKDLRVTFStpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 81 LRQHRRRT---AMIFQH------------HQLIERQsALANVLTGRLAFHNTLRSL--FPLPRADQEIALSclarvglad 143
Cdd:PRK09473 89 KELNKLRAeqiSMIFQDpmtslnpymrvgEQLMEVL-MLHKGMSKAEAFEESVRMLdaVKMPEARKRMKMY--------- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 144 kalsrVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRV 222
Cdd:PRK09473 159 -----PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-230 |
4.78e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVvypggvTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSAlrQHRRRTA 89
Cdd:PRK15439 268 VLTVEDLTG------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST--AQRLARG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 90 MIF-----QHHQLIERQSALANVLTgrLAFHNtlRSLFPLPRADQEIALSCLARVGL----ADKAlsrVDKLSGGQQQRV 160
Cdd:PRK15439 340 LVYlpedrQSSGLYLDAPLAWNVCA--LTHNR--RGFWIKPARENAVLERYRRALNIkfnhAEQA---ARTLSGGNQQKV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 161 GIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKeDGITVIVSLHQLEYARRFADRVVGLADSQI 230
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-211 |
6.46e-11 |
|
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: 59.95 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSL-NRlvtPTGGSVTSELgeLGSGSALRQHRRRTAmifqhhQLIERQSALA 105
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVITGEI--LINGRPLDKNFQRST------GYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NVLTGR--LAFHNTLRSlfplpradqeialsclarvgladkalsrvdkLSGGQQQRVGIARALAQQPAIILADEPVASLD 183
Cdd:cd03232 92 PNLTVReaLRFSALLRG-------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*...
gi 1393936756 184 PATSVRVLGLLRDICkEDGITVIVSLHQ 211
Cdd:cd03232 141 SQAAYNIVRFLKKLA-DSGQAILCTIHQ 167
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-232 |
7.92e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsgsalrqhrRRTAMIFQhhqlierQSALAN 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQ-------QAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 -VLTGRLAFHNTLRS--LFPLPRADQ-EIALSCLARvGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASL 182
Cdd:PTZ00243 735 aTVRGNILFFDEEDAarLADAVRVSQlEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1393936756 183 DPATSVRV-----LGLLRdickedGITVIVSLHQLEYARRfADRVVGLADSQIVF 232
Cdd:PTZ00243 814 DAHVGERVveecfLGALA------GKTRVLATHQVHVVPR-ADYVVALGDGRVEF 861
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-251 |
9.76e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtSELGELGSGSALRQHRRR-TAMIFQHHQLIERQ 101
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI-LYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVLTGRlAFHNTLRSLfPLPRADQEiALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:PRK10762 95 TIAENIFLGR-EFVNRFGRI-DWKKMYAE-ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 182 L-DPATS--VRVLGLLRDicKEDGItVIVSlHQLEYARRFADRVVGLADSQIVFDAAPSELTDAQLERIYAGR 251
Cdd:PRK10762 172 LtDTETEslFRVIRELKS--QGRGI-VYIS-HRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-244 |
1.30e-10 |
|
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: 61.38 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPGGVTALR--DTSIAFRRGEFTVLLGLSGAGKSTLLRSL-NRLVTPTGGSVTSELGELGSGS 79
Cdd:TIGR02633 250 PHEIGDVILEARNLTCWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 ALRQHRRRTAMIFQHHQlieRQSALANVLTGRLAFHNTLRSLFPLPRADQEIALSCLARV--GLADKALS---RVDKLSG 154
Cdd:TIGR02633 330 PAQAIRAGIAMVPEDRK---RHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAiqRLKVKTASpflPIGRLSG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 155 GQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIVFDA 234
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDF 485
|
250
....*....|
gi 1393936756 235 APSELTDAQL 244
Cdd:TIGR02633 486 VNHALTQEQV 495
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-223 |
2.19e-10 |
|
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: 57.46 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVTaLRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSelgelgsGSALRqhrrrtam 90
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------GSTVK-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 91 ifqhhqlierqsalanvltgrlafhntlrslfplpradqeialsclarvgladkaLSRVDKLSGGQQQRVGIARALAQQP 170
Cdd:cd03221 65 -------------------------------------------------------IGYFEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 171 AIILADEPVASLDPATSVRVLGLLRDickEDGITVIVSlHQleyaRRFADRVV 223
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKE---YPGTVILVS-HD----RYFLDQVA 134
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-212 |
2.34e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 5 PIQDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELgSGSAL 81
Cdd:PRK10790 335 PLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgRPLSSL-SHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHrrrTAMIfQHHQLIERQSALANVLTGR-LAFHNTLRSLfplpradQEIALSCLARvGLADKALSRV----DKLSGGQ 156
Cdd:PRK10790 414 RQG---VAMV-QQDPVVLADTFLANVTLGRdISEEQVWQAL-------ETVQLAELAR-SLPDGLYTPLgeqgNNLSVGQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdgITVIVSLHQL 212
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRL 535
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-213 |
3.20e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 60.69 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVY-PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTpTGGSVTSElGELGSGSALRQHRRRTAMI 91
Cdd:TIGR01271 1220 VQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-GVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQHhqlierqsalANVLTGrlafhnTLR-SLFPLPR-ADQEIaLSCLARVGLADKALSRVDKL-----------SGGQQQ 158
Cdd:TIGR01271 1298 PQK----------VFIFSG------TFRkNLDPYEQwSDEEI-WKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQ 1360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATsvrvLGLLRDICKE--DGITVIVSLHQLE 213
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVT----LQIIRKTLKQsfSNCTVILSEHRVE 1413
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-239 |
4.66e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 9 AVLRVDRLSVVYPGGVTALRDT---SIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSG-SALRQH 84
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDlQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRR------TAMIFQH------------HQLIErqsALANVLTGRlafhntlrslfplPRADQEIALSCLARVGLADKAl 146
Cdd:PRK11022 82 ERRnlvgaeVAMIFQDpmtslnpcytvgFQIME---AIKVHQGGN-------------KKTRRQRAIDLLNQVGIPDPA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 147 SRVD----KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRV 222
Cdd:PRK11022 145 SRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
250
....*....|....*..
