|
Name |
Accession |
Description |
Interval |
E-value |
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-201 |
3.75e-91 |
|
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: 265.63 E-value: 3.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQP--KKEVMTLKKEVLGF 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSI-------TGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLglkykklSKKEKREKKKEALEKVGL-NLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYI 201
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-206 |
6.10e-75 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 225.31 E-value: 6.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKL----ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVMTL 74
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVLGFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENvalpLLLAGvsrKERRERARELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-206 |
8.35e-71 |
|
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: 214.28 E-value: 8.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLK 75
Cdd:cd03255 1 IELKNLSKtyggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNYLLMENETVLEN----LSITG--GKNRKLMIEH-LEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENvelpLLLAGvpKKERRERAEElLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-206 |
2.10e-62 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 192.72 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKeVMTLKKEVlGF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP-PPEWRRQV-AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMEnETVLENL----SITGGK-NRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVR-ILLKPfQLLLADE 155
Cdd:COG4619 79 VPQEPALWG-GTVRDNLpfpfQLRERKfDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRaLLLQP-DVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 156 PTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-206 |
5.88e-58 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 181.79 E-value: 5.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK-IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLK-KEV 78
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG------QDLSRLKrREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 ------LGFIFQNYLLMENETVLEN----LSITGgKNRKLMIEH----LEEVGMdESYLAKKVYQLSGGEKQRIAIVR-I 143
Cdd:COG2884 75 pylrrrIGVVFQDFRLLPDRTVYENvalpLRVTG-KSRKEIRRRvrevLDLVGL-SDKAKALPHELSGGEQQRVAIARaL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 144 LLKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKAD-RIIYIEGGEI 206
Cdd:COG2884 153 VNRP-ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-206 |
9.13e-57 |
|
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: 179.17 E-value: 9.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQD---KL-ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKE--VMTL 74
Cdd:COG4181 8 IIELRGLTKTVGTgagELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaRARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVLGFIFQNYLLMENETVLEN----LSITGGKN-RKLMIEHLEEVGmdesyLAKKV--Y--QLSGGEKQRIAIVRILL 145
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENvmlpLELAGRRDaRARARALLERVG-----LGHRLdhYpaQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 146 -KPfQLLLADEPTGNLDDKNKHKIIELFLALKK-QGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:COG4181 163 tEP-AILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-206 |
9.86e-52 |
|
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: 166.35 E-value: 9.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKEVlG 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-KKNLRELRRKV-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQN---YLLMEneTV-------LENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPfQ 149
Cdd:COG1122 79 LVFQNpddQLFAP--TVeedvafgPENLGLPREEIRERVEEALELVGLEH-LADRPPHELSGGQKQRVAIAGVLaMEP-E 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRI 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
5.21e-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: 162.95 E-value: 5.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKK 76
Cdd:COG1116 7 ALELRGVSKrfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG------KPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVlGFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPf 148
Cdd:COG1116 81 DR-GVVFQEPALLPWLTVLDNvalgLELRGvpkAERRERARELLELVGLAG-FEDAYPHQLSGGMRQRVAIARALaNDP- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRII 199
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFlADRVV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-206 |
7.24e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 7.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkEVMTlkkEV-- 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-------RDVT---GLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 ----LGFIFQNYLLMENETVLEN----LSITGGKN---RKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LK 146
Cdd:COG3842 75 ekrnVGMVFQDYALFPHLTVAENvafgLRMRGVPKaeiRARVAELLELVGLEG-LADRYPHQLSGGQQQRVALARALaPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 147 PfQLLLADEPTGNLDDKNKHKI-IELFLALKKQGKTIICVTHDPE----ISakaDRIIYIEGGEI 206
Cdd:COG3842 154 P-RVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEealaLA---DRIAVMNDGRI 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-206 |
9.85e-49 |
|
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: 158.89 E-value: 9.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKI-QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEV 78
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 lGFIFQNYLLMENETVLEN---------------LSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:cd03256 81 -GMIFQQFNLIERLSVLENvlsgrlgrrstwrslFGLFPKEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-206 |
7.86e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 156.69 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEY-QPKKEVMTLKKEVl 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDINKLRRKV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLENLSI----TGGKNRK----LMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPfQL 150
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLapikVKKMSKAeaeeRAMELLERVGLAD-KADAYPAQLSGGQQQRVAIARALaMEP-KV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHdpEIS-AK--ADRIIYIEGGEI 206
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH--EMGfARevADRVVFMDGGRI 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-206 |
8.85e-48 |
|
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: 156.89 E-value: 8.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYqPKKEVMTLKK 76
Cdd:COG1124 1 MLEVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-TRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVlGFIFQNYLLMEN------ETVLENLSITGGKNRKLMIEH-LEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPf 148
Cdd:COG1124 80 RV-QMVFQDPYASLHprhtvdRILAEPLRIHGLPDREERIAElLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALiLEP- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAvVAHLCDRVAVMQNGRI 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-205 |
9.25e-48 |
|
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: 155.70 E-value: 9.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQD--KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKEVlG 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKV-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQN---YLLMenETV-------LENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPfQ 149
Cdd:cd03225 79 LVFQNpddQFFG--PTVeeevafgLENLGLPEEEIEERVEEALELVGLEG-LRDRSPFTLSGGQKQRVAIAGVLaMDP-D 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGE 205
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-206 |
1.49e-47 |
|
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: 155.36 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKL----ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVM--TL 74
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVlGFIFQNYLLMEN------ETVLENLSITGG-----KNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVR- 142
Cdd:cd03257 81 RKEI-QMVFQDPMSSLNprmtigEQIAEPLRIHGKlskkeARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARa 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 143 ILLKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03257 160 LALNP-KLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-206 |
1.72e-47 |
|
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: 154.98 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVlGF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG---RDVTGVPPERRNI-GM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSItGGKNRKL--------MIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLKLRGVpkaeirarVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDP-EISAKADRIIYIEGGEI 206
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQeEALALADRIAVMNEGRI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-206 |
1.91e-46 |
|
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: 152.30 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME-YQPKKEVMTLKKEVlG 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKlTDDKKNINELRQKV-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSITGGKNRKL--------MIEHLEEVGMDE---SYLAkkvyQLSGGEKQRIAIVRIL-LKPf 148
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMskaeaeerALELLEKVGLADkadAYPA----QLSGGQQQRVAIARALaMNP- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-206 |