gi 1393936756 223 VGLADSQIVFDAAPSEL 239
Cdd:PRK11022 225 IVMYAGQVVETGKAHDI 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-240 |
5.81e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLIE 99
Cdd:PRK10522 332 YQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD-GKPVTAEQPEDYRKLFSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 RqsalanvLTGRLAFhntlrslfplpRADQEIALSCLARVGLADKaLSRVD------KLSGGQQQRVGIARALAQQPAII 173
Cdd:PRK10522 411 Q-------LLGPEGK-----------PANPALVEKWLERLKMAHK-LELEDgrisnlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 174 LADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVVGLADSQIvfdaapSELT 240
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL------SELT 531
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2-211 |
6.82e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 2 MPHPIQDAVLRVDRLSVvypggvtaLRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRlvTPTGGSVTSELGELGSGSAL 81
Cdd:PLN03140 879 MPAEMKEQGVTEDRLQL--------LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQ 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRTAMIFQH--H--QLIERQSalanvltgrLAFHNTLRslfpLPR----------ADQEIALSCLARVGLADKALS 147
Cdd:PLN03140 949 ETFARISGYCEQNdiHspQVTVRES---------LIYSAFLR----LPKevskeekmmfVDEVMELVELDNLKDAIVGLP 1015
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 148 RVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQ 211
Cdd:PLN03140 1016 GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQ 1078
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-212 |
6.94e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 5 PIQDAVLRVDRLSVVYPGG-VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgelgsgsalRQ 83
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-------------RF 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIfqhhQLIERQSALANVLTGRLAFHNTLRSLFPLPRAD---QEI-ALSCLARV---------GLADKALSRVD 150
Cdd:PRK10789 375 HDIPLTKL----QLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDatqQEIeHVARLASVhddilrlpqGYDTEVGERGV 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 151 KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKedGITVIVSLHQL 212
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRL 510
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-207 |
1.17e-09 |
|
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: 58.64 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELG-----ELGSGSALRQHRR-------RTAMIFQHHQLIERqs 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlKRFRGTELQDYFKklangeiKVAHKPQYVDLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 alanVLTGrlafhnTLRSLfpLPRADQEIALSCLA-RVGLaDKALSR-VDKLSGGQQQRVGIARALAQQPAIILADEPVA 180
Cdd:COG1245 175 ----VFKG------TVREL--LEKVDERGKLDELAeKLGL-ENILDRdISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180
....*....|....*....|....*..
gi 1393936756 181 SLDPATSVRVLGLLRDICKEDGITVIV 207
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVV 268
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-247 |
1.28e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.49 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 11 LRVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgeLGSGSALRQH----- 84
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI------LLDGHDLRDYtlasl 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQHHQLIerQSALANvltgRLAFHNTLRslfpLPRADQEIAlsclARVGLADKALSRVDK------------L 152
Cdd:PRK11176 416 RNQVALVSQNVHLF--NDTIAN----NIAYARTEQ----YSREQIEEA----ARMAYAMDFINKMDNgldtvigengvlL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 153 SGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDgiTVIVSLHQLEYARRfADRVVGLADSQIVF 232
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
250 260
....*....|....*....|
gi 1393936756 233 DAAPSELTD-----AQLERI 247
Cdd:PRK11176 559 RGTHAELLAqngvyAQLHKM 578
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-223 |
1.78e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 28 RDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSV---------TSELGELGSGSALRQHRRRTAMIFqHHQLI 98
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdispRSPLDAVKKGMAYITESRRDNGFF-PNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 ERQSALANVLtgRLAFHNTLRSLFPlPRADQEIALSclARVGLADKALS---RVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:PRK09700 359 AQNMAISRSL--KDGGYKGAMGLFH-EVDEQRTAEN--QRELLALKCHSvnqNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVV 223
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIA 480
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-231 |
2.49e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.23 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 19 VYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSL--NRLVTPTGGSVTSElGElgSGSALRQHRRRTA---MIFQ 93
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLD-GE--DILELSPDERARAgifLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 94 HHQLIERQSaLANVLtgRLAfHNTLRSLFPLPRADQEIALSCLARVGLADKALSR-VD-KLSGGQQQRVGIARALAQQPA 171
Cdd:COG0396 85 YPVEIPGVS-VSNFL--RTA-LNARRGEELSAREFLKLLKEKMKELGLDEDFLDRyVNeGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 172 IILADEPVASLDpatsVRVLGLLRDIC---KEDGITVIVSLHQ---LEYARrfADRVVGLADSQIV 231
Cdd:COG0396 161 LAILDETDSGLD----IDALRIVAEGVnklRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIV 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
126-239 |
3.41e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 126 RADQeialsCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKeDGITV 205
Cdd:NF000106 124 RADE-----LLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATV 197
|
90 100 110
....*....|....*....|....*....|....
gi 1393936756 206 IVSLHQLEYARRFADRVVGLADSQIVFDAAPSEL 239
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-184 |
4.33e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 37 GEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtselgELGSGSALRQHRRRTAMIFQH-HQLIERQSALANvltgrLAFH 115
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSRFMAYLGHlPGLKADLSTLEN-----LHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 116 NTLRSlfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDP 184
Cdd:PRK13543 107 CGLHG-----RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-188 |
5.22e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 15 RLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGelgsgsalrqhrRRTAMIFQH 94
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG------------IKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 95 HQLIERQSALANVLTG------RLAFHNTLRSLFPLPRAD-----------QEIALSCLA-----RVGLADKAL------ 146
Cdd:PRK11819 79 PQLDPEKTVRENVEEGvaevkaALDRFNEIYAAYAEPDADfdalaaeqgelQEIIDAADAwdldsQLEIAMDALrcppwd 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1393936756 147 SRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDpATSV 188
Cdd:PRK11819 159 AKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESV 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-223 |
8.14e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 8.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRfADRVV 223
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIV 1429
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-185 |
1.18e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPGGVT-ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSgSAL 81
Cdd:PTZ00243 1301 PHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-YGL 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 82 RQHRRRTAMIFQHHQLierqsalanvltgrlaFHNTLRS-LFPLPRADQEIALSCLARVGLADKAL-------SRV---- 149
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVL----------------FDGTVRQnVDPFLEASSAEVWAALELVGLRERVAsesegidSRVlegg 1443
|
170 180 190
....*....|....*....|....*....|....*..
gi 1393936756 150 DKLSGGQQQRVGIARALAQQ-PAIILADEPVASLDPA 185
Cdd:PTZ00243 1444 SNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPA 1480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-212 |
1.32e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELG-----ELGSGSALRQHRRRTA----MIFQHHQLIErqsALA 105
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlKRFRGTELQNYFKKLYngeiKVVHKPQYVD---LIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 106 NVLTGrlafhnTLRSLfpLPRADQEIALSCLA-RVGLaDKALSR-VDKLSGGQQQRVGIARALAQQPAIILADEPVASLD 183
Cdd:PRK13409 174 KVFKG------KVREL--LKKVDERGKLDEVVeRLGL-ENILDRdISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 1393936756 184 PATSVRVLGLLRDICKedGITVIVSLHQL 212
Cdd:PRK13409 245 IRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-223 |
1.45e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 19 VYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLrslnrlvtptggsvtselgelgsgsalrqhrrrtamifqhhqli 98
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 99 erQSALANVLTGRLAFHNTLRSLFPLPRADQeiaLSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQQP--AIILA 175
Cdd:cd03238 39 --NEGLYASGKARLISFLPKFSRNKLIFIDQ---LQFLIDVGLGYLTLGQkLSTLSGGELQRVKLASELFSEPpgTLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRfADRVV 223
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWII 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-229 |
1.51e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT----------------SELGELGSGSALRQHRRR 87
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlkwwrSKIGVVSQDPLLFSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 88 TAMIFQHHQLIE---------------------RQSALANVLTGRLAFHNTLRS--LFPLPRADQEIALSCLARV----- 139
Cdd:PTZ00265 478 NNIKYSLYSLKDlealsnyynedgndsqenknkRNSCRAKCAGDLNDMSNTTDSneLIEMRKNYQTIKDSEVVDVskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 140 ------GLADK----ALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDI-CKEDGITVIVS 208
Cdd:PTZ00265 558 ihdfvsALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
|
250 260
....*....|....*....|.