2.33e-46 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 152.18 E-value: 2.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKK--EVMTL 74
Cdd:NF038007 1 MLNMQNAEKcyitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVLGFIFQNYLLMENETVLENLSIT---GGKNRKLMIEHLEEV----GMDESYLAKKVyQLSGGEKQRIAIVRILLKP 147
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPlkyRGVAKKERIERVNQVlnlfGIDNRRNHKPM-QLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-205 |
2.85e-46 |
|
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: 150.80 E-value: 2.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEVLGF 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLsitggknrklmiehleevgmdesylakkVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENI----------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 162 DKNKHKIIELFLALKKQ-GKTIICVTHDP-EISAKADRIIYIEGGE 205
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-205 |
6.10e-46 |
|
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: 150.86 E-value: 6.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQ-DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKE 77
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgeDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VlGFIFQNYLLMENETVLEN----LSITGGKNRKlmIEH-----LEEVGMDESYLAKKVyQLSGGEKQRIAIVRILLKPF 148
Cdd:TIGR02673 81 I-GVVFQDFRLLPDRTVYENvalpLEVRGKKERE--IQRrvgaaLRQVGLEHKADAFPE-QLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGE 205
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-199 |
1.66e-45 |
|
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: 149.93 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeYQPKKEVmtlkKE 77
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD---GEPVTGP----GP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGFIFQNYLLMENETVLEN----LSITGGKNRKLM---IEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPfQ 149
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNvalgLELQGVPKAEAReraEELLELVGLSG-FENAYPHQLSGGMRQRVALARALaVDP-D 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHD-PEISAKADRII 199
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDiDEAVFLADRVV 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-206 |
2.67e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.83 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEyqPKKEVMTLKKEVlGF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED--VARDPAEVRRRI-GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITGG-------KNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARlyglprkEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-206 |
4.44e-45 |
|
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: 156.22 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK-----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMT 73
Cdd:COG1123 260 LLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 74 LKKEVlGFIFQNYLLMEN------ETVLENLSITGGKN----RKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:COG1123 340 LRRRV-QMVFQDPYSSLNprmtvgDIIAEPLRLHGLLSraerRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 144 L-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:COG1123 419 LaLEP-KLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-207 |
2.32e-43 |
|
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: 145.39 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemEYQPKKEVMTLKKEvLG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID--GEDVRKEPREARRQ-IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSITG------GKNRKLMIEHL-EEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAelyglfDEELKKRIEELiELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMqEVEALCDRVVILHKGKVV 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-203 |
3.14e-43 |
|
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: 143.77 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVLG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG---EPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENL----SITGGKNRKLMI-EHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:COG4133 79 YLGHADGLKPELTVRENLrfwaALYGLRADREAIdEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPeISAKADRIIYIEG 203
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQP-LELAAARVLDLGD 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-206 |
1.24e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 151.42 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQ----DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSG--QVIINEMEYQPKKEVMTL 74
Cdd:PRK10535 4 LLELKDIRRSYPsgeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVLGFIFQNYLLMENETVLENLSI------TGGKNRKL-MIEHLEEVGmdesyLAKKVY----QLSGGEKQRIAIVRI 143
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVpavyagLERKQRLLrAQELLQRLG-----LEDRVEyqpsQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-205 |
1.74e-42 |
|
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: 140.60 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD--KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKKEVL 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG------VDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 ----GFIFQNYLLMeNETVLENLsitggknrklmiehleevgmdesylakkvyqLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:cd03228 75 rkniAYVPQDPFLF-SGTIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGE 205
Cdd:cd03228 123 ATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-206 |
6.62e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.52 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkEVMTLKKEV--- 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-------RDLFTNLPPrer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 -LGFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDEsyLAKKvY--QLSGGEKQRIAIVRIL-LKP 147
Cdd:COG1118 76 rVGFVFQHYALFPHMTVAENiafgLRVRPpskAEIRARVEELLELVQLEG--LADR-YpsQLSGGQRQRVALARALaVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 148 fQLLLADEPTGNLDDKNKHKI-IELFLALKKQGKTIICVTHDPE----IsakADRIIYIEGGEI 206
Cdd:COG1118 153 -EVLLLDEPFGALDAKVRKELrRWLRRLHDELGGTTVFVTHDQEealeL---ADRVVVMNQGRI 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-197 |
5.99e-41 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 138.80 E-value: 5.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQD-KL---ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVI-----INEMEYQPKKEvmtLKK 76
Cdd:PRK11629 10 NLCKRYQEgSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpMSKLSSAAKAE---LRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVLGFIFQNYLLMENETVLENLS---ITGGKNRKLM----IEHLEEVGmdesyLAKKVY----QLSGGEKQRIAIVRILL 145
Cdd:PRK11629 87 QKLGFIYQFHHLLPDFTALENVAmplLIGKKKPAEInsraLEMLAAVG-----LEHRANhrpsELSGGERQRVAIARALV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAKADR 197
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSR 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-206 |
7.12e-41 |
|
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: 138.48 E-value: 7.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDK----LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTL 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVlGFIFQNYLLMENETVLEN----LSITG--GKNRKLMIEH-LEEVGMD---ESYLAkkvyQLSGGEKQRIAIVRIL 144
Cdd:cd03258 81 RRRI-GMIFQHFNLLSSRTVFENvalpLEIAGvpKAEIEERVLElLELVGLEdkaDAYPA----QLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 145 LKPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEvVKRICDRVAVMEKGEV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
1.13e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkkevmtLKKEVLG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-------RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMEN------ETVLENLSITGG------KNRKLMIEH-LEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:COG1121 79 YVPQRAEVDWDfpitvrDVVLMGRYGRRGlfrrpsRADREAVDEaLERVGLED-LADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEIR 207
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNRGLVA 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-206 |
1.60e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.92 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ-PKKEVMTLKKEVl 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDERLIRQEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLEN-----LSITGGKN---RKLMIEHLEEVGMDES---YLAkkvyQLSGGEKQRIAIVRIL-LKP 147
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENvmfgpLRVRGASKeeaEKQARELLAKVGLAERahhYPS----ELSGGQQQRVAIARALaVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK09493 156 -KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-206 |
2.26e-40 |
|
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: 137.87 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLK-KEV- 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG------RDLASLSrRELa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 --LGFIFQNYLLMENETVLE-----------NLSITGGKNRKLMIEHLEEVGMDEsyLAKK-VYQLSGGEKQRIAIVRIL 144
Cdd:COG1120 75 rrIAYVPQEPPAPFGLTVRElvalgryphlgLFGRPSAEDREAVEEALERTGLEH--LADRpVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 145 L-KPfQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG1120 153 AqEP-PLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARyADRLVLLKDGRI 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-206 |