gi 1393936756 209 lHQLEYArRFADRVVGLADSQ 229
Cdd:PTZ00265 638 -HRLSTI-RYANTIFVLSNRE 656
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-232 |
2.39e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 24 VTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELGELGSGSALRQHRRRTAMIFqhhqlierqSA 103
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVY---------NA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 104 LANVLTGRLAFHNTL----RSLFPLPRA---DQEIALSCLARVGLADKALSR----------VDKLSGGQQQRVGIARAL 166
Cdd:TIGR00956 145 ETDVHFPHLTVGETLdfaaRCKTPQNRPdgvSREEYAKHIADVYMATYGLSHtrntkvgndfVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 167 AQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQL-EYARRFADRVVGLADSQIVF 232
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIY 291
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-258 |
3.89e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 21 PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---SELGELGsgsaLRQHRRRTAMIFQHHQL 97
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMiddCDVAKFG----LTDLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 98 IerqSALANVLTGRLAFHNTLRSLFPLPRADQEIALScLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADE 177
Cdd:PLN03232 1322 F---SGTVRFNIDPFSEHNDADLWEALERAHIKDVID-RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 178 PVASLDpatsVRVLGLLRDICKED--GITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTDAQLERIYAGRSTTQ 255
Cdd:PLN03232 1398 ATASVD----VRTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
...
gi 1393936756 256 PAN 258
Cdd:PLN03232 1473 PAN 1475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-236 |
7.26e-08 |
|
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: 52.86 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELgelgsgsalrqhrrrtaMIFQHHQLIER------QSALANVL 108
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL-----------------KISYKPQYISPdydgtvEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TGRL--AFHNTlrslfplpradqEIAlsclARVGLaDKAL-SRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPA 185
Cdd:COG1245 427 TDDFgsSYYKT------------EII----KPLGL-EKLLdKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 186 TSVRVLGLLRDICKEDGITVIVSLHQL---EYarrfadrvvgLADSQIVFDAAP 236
Cdd:COG1245 490 QRLAVAKAIRRFAENRGKTAMVVDHDIyliDY----------ISDRLMVFEGEP 533
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-212 |
7.54e-08 |
|
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: 51.98 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLnrlvtptGGSVTSELGELGSGSALRQhrrrtamIFQHHQLIERQSALANVLTGRL-- 112
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPDWDE-------ILDEFRGSELQNYFTKLLEGDVkv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 113 ------------AFHNTLRSLfpLPRADQEIALSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQQPAIILADEPV 179
Cdd:cd03236 90 ivkpqyvdlipkAVKGKVGEL--LKKKDERGKLDELVDQLELRHVLDRnIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 1393936756 180 ASLDPATSVRVLGLLRDICKEDGiTVIVSLHQL 212
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDN-YVLVVEHDL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-237 |
8.63e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 35 RRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSELgelgsgsalrqhrrrtaMIFQHHQLIER------QSALANVl 108
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-----------------KISYKPQYIKPdydgtvEDLLRSI- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TGRLA--FHNTlrslfplpradqEIAlsclARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPAT 186
Cdd:PRK13409 425 TDDLGssYYKS------------EII----KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1393936756 187 SVRVLGLLRDICKEDGITVIVSLHQL---EYarrfadrvvgLADSQIVFDAAPS 237
Cdd:PRK13409 489 RLAVAKAIRRIAEEREATALVVDHDIymiDY----------ISDRLMVFEGEPG 532
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
27-210 |
9.32e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 52.31 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGeFTVLLGLSGAGKSTLLRSLNRLVTPTGG-SVTSE---LGELGS----------GSALRQHRRRTAMIF 92
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEdfyLGDDPDlpeieieltfGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 93 QHHQLIERQSALANVLTGRL-AFHNTLRSLFPLPRADQEIALSC----------LARVGLADKALSRVDKLSGGQQQRVG 161
Cdd:COG3593 93 DKEELEEALEELNEELKEALkALNELLSEYLKELLDGLDLELELsldeledllkSLSLRIEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 162 IA--RALAQ-----QPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLH 210
Cdd:COG3593 173 LAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTH 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-213 |
1.87e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.01 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 13 VDRLSVVY-PGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTpTGGSVTSElGELGSGSALRQHRRRTAMI 91
Cdd:cd03289 5 VKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID-GVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 FQHhqlierqsalanvltgRLAFHNTLR-SLFPLPR-ADQEIaLSCLARVGLA---DKALSRVD--------KLSGGQQQ 158
Cdd:cd03289 83 PQK----------------VFIFSGTFRkNLDPYGKwSDEEI-WKVAEEVGLKsviEQFPGQLDfvlvdggcVLSHGHKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATSvrvlGLLRDICKE--DGITVIVSLHQLE 213
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITY----QVIRKTLKQafADCTVILSEHRIE 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-225 |
2.28e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE---------------------------LGELGSgs 79
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnvegtvydfvaegIEEQAE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 80 ALRQHRR--RTAMIFQHHQLIERQSALANVLTgrlafHNTLRSLfplpraDQEIAlSCLARVGL-ADKALSrvdKLSGGQ 156
Cdd:PRK11147 97 YLKRYHDisHLVETDPSEKNLNELAKLQEQLD-----HHNLWQL------ENRIN-EVLAQLGLdPDAALS---SLSGGW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIckeDGITVIVSlHQLEYARRFADRVVGL 225
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFIS-HDRSFIRNMATRIVDL 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-244 |
2.58e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVvyPGgvtaLR-DTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---------SEL 72
Cdd:PRK11288 250 PRPLGEVRLRLDGLKG--PG----LRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidirSPR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 73 GELGSGSALRQHRRRTAMIFQHHQLIERQ--SALANVLTGRLAFHNtlrslfplpRADQEIALSCLARvgLADKALSR-- 148
Cdd:PRK11288 324 DAIRAGIMLCPEDRKAEGIIPVHSVADNIniSARRHHLRAGCLINN---------RWEAENADRFIRS--LNIKTPSReq 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 149 -VDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICkEDGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:PRK11288 393 lIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
250
....*....|....*..