2.61e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.21 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTL--KKEV 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG------RDVTDLppKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENLSItGGKNRKL-------MIEH-LEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQL 150
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAF-PLKLRKVpkaeidrRVREaAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 151 LLADEPTGNLDDKNKHKI-IELFLALKKQGKTIICVTHDP-EISAKADRIIYIEGGEI 206
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMrAEIKRLHRRLGTTTIYVTHDQvEAMTLADRIAVMNDGRI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-207 |
2.93e-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: 137.95 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKK--IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEVl 79
Cdd:TIGR04520 1 IEVENVSFSypESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNyllMENE----TV-------LENLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRIL-LKP 147
Cdd:TIGR04520 80 GMVFQN---PDNQfvgaTVeddvafgLENLGVPREEMRKRVDEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLaMRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIELFLALKK-QGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:TIGR04520 156 -DIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-206 |
5.25e-40 |
|
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: 134.45 E-value: 5.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeYQPKKEVMTLKKEVlGF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--KDIKKEPEEVKRRI-GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLsitggknrklmiehleevgmdesylakkvyQLSGGEKQRIAIVRILL-KPfQLLLADEPTGNL 160
Cdd:cd03230 78 LPEEPSLYENLTVRENL------------------------------KLSGGMKQRLALAQALLhDP-ELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 161 DDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-206 |
9.67e-40 |
|
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: 135.71 E-value: 9.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQP--KKEVMTLKKEVl 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLENLS--------ITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVR-ILLKPfQL 150
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAfplrehtrLSEEEIREIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARaLALDP-EL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-205 |
1.42e-39 |
|
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: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEyqpkkevmtlkkevlgfi 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 fqnyllmenetvlenlsitggKNRKLMIEHLEEVGMdesylakkVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDD 162
Cdd:cd00267 63 ---------------------IAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 163 KNKHKIIELFLALKKQGKTIICVTHDPEISAKA-DRIIYIEGGE 205
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-207 |
5.49e-39 |
|
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: 133.15 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkEVMTL---KKEV 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-------RDVTDlppKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENLSItGGKNRK----------------LMIEHLeevgmdesyLAKKVYQLSGGEKQRIAIVR 142
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAF-GLKLRKvpkdeidervrevaelLQIEHL---------LDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 143 ILLKPFQLLLADEPTGNLDDKNKHKI-IELFLALKKQGKTIICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHDQvEAMTMADRIAVMNDGQIQ 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-206 |
1.30e-38 |
|
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: 140.74 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKK--IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkkevmTLKKEVL 79
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR------QIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 ----GFIFQNYLLMeNETVLENLSITGGK-NRKLMIEHLEEVGMDE----------SYLAKKVYQLSGGEKQRIAIVRIL 144
Cdd:COG2274 548 rrqiGVVLQDVFLF-SGTIRENITLGDPDaTDEEIIEAARLAGLHDfiealpmgydTVVGEGGSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 145 LKPFQLLLADEPTGNLDDKNKHKIIElFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILE-NLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-206 |
1.38e-38 |
|
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: 139.51 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVS-KKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkkevmTLKKE--- 77
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS------DLDPAswr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 -VLGFIFQN-YLLmeNETVLENLSItGGKN--RKLMIEHLEEVGMDE----------SYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:COG4988 411 rQIAWVPQNpYLF--AGTIRENLRL-GRPDasDEELEAALEAAGLDEfvaalpdgldTPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-206 |
2.34e-38 |
|
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: 131.98 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVlGF 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITNLPPHKRPV-NT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSItGGKNRKL--------MIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLpkaeikerVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDK-NKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03300 155 DEPLGALDLKlRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-207 |
2.95e-38 |
|
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: 138.36 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSkDSGQVIINEMEYQ--PKKEVmtlkKEVLGFIFQN-YL 87
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLDP-QSGSITLGGVDLRdlDEDDL----RRRIAVVPQRpHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 88 LmeNETVLENLsitggknrKL---------MIEHLEEVGMDEsYLAKKVY-----------QLSGGEKQRIAIVRILLKP 147
Cdd:COG4987 421 F--DTTLRENL--------RLarpdatdeeLWAALERVGLGD-WLAALPDgldtwlgeggrRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALkKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-206 |
7.86e-38 |
|
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: 136.57 E-value: 7.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLN-VIGHLDS--KDSGQVIINEmeyqpkKEVMTLKKEV 78
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHggRISGEVLLDG------RDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LG----FIFQNYLLMENET--------VLENLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLK 146
Cdd:COG1123 81 RGrrigMVFQDPMTQLNPVtvgdqiaeALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGvVAEIADRVVVMDDGRI 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-206 |
1.58e-37 |
|
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: 129.45 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKI-QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEv 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqDVSDLRGRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLEN----LSITGGKNR---KLMIEHLEEVGmdesyLAKKVY----QLSGGEKQRIAIVRILLKP 147
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENvafaLEVTGVPPReirKRVPAALELVG-----LSHKHRalpaELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEI-SAKADRIIYIEGGEI 206
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-207 |
2.47e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 129.51 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVI-----INEMEYQPKKEvmtLKKEVLGFIFQNYLLME 90
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqpLHQMDEEARAK---LRAKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENLSITG-------GKNRKLMIEHLEEVGmdesyLAKKVY----QLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:PRK10584 102 TLNALENVELPAllrgessRQSRNGAKALLEQLG-----LGKRLDhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 160 LDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PRK10584 177 LDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-206 |
6.93e-37 |
|
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: 126.78 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLK-KEV--- 78
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------KDLASLSpKELark 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNyllmenetvlenlsitggknrklmiehLEEVGMDesYLAKKVY-QLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:cd03214 75 IAYVPQA---------------------------LELLGLA--HLADRPFnELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 158 GNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-206 |
1.29e-36 |
|
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: 127.30 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-----DSKDSGQVIINEME-YQPKKEVMTLK 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVlGFIFQ--NYLLMeneTVLENLS----ITGGKNRK----LMIEHLEEVGMDESYLAK-KVYQLSGGEKQRIAIVRIL 144
Cdd:cd03260 81 RRV-GMVFQkpNPFPG---SIYDNVAyglrLHGIKLKEeldeRVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 145 -LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03260 157 aNEP-EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-206 |
5.21e-36 |
|
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: 126.25 E-value: 5.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVMTLKKEV 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 lGFIFQNYLLMENETVLENL--------SITGGKNRKLMIEHLEEVGMDEsylAKKVY--QLSGGEKQRIAIVR-ILLKP 147
Cdd:COG1127 85 -GMLFQGGALFDSLTVFENVafplrehtDLSEAEIRELVLEKLELVGLPG---AADKMpsELSGGMRKRVALARaLALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:COG1127 161 -EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-206 |
7.61e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 128.27 E-value: 7.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKK 76
Cdd:COG1135 1 MIELENLSKtfptKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG------VDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVL-------GFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDE---SYLAkkvyQLSGGEKQRIA 139
Cdd:COG1135 75 RELraarrkiGMIFQHFNLLSSRTVAENvalpLEIAGvpkAEIRKRVAELLELVGLSDkadAYPS----QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 140 IVRIL-LKPfQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG1135 151 IARALaNNP-KVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDvVRRICDRVAVLENGRI 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-204 |
2.13e-35 |
|
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: 123.80 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqPKKEVMTLKKevLGFI 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKR--IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQNYLLMEN------ETVLENL-------SITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQ 149
Cdd:cd03235 74 PQRRSIDRDfpisvrDVVLMGLyghkglfRRLSKADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGG 204
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLLNRT 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-206 |
2.29e-34 |
|
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: 122.06 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEV--MTLKKEVL 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDAtdVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLEN----LSITGGKNR--KLMI-----EHLEEVGMDesYLAKKV-YQLSGGEKQRIAIVRILLKP 147
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNvafgLRVKPRSERppEAEIrakvhELLKLVQLD--WLADRYpAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 148 FQLLLADEPTGNLDDKNKHkiiELFLALKK----QGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRK---ELRRWLRRlhdeLHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-206 |
2.92e-34 |
|
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: 121.64 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINE---MEYQPKKevmtLKKE 77
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGediREQDPVE----LRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 vLGFIFQNYLLMENETVLENLSIT-------GGKNRKLMIEHLEEVGMDE-SYLAKKVYQLSGGEKQRIAIVRILLKPFQ 149
Cdd:cd03295 77 -IGYVIQQIGLFPHMTVEENIALVpkllkwpKEKIRERADELLALVGLDPaEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRlADRIAIMKNGEI 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-190 |
3.47e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.28 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVS----KKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ-PKKEvmtlk 75
Cdd:COG4525 3 MLTVRHVSvrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPGAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 kevLGFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:COG4525 78 ---RGVVFQKDALLPWLNVLDNvafgLRLRGvpkAERRARAEELLALVGLAD-FARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPE 190
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVE 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-203 |
4.93e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 120.28 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDS--KDSGQVIINEmeyqpkKEVMTLKKE 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIaGTLSPafSASGEVLLNG------RRLTALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 V--LGFIFQNYLLMENETVLENLSI-----TGGKNRKLMIEH-LEEVGMDesYLAKK-VYQLSGGEKQRIAIVRILL-KP 147
Cdd:COG4136 75 QrrIGILFQDDLLFPHLSVGENLAFalpptIGRAQRRARVEQaLEEAGLA--GFADRdPATLSGGQRARVALLRALLaEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIEL-FLALKKQGKTIICVTHDPEISAKADRIIYIEG 203
Cdd:COG4136 153 -RALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-206 |
1.18e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.86 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKkIQDKLILEkVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQP--KKEVMTLkk 76
Cdd:COG3840 1 MLRLDDLTY-RYGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqDLTALPpaERPVSML-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 evlgfiFQNYLLMENETVLENLSI---TGGK----NRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQ 149
Cdd:COG3840 77 ------FQENNLFPHLTVAQNIGLglrPGLKltaeQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARiADRVLLVADGRI 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-207 |
4.16e-33 |
|
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: 121.36 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIElVNVSKKIQDkLILEkVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKE--V 78
Cdd:COG4148 2 MLE-VDFRLRRGG-FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENL----SITGGKNRK---------LMIEHLeevgmdesyLAKKVYQLSGGEKQRIAIVRILL 145
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLlygrKRAPRAERRisfdevvelLGIGHL---------LDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 146 -KPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGKT-IICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:COG4148 150 sSP-RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLdEVARLADHVVLLEQGRVV 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-206 |
4.24e-33 |
|
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: 117.98 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 21 SLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkkeVMTLKKEVLGFIFQNYLLMENETVLENLSI 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT----AAPPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 101 TGGKNRKLMIEH-------LEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFL 173
Cdd:cd03298 94 GLSPGLKLTAEDrqaievaLARVGLAG-LEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 489821526 174 ALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03298 173 DLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-206 |
8.96e-33 |
|
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: 115.78 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD--KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKevMTLKKEVL 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD--PNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENeTVLENLsitggknrklmiehleevgmdesylakkvyqLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 160 LDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-206 |
9.19e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 118.24 E-value: 9.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLkkevlgfIFQN 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL-------MFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENLSI-TGGKNRKLMIEHLEEVGmdesyLAKKVYQ----LSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:PRK11247 90 ARLLPWKKVIDNVGLgLKGQWRDAALQALAAVG-----LADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489821526 161 DDKNKHKIIELFLAL-KKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK11247 165 DALTRIEMQDLIESLwQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-206 |
1.03e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.81 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEY----QPK-KEVMTLKK 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSeKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVlGFIFQNYLLMENETVLENL--------SITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:COG4161 83 KV-GMVFQQYNLWPHLTVMENLieapckvlGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRI 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-206 |
3.00e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.42 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKeVMTLKKEVlGFIFQNyllMEN 91
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-VWDVRRQV-GMVFQN---PDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETV-----------LENLSITggknRKLMIEH----LEEVGMdESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADE 155
Cdd:PRK13635 93 QFVgatvqddvafgLENIGVP----REEMVERvdqaLRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLaLQP-DIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGK-TIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-206 |
5.69e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.00 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEY-------QPKKEVMT 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 74 LKKEVlGFIFQNYLLMENETVLENL----SITGGKNRKLMI----EHLEEVGM---DESYLAKkvyqLSGGEKQRIAIVR 142
Cdd:PRK11264 83 LRQHV-GFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEATararELLAKVGLagkETSYPRR----LSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 143 ILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-206 |
8.92e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 8.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK---KEVMTLKKEVlGFIFQ--NYLL 88
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknKKLKPLRKKV-GIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MEnETVLE-------NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:PRK13634 99 FE-ETVEKdicfgpmNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 162 DKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13634 178 PKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-207 |
1.81e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.40 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkevmTLKkevLG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----------TVK---IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNY-LLMENETVLENLS--ITGGKNRKLMiehleevgmdeSYLA----------KKVYQLSGGEKQRIAIVRILLKP 147