gi 1393936756 228 SQIVFDAAPSELTDAQL 244
Cdd:PRK11288 472 GRIAGELAREQATERQA 488
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-183 |
3.17e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 20 YPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTggsvtselgelgSGSALRQHRRRTAMIFQHHqlie 99
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPS------------SGTVFRSAKVRMAVFSQHH---- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 100 rqsalanVLTGRLAFHNTLRSLFPLPRADQEIALSCLARVGLA-DKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:PLN03073 582 -------VDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
....*
gi 1393936756 179 VASLD 183
Cdd:PLN03073 655 SNHLD 659
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-246 |
3.66e-07 |
|
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: 49.45 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 19 VYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSL--NRLVTPTGGSVTselgelgsgsalrqhrrrtamiFQHHQ 96
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEIL----------------------FKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 LI-----ERqsALANVLtgrLAFHNtlrslfplPRADQEIALSCLAR-VGladkalsrvDKLSGGQQQRVGIARALAQQP 170
Cdd:cd03217 66 ITdlppeER--ARLGIF---LAFQY--------PPEIPGVKNADFLRyVN---------EGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 171 AIILADEPVASLDpATSVRVLGLLRDICKEDGITVIVSLHQ---LEYARrfADRVVGLADSQIVfDAAPSELTDaQLER 246
Cdd:cd03217 124 DLAILDEPDSGLD-IDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIV-KSGDKELAL-EIEK 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-243 |
8.96e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYPG--GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtpTG-------GSVTSELG 73
Cdd:PRK13549 252 PHTIGEVILEVRNLTAWDPVnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL------FGaypgrweGEIFIDGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 74 ELGSGSALRQHRRRTAMI---FQHHQLIERQSALANVLT---GRLAFHNTLRSLFPLPRADQEIALsclARVGLADKALs 147
Cdd:PRK13549 326 PVKIRNPQQAIAQGIAMVpedRKRDGIVPVMGVGKNITLaalDRFTGGSRIDDAAELKTILESIQR---LKVKTASPEL- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 148 RVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLAD 227
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHE 480
|
250
....*....|....*.
gi 1393936756 228 SQIVFDAAPSELTDAQ 243
Cdd:PRK13549 481 GKLKGDLINHNLTQEQ 496
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
151-242 |
1.56e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 151 KLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKEDGITVIVSLHQLEYARRFADRVvgladsqI 230
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI-------H 143
|
90
....*....|..
gi 1393936756 231 VFDAAPSELTDA 242
Cdd:cd03222 144 VFEGEPGVYGIA 155
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-239 |
1.57e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 10 VLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLL------RSLNRlvtptgGSVTSelgeLGSGSALRQ 83
Cdd:NF033858 1 VARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQQ------GRVEV----LGGDMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRtamifqhhqlierqsalanvLTGRLAF------HN---TL----------RsLFPLPRA--DQEIAlSCLARVGLA 142
Cdd:NF033858 70 HRRA--------------------VCPRIAYmpqglgKNlypTLsvfenldffgR-LFGQDAAerRRRID-ELLRATGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 143 DKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDICKE-DGITVIVSLHQLEYARRFaDR 221
Cdd:NF033858 128 PFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErPGMSVLVATAYMEEAERF-DW 206
|
250
....*....|....*...
gi 1393936756 222 VVGLADSQIVFDAAPSEL 239
Cdd:NF033858 207 LVAMDAGRVLATGTPAEL 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-211 |
1.64e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 34 FRRGEFTVLLGLSGAGKSTLLRSLNRLVtpTGGSVTSelGELGSGSALRQH--RRRTAMIFQH--H--QLIERQSalanv 107
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITG--GDRLVNGRPLDSsfQRSIGYVQQQdlHlpTSTVRES----- 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 108 ltgrLAFHNTLRSLFPLPRA------DQEIALSCL-----ARVGLADKALSrVDklsggQQQRVGIARALAQQPAIIL-A 175
Cdd:TIGR00956 857 ----LRFSAYLRQPKSVSKSekmeyvEEVIKLLEMesyadAVVGVPGEGLN-VE-----QRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....*.