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRdgAPGGTEQEVR-----------GYLGrflfsgddafKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 148 FQLLLADEPTGNLDdknkhkiIE----LFLALKK-QGkTIICVTHDPE-ISAKADRIIYIEGGEIR 207
Cdd:COG0488 451 PNVLLLDEPTNHLD-------IEtleaLEEALDDfPG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-206 |
2.50e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.72 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEV--MTLKKEVL 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH------GTDVsrLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLENLSI-----------TGGKNRKLMIEHLEEVGMdeSYLAKKvY--QLSGGEKQRIAIVRILLK 146
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFgltvlprrerpNAAAIKAKVTQLLEMVQL--AHLADR-YpaQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGK-TIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-206 |
3.20e-31 |
|
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: 114.66 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVMTLKKEVLGFIFQNYLLMENETVLEN 97
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 98 ----LSITG---GKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIE 170
Cdd:cd03294 123 vafgLEVQGvprAEREERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 489821526 171 LFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03294 202 ELLRLqAELQKTIVFITHDLDEALRlGDRIAIMKDGRL 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-206 |
3.31e-31 |
|
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: 115.54 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHL---DSKDSGQVIINEmeyqpkKEVMTLKKEVL--------GFIFQN--- 85
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDG------EDLLKLSEKELrkirgreiQMIFQDpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 ---------YLLMenETVLENLSITGGKNRKLMIEHLEEVGMD--ESYLAKKVYQLSGGEKQRIAIVR-ILLKPfQLLLA 153
Cdd:COG0444 98 slnpvmtvgDQIA--EPLRIHGGLSKAEARERAIELLERVGLPdpERRLDRYPHELSGGMRQRVMIARaLALEP-KLLIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRII--YieGGEI 206
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEiADRVAvmY--AGRI 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-206 |
4.80e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.20 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQP--KKEVMTlkke 77
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqDITHVPaeNRHVNT---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 vlgfIFQNYLLMENETVLENLSItGGKNRKLMIEHLEEVGMD-------ESYLAKKVYQLSGGEKQRIAIVRILLKPFQL 150
Cdd:PRK09452 91 ----VFQSYALFPHMTVFENVAF-GLRMQKTPAAEITPRVMEalrmvqlEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 151 LLADEPTGNLDDK-NKHKIIELFLALKKQGKTIICVTHDPEIS-AKADRIIYIEGGEI 206
Cdd:PRK09452 166 LLLDESLSALDYKlRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-157 |
6.24e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 110.43 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKevLGFIFQNYLLMENETVLE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE--IGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 97 NLSITG--------GKNRKL--MIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:pfam00005 79 NLRLGLllkglskrEKDARAeeALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
8.08e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK--IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkKEVMTLKKEV 78
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNyllMENE----TV-------LENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LK 146
Cdd:PRK13632 85 IGIIFQN---PDNQfigaTVeddiafgLENKKVPPKKMKDIIDDLAKKVGMED-YLDKEPQNLSGGQKQRVAIASVLaLN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 147 PfQLLLADEPTGNLDDKNKHKIIELFLALKKQG-KTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13632 161 P-EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-206 |
9.72e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.96 E-value: 9.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKKEVL----GFIFQNYLL 88
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG------VDIRDLTLESLrrqiGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MeNETVLENlsITGGKN---RKLMIEHLEEVGMDE----------SYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:COG1132 426 F-SGTIREN--IRYGRPdatDEEVEEAAKAAQAHEfiealpdgydTVVGERGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 156 PTGNLDDKNKHKIIElflALKK--QGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:COG1132 503 ATSALDTETEALIQE---ALERlmKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-206 |
1.09e-30 |
|
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: 111.10 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDS-KDSGQVIINEmeyqpKKEVMTLKKEVLGFIFQNYLLMEN 91
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGlGVSGEVLING-----RPLDKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLsitggknrklmiehleevgmdesYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIEL 171
Cdd:cd03213 97 LTVRETL-----------------------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 489821526 172 FLALKKQGKTIICVTHDP--EISAKADRIIYIEGGEI 206
Cdd:cd03213 154 LRRLADTGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-199 |
1.19e-30 |
|
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: 112.14 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK----IQDKLIL---EKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ------P 67
Cdd:COG4778 4 LLEVENLSKTftlhLQGGKRLpvlDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqaS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 68 KKEVMTLKKEVLGFIFQnYLlmeneTVLENLSitggkNRKLMIEHLEEVGMDESYLAKKVYQL----------------- 130
Cdd:COG4778 84 PREILALRRRTIGYVSQ-FL-----RVIPRVS-----ALDVVAEPLLERGVDREEARARARELlarlnlperlwdlppat 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 131 -SGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRII 199
Cdd:COG4778 153 fSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEvREAVADRVV 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-204 |
2.41e-30 |
|
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: 111.40 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ-PKKEVMTlkkevlgfIFQNYLLMENETVL 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITePGPDRMV--------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLSI---------TGGKNRKLMIEHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKH 166
Cdd:TIGR01184 73 ENIALavdrvlpdlSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489821526 167 KIIELFLAL-KKQGKTIICVTHD-PEISAKADRIIYIEGG 204
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
4.16e-30 |
|
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: 115.85 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKevLGFIFQNYLLMENeTVLENLS 99
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ--IAWVPQHPFLFAG-TIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 100 I-TGGKNRKLMIEHLEEVGMDE------SYLAKKVYQ----LSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKI 168
Cdd:TIGR02857 418 LaRPDASDAEIREALERAGLDEfvaalpQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180 190
....*....|....*....|....*....|.
gi 489821526 169 IELFLALkKQGKTIICVTHDPEISAKADRII 199
Cdd:TIGR02857 498 LEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-206 |
1.38e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPK---KEVMTLKK 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTpsdKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVlGFIFQNYLLMENETVLENL--------SITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PRK11124 83 NV-GMVFQQYNLWPHLTVQQNLieapcrvlGLSKDQALARAEKLLERLRLKP-YADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHI 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-206 |
1.84e-29 |
|
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: 109.35 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDkLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLK--KEVL 79
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG------KDITNLPpeKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLENLSItGGKNRKLMIEHLEE--------VGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAY-GLKKRKVDKKEIERkvleiaemLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 152 LADEPTGNLDDKNKHKII-ELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03299 152 LLDEPFSALDVRTKEKLReELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-207 |
3.14e-29 |
|
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: 107.69 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMtlkkEVLGF 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITG---GKNRKLMIEHLEEVGMDESYlAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLArllGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 159 NLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-206 |
3.70e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.18 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKL-----ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKK 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EV----------------------LGFIFQ--NYLLMEnETVLEN-------LSITGGKNRKLMIEHLEEVGMDESYLAK 125
Cdd:PRK13651 83 VLeklviqktrfkkikkikeirrrVGVVFQfaEYQLFE-QTIEKDiifgpvsMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 126 KVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGG 204
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDnVLEWTKRTIFFKDG 241
|
..
gi 489821526 205 EI 206
Cdd:PRK13651 242 KI 243
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-207 |
3.71e-29 |
|
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: 107.66 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGeFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEyqPKKEVMTLKKeVLGF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQPQKLRR-RIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLS-------ITGGKNRKLMIEHLEEVGMDESYlAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDyiawlkgIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPE-ISAKADRIIYIEGGEIR 207
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-207 |
5.94e-29 |
|
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: 107.38 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQP--KKEVMTLKKEVLGFIFQNYLLMENETVLENLS--ITG 102
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrKKINLPPQQRKIGLVFQQYALFPHLNVRENLAfgLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 103 GKNRKLMI---EHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQ- 178
Cdd:cd03297 103 KRNREDRIsvdELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNl 181
|
170 180 190
....*....|....*....|....*....|
gi 489821526 179 GKTIICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:cd03297 182 NIPVIFVTHDLsEAEYLADRIVVMEDGRLQ 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-190 |
6.27e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.25 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ-PKKEvmtlkkevL 79
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgPGAE--------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNvafgLQLAGvekMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 489821526 153 ADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPE 190
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIE 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-206 |
8.63e-29 |
|
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: 106.57 E-value: 8.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKevmtlKKEVLGFIFQN--YLLMEn 91
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-----RRKSIGYVMQDvdYQLFT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSItGGKNRKLMIEHLEEVgMDESYLAKKVYQ----LSGGEKQRIAI-VRILLKPfQLLLADEPTGNLDDKNKH 166
Cdd:cd03226 87 DSVREELLL-GLKELDAGNEQAETV-LKDLDLYALKERhplsLSGGQKQRLAIaAALLSGK-DLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 167 KIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-206 |
8.83e-29 |
|
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: 105.86 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 5 VNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSkDSGQVIINEmeyqpkKEVMTLKKEV---LG 80
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKP-QQGEITLDG------VPVSDLEKALsslIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMeNETVLENLSItggknrklmiehleevgmdesylakkvyQLSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNLGR----------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 161 DDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03247 130 DPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-206 |
1.01e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 110.12 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVlGFIF 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAERGV-GMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 84 QNYLLMENETVLENLSI------TGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:PRK11000 82 QSYALYPHLSVAENMSFglklagAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 158 GNLDDKNKHKI-IELFLALKKQGKTIICVTHDP-EISAKADRIIYIEGGEI 206
Cdd:PRK11000 162 SNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-199 |
1.35e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEVMTLKKEV-- 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE------GEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 --LGFIFQNYLLMeNETVLENL----SITGGK-NRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK10247 81 qqVSYCAQTPTLF-GDTVYDNLifpwQIRNQQpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAKADRII 199
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVI 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-206 |
3.93e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.21 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEY--------QPK---KE 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgQLKvadKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 71 VMTLKKEVLGFIFQNYLLMENETVLEN--------LSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVR 142
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 143 ILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-207 |
3.96e-28 |
|
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: 105.28 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSK--KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEvmtlkKE 77
Cdd:cd03263 1 LQIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgySIRTDRKAA-----RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGFIFQNYLLMENETVLENL-------SITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQL 150
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLrfyarlkGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMdEAEALCDRIAIMSDGKLR 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-207 |
5.31e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpkkevmtlKKEVLGFIFQN 85
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-------------KGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENLsITGGKNRKLMIEHLEEV----------------------------------------GMDESYLAK 125
Cdd:COG0488 70 PPLDDDLTVLDTV-LDGDAELRALEAELEELeaklaepdedlerlaelqeefealggweaearaeeilsglGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 126 KVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDdknkhkiIE--LFLA--LKKQGKTIICVTHDPE-ISAKADRIIY 200
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LEsiEWLEefLKNYPGTVLVVSHDRYfLDRVATRILE 221
|
....*..
gi 489821526 201 IEGGEIR 207
Cdd:COG0488 222 LDRGKLT 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-190 |
7.74e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME------YQPKKEVMtl 74
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvppYQRPINMM-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 kkevlgfiFQNYLLMENETVLENLSItGGKNRKL--------MIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLK 146
Cdd:PRK11607 97 --------FQSYALFPHMTVEQNIAF-GLKQDKLpkaeiasrVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKI-IELFLALKKQGKTIICVTHDPE 190
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQE 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
9.12e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.55 E-value: 9.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK-----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLK 75
Cdd:COG1101 1 MLELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG------KDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEV----LGFIFQNYLL--MENETVLENLSI-------------TGGKNRKLMIEHLEEVGMD-ESYLAKKVYQLSGGEK 135
Cdd:COG1101 75 EYKrakyIGRVFQDPMMgtAPSMTIEENLALayrrgkrrglrrgLTKKRRELFRELLATLGLGlENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 136 QRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDyGNRLIMMHEGRI 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-206 |
9.57e-28 |
|
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: 109.12 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDS--KDSGQVIINeMEYQPKKEVM------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYH-VALCEKCGYVerpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 73 --------TLKKEVLGFI-----------------FQ-NYLLMENETVLEN-------LSITGGKNRKLMIEHLEEVGMD 119
Cdd:TIGR03269 80 epcpvcggTLEPEEVDFWnlsdklrrrirkriaimLQrTFALYGDDTVLDNvlealeeIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 120 E--SYLAKkvyQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFL-ALKKQGKTIICVTHDPEISAK-A 195
Cdd:TIGR03269 160 HriTHIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSHWPEVIEDlS 236
|
250
....*....|.
gi 489821526 196 DRIIYIEGGEI 206
Cdd:TIGR03269 237 DKAIWLENGEI 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-206 |
9.82e-28 |
|
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: 102.51 E-value: 9.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKkevmtlkkevlgf 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 ifqnyllmenetvlenlsitggkNRKLMIEHLeeVGMdesylakkVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:cd03216 68 -----------------------SPRDARRAG--IAM--------VYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 162 DKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-198 |
1.14e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK--KEVMTLKkev 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRspRDAIALG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENL------SITGGKNRKLMIEHLEEVGmdESY-----LAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIvlglepTKGGRLDRKAARARIRELS--ERYgldvdPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRI 198
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKlREVMAIADRV 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-206 |
3.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMT-LKKEVlGFIFQ--NYLLMEnET 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdIRKKV-GLVFQypEYQLFE-ET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 V-------LENLSITGGKNRKLMIEHLEEVGMD-ESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:PRK13637 101 IekdiafgPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 166 HKIIELFLALKKQGK-TIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13637 181 DEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-207 |
3.63e-27 |
|
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: 105.58 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 19 KVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQP--KKEVMTLKKEVLGFIFQNYLLMENETVLE 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 97 NL----SITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELF 172
Cdd:TIGR02142 95 NLrygmKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 489821526 173 LALKKQ-GKTIICVTHDP-EISAKADRIIYIEGGEIR 207
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLqEVLRLADRVVVLEDGRVA 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-206 |