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQ 211
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQ 961
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-232 |
2.49e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 36 RGEFTVLLGLSGAGKSTLLRslnrLVT---PTGGS--VTSELGELGSGSALRQHRRRTAMIFQHHQLIERQSA-LANV-L 108
Cdd:PRK10938 285 PGEHWQIVGPNGAGKSTLLS----LITgdhPQGYSndLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTsVRNViL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 109 TGrlaFHNTLRSLFPLPRADQEIALSCLARVGLADK-ALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPats 187
Cdd:PRK10938 361 SG---FFDSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP--- 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1393936756 188 vrvlgLLRdickedgitvivslhQLeyARRFADRVVGLADSQIVF 232
Cdd:PRK10938 435 -----LNR---------------QL--VRRFVDVLISEGETQLLF 457
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-208 |
3.10e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 26 ALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT---------SELGELGSGSALRQHRRRTAMIFQHHQ 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlhgkkinnhNANEAINHGFALVTEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 97 lIERQSALANV--LTGRLAFHNTLRSlfplpRADQEIALSCLaRVGLADKAlSRVDKLSGGQQQRVGIARALAQQPAIIL 174
Cdd:PRK10982 343 -IGFNSLISNIrnYKNKVGLLDNSRM-----KSDTQWVIDSM-RVKTPGHR-TQIGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190
....*....|....*....|....*....|....*
gi 1393936756 175 ADEPVASLDPATSVRVLGLLRDICKED-GITVIVS 208
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKKDkGIIIISS 449
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-242 |
3.99e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.49 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 31 SIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElGELGSGSALRQHRRRTAMIFQHHQLIERqsalanvLTG 110
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTADNREAYRQLFSAVFSDFHLFDR-------LLG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 111 rlafhntlrslfPLPRADQEIALSCLARVGLADK------ALSRVDkLSGGQQQRVGIARALAQQPAIILADEPVASLDP 184
Cdd:COG4615 424 ------------LDGEADPARARELLERLELDHKvsvedgRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 185 AtsVR------VLGLLrdicKEDGITVIVSLHQLEYarrF--ADRVVGLADSQIVFDAAPSELTDA 242
Cdd:COG4615 491 E--FRrvfyteLLPEL----KARGKTVIAISHDDRY---FdlADRVLKMDYGKLVELTGPAALAAS 547
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-243 |
4.89e-06 |
|
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: 47.63 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSE---LGELGsgsaLRQHRRRTAMIFQHHQLierqsa 103
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglnIAKIG----LHDLRFKITIIPQDPVL------ 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 104 lanvltgrlaFHNTLR-SLFPLPRADQEIALSCLARVGLADKALSRVDKL-----------SGGQQQRVGIARALAQQPA 171
Cdd:TIGR00957 1372 ----------FSGSLRmNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393936756 172 IILADEPVASLDPATSVRVLGLLRdiCKEDGITVIVSLHQLEYARRFAdRVVGLADSQIVFDAAPSELTDAQ 243
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQR 1510
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-243 |
5.52e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 23 GVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtptggsvtseLGELGSGSALRQHRRRTAMIFQHhQLIERQS 102
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--------------MGELEPSEGKIKHSGRISFSPQT-SWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 103 ALANVLTGRLAFHNTLRSLFPLPRADQEIA-LSCLARVGLADKALSrvdkLSGGQQQRVGIARALAQQPAIILADEPVAS 181
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRYTSVIKACQLEEDIAlFPEKDKTVLGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1393936756 182 LDPATSVRVLGllRDICK-EDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTDAQ 243
Cdd:TIGR01271 579 LDVVTEKEIFE--SCLCKlMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-243 |
8.76e-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: 46.00 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 4 HPIQDAVLRVDRLSVVypgGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtptggsvtseLGELGSGSALRQ 83
Cdd:cd03291 33 HSSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--------------LGELEPSEGKIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 84 HRRRTAMIFQHhQLIERQSALANVLTGRLAFHNTLRSLFPLPRADQEIA-LSCLARVGLADKALSrvdkLSGGQQQRVGI 162
Cdd:cd03291 96 HSGRISFSSQF-SWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITkFPEKDNTVLGEGGIT----LSGGQRARISL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 163 ARALAQQPAIILADEPVASLDPATSVRVLGllRDICK-EDGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTD 241
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLDVFTEKEIFE--SCVCKlMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQS 247
|
..
gi 1393936756 242 AQ 243
Cdd:cd03291 248 LR 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-210 |
9.11e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 22 GGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSeLG-ELGSGSalRQHRRRTAMIFQHHQLIER 100
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL-FGqPVDAGD--IATRRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 101 QSALAN-VLTGRLaFHntlrslfpLPRADQEIALS-CLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEP 178
Cdd:NF033858 354 LTVRQNlELHARL-FH--------LPAAEIAARVAeMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190
....*....|....*....|....*....|..