4.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQD------KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTL 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVlGFIFQNyllMENETVL-----------ENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:PRK13633 84 RNKA-GMVFQN---PDNQIVAtiveedvafgpENLGIPPEEIRERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-206 |
6.60e-27 |
|
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: 102.28 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKI--QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKEVl 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-QLDPADLRRNI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMeNETVLENLSITG--GKNRKLMiEHLEEVGMDEsYLAK-----------KVYQLSGGEKQRIAIVRILLK 146
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAplADDERIL-RAAELAGVTD-FVNKhpngldlqigeRGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-206 |
8.00e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 8.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSkDSGQVIINEME---YQPKKEVMTL-- 74
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSP-DSGEVRLNGRPladWSPAELARRRav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 --KKEVLGFIFqnyllmeneTVLE-------NLSITGGKNRKLMIEHLEEVGMDEsyLAKKVY-QLSGGEKQRIAIVRIL 144
Cdd:PRK13548 81 lpQHSSLSFPF---------TVEEvvamgraPHGLSRAEDDALVAAALAQVDLAH--LAGRDYpQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 145 L------KPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARyADRIVLLHQGRL 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-206 |
8.04e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.88 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK-IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKEVMTLKKE 77
Cdd:PRK10908 1 MIRFEHVSKAyLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VlGFIFQNYLLMENETVLENLSI-------TGGKNRKLMIEHLEEVGMDESylAKKV-YQLSGGEKQRIAIVRILLKPFQ 149
Cdd:PRK10908 81 I-GMIFQDHHLLMDRTVYDNVAIpliiagaSGDDIRRRVSAALDKVGLLDK--AKNFpIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHL 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-205 |
9.46e-27 |
|
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: 99.45 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQViinemeyqpkkevmtlkkevlgf 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 ifqnyllmeneTVLENLSItggknrklmiehleevgmdeSYLAkkvyQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:cd03221 58 -----------TWGSTVKI--------------------GYFE----QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 162 DKNKHKIIElflALKKQGKTIICVTHDPE-ISAKADRIIYIEGGE 205
Cdd:cd03221 103 LESIEALEE---ALKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-206 |
9.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 9.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK---KEVMTLKKEV-LGFIFQNYLLMENe 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLKKLRKKVsLVFQFPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLE-------NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:PRK13641 102 TVLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489821526 166 HKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-206 |
1.16e-26 |
|
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: 101.58 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 9 KKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKD--SGQVIINEMEYQPKkevmTLKKEVlGFIFQN 85
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPRKPD----QFQKCV-AYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENL---------SITGGKNRKLMIE--HLEEVGmDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:cd03234 90 DILLPGLTVRETLtytailrlpRKSSDAIRKKRVEdvLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDP--EISAKADRIIYIEGGEI 206
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPrsDLFRLFDRILLLSSGEI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
1.74e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.76 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMeyqPKKEVMTLKKEVLGF 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITGG----KNRKL--MIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRyfgmSTREIeaVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGG 204
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-206 |
8.74e-26 |
|
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: 99.61 E-value: 8.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDK--LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN-----EMEYQpkkevmTL 74
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvrDYTLA------SL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVlGFIFQNYLLMeNETVLENLSI-TGGKNRKLMIE-----HLEEV--GMDESY---LAKKVYQLSGGEKQRIAIVRI 143
Cdd:cd03251 75 RRQI-GLVSQDVFLF-NDTVAENIAYgRPGATREEVEEaaraaNAHEFimELPEGYdtvIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIElflALKK--QGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQA---ALERlmKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-206 |
9.93e-26 |
|
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: 99.61 E-value: 9.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVmTLK--KEV 78
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREV-TLDslRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMeNETVLENlsITGGK---NRKLMIE-------HLEEVGMDESY---LAKKVYQLSGGEKQRIAIVRILL 145
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYN--IRYGRpdaTDEEVIEaakaaqiHDKIMRFPDGYdtiVGERGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-206 |
1.01e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.42 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEVMTLKK 76
Cdd:PRK11153 1 MIELKNISKvfpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD------GQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVL-------GFIFQNYLLMENETVLEN----LSITG---GKNRKLMIEHLEEVGMDESylaKKVY--QLSGGEKQRIAI 140
Cdd:PRK11153 75 KELrkarrqiGMIFQHFNLLSSRTVFDNvalpLELAGtpkAEIKARVTELLELVGLSDK---ADRYpaQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 141 VRILLKPFQLLLADEPTGNLDDKNKHKIIELflaLKK----QGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILEL---LKDinreLGLTIVLITHEMDvVKRICDRVAVIDAGRL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-206 |
1.91e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 99.49 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 10 KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII-NEMEYQPKKEVMTLKKEVLGFIFQNYLL 88
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDRKQRRAFRRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MEN--ETV-------LENLSITGGKNRKLMIEH-LEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPT 157
Cdd:TIGR02769 100 AVNprMTVrqiigepLRHLTSLDESEQKARIAElLDMVGLRSEDADKLPRQLSGGQLQRINIARALaVKP-KLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 158 GNLDDKNKHKIIELFLALKKQGKT-IICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-207 |
2.41e-25 |
|
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: 97.82 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDK----LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME-YQPKKEVmtlk 75
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvVKEPAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNYLLMENETVLENLSITG---GKNRKLMIEHLEEV----GMDEsYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAglyGLKGDELTARLEELadrlGMEE-LLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-206 |
2.56e-25 |
|
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: 98.28 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKKEV---LGFI--FQNYLLMEN 91
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG------EDITGLPPHEiarLGIGrtFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENL----------SITGGKNRKLMIEH-------LEEVGMDEsYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLA 153
Cdd:cd03219 90 LTVLENVmvaaqartgsGLLLARARREEREAreraeelLERVGLAD-LADRPAGELSYGQQRRLEIARALaTDP-KLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDvVMSLADRVTVLDQGRV 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-207 |
3.23e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEvMTLKkEVLGFIFQN-YLLme 90
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALR-QAISVVSQRvHLF-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENLSITGGK-NRKLMIEHLEEVGMD---------ESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:PRK11160 427 SATLRDNLLLAAPNaSDEALIEVLQQVGLEklleddkglNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 161 DDKNKHKIIELFLALkKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PRK11160 507 DAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-206 |
3.84e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK---KEVMTLKKEVlGFIFQNYLLMENET 93
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIRPVRKRI-GMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 VLENLSITGGKNRKLMIEH--------LEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEvknyahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 166 HKIIELFLALK-KQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK13646 182 RQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-206 |
3.85e-25 |
|
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: 97.94 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 15 LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKevmTLKKEVlGFIFQNYLLMeNE 92
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPA---WLRRQV-GVVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLENLSITG-GKNRKLMIEHLEEVG-------MDESY---LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:cd03252 91 SIRDNIALADpGMSMERVIEAAKLAGahdfiseLPEGYdtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 162 DKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03252 171 YESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-206 |
7.11e-25 |
|
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: 96.91 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVS-KKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVmtlkKEV 78
Cdd:cd03254 3 IEFENVNfSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdiSRKSL----RSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMeNETVLENLSITGGKNR-KLMIEHLEEVGMD----------ESYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:cd03254 79 IGVVLQDTFLF-SGTIMENIRLGRPNATdEEVIEAAKEAGAHdfimklpngyDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-206 |
7.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEK-----VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK---KEVMT 73