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEDGITVIVSLH 210
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-238 |
1.46e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 113 AFHNTLRSLFPLPRADQEIA------LSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQQPAII--LADEPVASLD 183
Cdd:PRK00635 431 ELFIFLSQLPSKSLSIEEVLqglksrLSILIDLGLPYLTPERaLATLSGGEQERTALAKHLGAELIGItyILDEPSIGLH 510
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393936756 184 PATSVRVLGLLRDIcKEDGITVIVSLHQlEYARRFADRVV------GLADSQIVFDAAPSE 238
Cdd:PRK00635 511 PQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADRIIdigpgaGIFGGEVLFNGSPRE 569
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
7-211 |
2.01e-05 |
|
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: 45.51 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 7 QDAVLRVDRLSVVYPGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelgsgsalrqhrR 86
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------------A 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 87 RTAMIFqhhqlIERQSALANvltgrlafhNTLRS--LFPLPRADQEialsclaRVGLADKALSRV--------------- 149
Cdd:TIGR00954 514 KGKLFY-----VPQRPYMTL---------GTLRDqiIYPDSSEDMK-------RRGLSDKDLEQIldnvqlthileregg 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 150 --------DKLSGGQQQRVGIARALAQQPAIILADEPVAsldpATSVRVLGLLRDICKEDGITVIVSLHQ 211
Cdd:TIGR00954 573 wsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSHR 638
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
27-223 |
2.43e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLL------RSLNRLVTPTGGSVTSELGEL---------GSGSALRQHRRRTAmi 91
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaEGQRRYVESLSAYARQFLGQMdkpdvdsieGLSPAIAIDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 92 fqhhqlierQSALANV--LTGrlaFHNTLRSLFPlpRADQEIALSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQ 168
Cdd:cd03270 89 ---------RNPRSTVgtVTE---IYDYLRLLFA--RVGIRERLGFLVDVGLGYLTLSRsAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 169 QPAIIL--ADEPVASLDPATSVRVLGLLRDIcKEDGITVIVSLHQLEYARRfADRVV 223
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-232 |
2.59e-05 |
|
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: 45.31 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 8 DAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVtsELGE---LGSGSALRQH 84
Cdd:TIGR03719 320 DKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--EIGEtvkLAYVDQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 85 RRRTAMIFQ-------HHQLIERQ-SALANVltGRLAFHNtlrslfplprADQEialsclarvgladkalSRVDKLSGGQ 156
Cdd:TIGR03719 397 LDPNKTVWEeisggldIIKLGKREiPSRAYV--GRFNFKG----------SDQQ----------------KKVGQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 157 QQRVGIARALAQQPAIILADEPVASLDpatsVRVLGLLRD-ICKEDGITVIVSlHQleyaRRFADRVVG--LA---DSQI 230
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEaLLNFAGCAVVIS-HD----RWFLDRIAThiLAfegDSHV 519
|
..
gi 1393936756 231 VF 232
Cdd:TIGR03719 520 EW 521
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-183 |
3.01e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 4 HPIQDAVLRVDRLSVvyPGgvtaLRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVT-------------- 69
Cdd:PRK10762 251 KAPGEVRLKVDNLSG--PG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldghevvtrspqdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 70 --------SE--------LG----ELGSGSALRQHRRRTAMIfQHHQliERQSA-----LANVLTgrlafhntlrslfpl 124
Cdd:PRK10762 325 langivyiSEdrkrdglvLGmsvkENMSLTALRYFSRAGGSL-KHAD--EQQAVsdfirLFNIKT--------------- 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 125 PRADQEIALsclarvgladkalsrvdkLSGGQQQRVGIARALAQQPAIILADEPVASLD 183
Cdd:PRK10762 387 PSMEQAIGL------------------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-249 |
3.59e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.94 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTSElgelGSGSALRQHrrrtamifqhhQLIERQSALAN 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK----GSVAYVPQQ-----------AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VLTGRLA----FHNTLRSLFPLPraDQEIaLSCLARVGLADKALSrvdkLSGGQQQRVGIARALAQQPAIILADEPVASL 182
Cdd:TIGR00957 719 ILFGKALnekyYQQVLEACALLP--DLEI-LPSGDRTEIGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393936756 183 DPATSVRVL-------GLLRdickedGITVIVSLHQLEYARRfADRVVGLADSQIVFDAAPSELTD-----AQLERIYA 249
Cdd:TIGR00957 792 DAHVGKHIFehvigpeGVLK------NKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQrdgafAEFLRTYA 863
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-263 |
7.93e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 3 PHPIQDAVLRVDRLSVVYpGGVTALRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLnrlvtptGGSVTSELGELGSGSALR 82
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVSGEIGLAKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 83 qhrrrtAMIFQHHQL---IERQSALANVLtgRLAfhntlrslfplPRADQEIALSCLARVGL-ADKALSRVDKLSGGQQQ 158
Cdd:PRK10636 377 ------LGYFAQHQLeflRADESPLQHLA--RLA-----------PQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 159 RVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRDIckeDGITVIVSlHQLEYARRFADRVVGLADSQI-VFDAaps 237
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVS-HDRHLLRSTTDDLYLVHDGKVePFDG--- 510
|
250 260
....*....|....*....|....*.
gi 1393936756 238 ELTDAQLERIYAGRSTTQPANTPAEP 263
Cdd:PRK10636 511 DLEDYQQWLSDVQKQENQTDEAPKEN 536
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-231 |
2.71e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRSLNrlvtptggsvtselGELG--SGSALRQHRRRTAMIF-QHHQLIER--Q 101
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALA--------------GELPllSGERQSQFSHITRLSFeQLQKLVSDewQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 102 SALANVL------TGRlafhnTLRSLFPLPRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILA 175
Cdd:PRK10938 85 RNNTDMLspgeddTGR-----TTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1393936756 176 DEPVASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYARRFADRVVGLADSQIV 231
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
152-240 |
6.30e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLgllrDICKEDGI---TVIVSLHQLEYARRFaDRVVGLADS 228
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF----DSCMKDELkgkTRVLVTNQLHFLPLM-DRIILVSEG 815
|
90
....*....|..
gi 1393936756 229 QIVFDAAPSELT 240
Cdd:PLN03232 816 MIKEEGTFAELS 827
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-225 |
1.10e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTLLRslnrlvtptggsvtselgelgsgsalrqhrrrtamifqhhqlierqsALAN 106
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILD-----------------------------------------------AIGL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 107 VLTGRlaFHNTLRSLFPLPR---ADQEIALsclarvgladkaLSRVDKLSGGQQQRVGIARALAQQ-----PAIILaDEP 178
Cdd:cd03227 44 ALGGA--QSATRRRSGVKAGcivAAVSAEL------------IFTRLQLSGGEKELSALALILALAslkprPLYIL-DEI 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1393936756 179 VASLDPATSVRVLGLLRDICKEdGITVIVSLHQLEYArRFADRVVGL 225
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELA-ELADKLIHI 153
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
28-76 |
1.22e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.49 E-value: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1393936756 28 RDTSIAFRRGeFTVLLGLSGAGKSTLLRSLNRLVtptGGSVTSELGELG 76
Cdd:cd03241 13 EELELDFEEG-LTVLTGETGAGKSILLDALSLLL---GGRASADLIRSG 57
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-239 |
1.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 129 QEIA--LSCLARVGLADKALSR-VDKLSGGQQQRVGIARALAQQPAIIL--ADEPVASLDPATSVRVLGLLRDIcKEDGI 203
Cdd:TIGR00630 463 KEIRerLGFLIDVGLDYLSLSRaAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRL-RDLGN 541
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1393936756 204 TVIVSLHQlEYARRFADRVV------GLADSQIVFDAAPSEL 239
Cdd:TIGR00630 542 TLIVVEHD-EDTIRAADYVIdigpgaGEHGGEVVASGTPEEI 582
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
16-61 |
1.44e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1393936756 16 LSVVYPGGVTALRdtsiAFRRGEFTVLLGLSGAGKSTLlrsLNRLV 61
Cdd:cd01854 68 VSAKTGEGLDELR----ELLKGKTSVLVGQSGVGKSTL---LNALL 106
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-225 |
2.56e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 36 RGEFTVLLGLSGAGKSTLLRSLNRLVTPTGGSVTselgelgsgsalrqhrrrtamifqhhqlierqsalanvltgrlafh 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 116 ntlrslfplpRADQEIALSCLARVGLADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATSVRVLGLLR 195
Cdd:smart00382 35 ----------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1393936756 196 D-----ICKEDGITVIVSLHQLE-----YARRFADRVVGL 225
Cdd:smart00382 105 LrllllLKSEKNLTVILTTNDEKdlgpaLLRRRFDRRIVL 144
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
29-65 |
2.86e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.86e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1393936756 29 DTSIAFRRGEFTVLLGLSGAGKSTLLRSLNRLVTPTG 65
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
148-232 |
6.00e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 148 RVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDpatsVRVLGLLrdickEDGI------TVIVSlHQleyaRRFADR 221
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRAL-----EEALlefpgcAVVIS-HD----RWFLDR 507
|
90
....*....|....*.
gi 1393936756 222 VVG--LA---DSQIVF 232
Cdd:PRK11819 508 IAThiLAfegDSQVEW 523
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
152-183 |
7.24e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.80 E-value: 7.24e-03
10 20 30
....*....|....*....|....*....|..
gi 1393936756 152 LSGGQQQRVGIARALAQQPAIILADEPVASLD 183
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
16-81 |
7.29e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 7.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393936756 16 LSVVYPGGVTALRdtsiAFRRGEFTVLLGLSGAGKSTLLRSLN-RLVTPTGG-----------SVTSELGELGSGSAL 81
Cdd:pfam03193 89 VSAKTGEGIEALK----ELLKGKTTVLAGQSGVGKSTLLNALLpELDLRTGEiseklgrgrhtTTHVELFPLPGGGLL 162
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
27-53 |
7.38e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 7.38e-03
10 20
....*....|....*....|....*..
gi 1393936756 27 LRDTSIAFRRGEFTVLLGLSGAGKSTL 53
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
142-223 |
8.76e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.53 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393936756 142 ADKALSRVDKLSGGQQQRVGIARALAQQPAIILADEPVASLDPATsvrVLGLLRDICKEDGITVIVSlhqleYARRFADR 221
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVS-----HAREFLNT 406
|
..
gi 1393936756 222 VV 223
Cdd:PLN03073 407 VV 408
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
150-213 |
8.86e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.98 E-value: 8.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393936756 150 DKLSGGQQQ---RVGIARALAQQPAIILADEPVASLDPATSVRVLGLLRdICKEDGITVIVSLHQLE 213
Cdd:pfam13304 235 FELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLK-ELSRNGAQLILTTHSPL 300
|
|
| |