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 74 LKKEV-LGFIFQNYLLMEnETVLE-------NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILL 145
Cdd:PRK13649 83 IRKKVgLVFQFPESQLFE-ETVLKdvafgpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTH-DPEISAKADRIIYIEGGEI 206
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-206 |
7.77e-25 |
|
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: 100.91 E-value: 7.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTL-LNVIGHLDSkdSGQVIINEMEYQ--PKKEVMTLKKEvLGFIFQN-Y------LLM 89
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQDLDglSRRALRPLRRR-MQVVFQDpFgslsprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 90 EnETVLENLSI-----TGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLDDK 163
Cdd:COG4172 382 G-QIIAEGLRVhgpglSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALiLEP-KLLVLDEPTSALDVS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 164 NKHKIIELFLAL-KKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG4172 460 VQAQILDLLRDLqREHGLAYLFISHDLAvVRALAHRVMVMKDGKV 504
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-206 |
7.95e-25 |
|
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: 97.46 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGqviiNEMEYQPKK----EVMTLKK 76
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGERrggeDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EvLGFI---FQNYLlMENETVLENLsITGG------------KNRKLMIEHLEEVGMDEsyLAKKVY-QLSGGEKQRIAI 140
Cdd:COG1119 79 R-IGLVspaLQLRF-PRDETVLDVV-LSGFfdsiglyreptdEQRERARELLELLGLAH--LADRPFgTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 141 VRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQG-KTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEeIPPGITHVLLLKDGRV 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-198 |
8.62e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.48 E-value: 8.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK--KEVMTLKkev 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRDAQAAG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENLSI-----TGGK-NRKLMI----EHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLgreprRGGLiDWRAMRrrarELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRI 198
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRV 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-206 |
1.25e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.03 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-----DSKDSGQVIINEME-YQPKKEVMTLK 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDiYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVlGFIFQ--NYLLMeneTVLEN----LSITGGKNRKLMIEHLEE----VGM-DESY--LAKKVYQLSGGEKQRIAIVR 142
Cdd:COG1117 92 RRV-GMVFQkpNPFPK---SIYDNvaygLRLHGIKSKSELDEIVEEslrkAALwDEVKdrLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 143 IL-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG1117 168 ALaVEP-EVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARvSDYTAFFYLGEL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-206 |
1.40e-24 |
|
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: 100.14 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKT-TLLNVIGHL---DSKDSGQVIINEmeyqpkKEVMTLKKEVL-------- 79
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLpdpAAHPSGSILFDG------QDLLGLSERELrrirgnri 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQ------NYLL-MEN---ETVLENLSITGGKNRKLMIEHLEEVGMDESylAKKV----YQLSGGEKQR--IAIVrI 143
Cdd:COG4172 95 AMIFQepmtslNPLHtIGKqiaEVLRLHRGLSGAAARARALELLERVGIPDP--ERRLdaypHQLSGGQRQRvmIAMA-L 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 144 LLKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG4172 172 ANEP-DLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-206 |
1.57e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.30 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKdsGQVIINEMEYqpKKEVMTLKKEVLGFIFQNYLLME 90
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlGFLPYQ--GSLKINGIEL--RELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 nETVLENLSITggkNRKLMIEHLEEVgMDESYLAKKVYQ---------------LSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK11174 437 -GTLRDNVLLG---NPDASDEQLQQA-LENAWVSEFLPLlpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 156 PTGNLDDKNKHKIIElflALKK--QGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK11174 512 PTASLDAHSEQLVMQ---ALNAasRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-206 |
1.97e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK----KIQdklILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII-----NEMEyqPKKE- 70
Cdd:PRK11650 3 GLKLQAVRKsydgKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvNELE--PADRd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 71 -VMtlkkevlgfIFQNYLLMENETVLENLSItGGKNRKLMIEHLEEVGMD-------ESYLAKKVYQLSGGEKQRIA--- 139
Cdd:PRK11650 78 iAM---------VFQNYALYPHMSVRENMAY-GLKIRGMPKAEIEERVAEaarilelEPLLDRKPRELSGGQRQRVAmgr 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 140 -IVRillKPfQLLLADEPTGNLDDKNKhkiIELFLALKK-Q---GKTIICVTHDpEISAK--ADRIIYIEGGEI 206
Cdd:PRK11650 148 aIVR---EP-AVFLFDEPLSNLDAKLR---VQMRLEIQRlHrrlKTTSLYVTHD-QVEAMtlADRVVVMNGGVA 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-188 |
2.18e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 96.41 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKE-----VMTLK 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEV------LGFIFQNYLLMENETVLENLsITG-----GKNRKLMIEH----LEEVGMDEsylAKKVY--QLSGGEKQRI 138
Cdd:COG4598 88 RQLqrirtrLGMVFQSFNLWSHMTVLENV-IEApvhvlGRPKAEAIERaealLAKVGLAD---KRDAYpaHLSGGQQQRA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 139 AIVRIL-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD 188
Cdd:COG4598 164 AIARALaMEP-EVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-206 |
2.55e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEM---EYQPKKEVMTLKKEVlGFIFQ--NYLLMEnETV 94
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsSTSKQKEIKPVRKKV-GVVFQfpESQLFE-ETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 L-------ENLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHK 167
Cdd:PRK13643 103 LkdvafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489821526 168 IIELFLALKKQGKTIICVTH-DPEISAKADRIIYIEGGEI 206
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-206 |
3.32e-24 |
|
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: 94.04 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEVlGFI---FQNYLLMENET 93
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI-AYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 VLENLSITggknrklmiehleevgmdesylakkvYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFL 173
Cdd:cd03215 95 VAENIALS--------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....
gi 489821526 174 ALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03215 149 ELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-207 |
3.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKL-ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKeVL 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRK-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQN----YLLMENETVL----ENLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK13644 80 GIVFQNpetqFVGRTVEEDLafgpENLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-206 |
5.80e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.85 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME----YQPKKEVMTLKKEV-LGFIFQNYLLMEn 91
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVKRLRKEIgLVFQFPEYQLFQ- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLS---ITGGKNR----KLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKN 164
Cdd:PRK13645 106 ETIEKDIAfgpVNLGENKqeayKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 165 KHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13645 186 EEDFINLFERLnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKV 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-189 |
7.19e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.20 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEvmTLKKEVLGFIFQNYLLMEN 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--DEVRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 eTVLENLSIT-GGKNRKLMIEHLEEVGMdESYLAKKVY-----------QLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:TIGR02868 424 -TVRENLRLArPDATDEELWAALERVGL-ADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 489821526 160 LDDKNKHKIIELFLAlKKQGKTIICVTHDP 189
Cdd:TIGR02868 502 LDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-206 |
8.06e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-----DSKDSGQVIINEMEYQpKKEVMTLKK 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF-KMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVlGFIFQNYLLMENETVLENLSITGGKNR--KLMIEHLEEV--GMDESYLAKKVY--------QLSGGEKQRIAIVRIL 144
Cdd:PRK14247 83 RV-QMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVrwALEKAQLWDEVKdrldapagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 145 LKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARiSDYVAFLYKGQI 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-206 |
1.33e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.89 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKevmtlKKEVLGFIfqNYLLME----N 91
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-----RHTLRQFI--NYLPQEpyifS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSItgGKNRKLMIEHLEEV-----------GMDESY---LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:TIGR01193 562 GSILENLLL--GAKENVSQDEIWAAceiaeikddieNMPLGYqteLSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 158 GNLDDKNKHKIIELFLALKKqgKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-206 |
1.46e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.43 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKD---SGQVIINEMeyqpkkeVMTLKK--EVLGFIFQNYLL 88
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM-------PIDAKEmrAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENETVLENLSI---------TGGKNRKLMIEH-LEEVGmdesyLAK----------KVYQLSGGEKQRIAIVRILLKPF 148
Cdd:TIGR00955 111 IPTLTVREHLMFqahlrmprrVTKKEKRERVDEvLQALG-----LRKcantrigvpgRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDP--EISAKADRIIYIEGGEI 206
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPssELFELFDKIILMAEGRV 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-207 |
2.91e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK------KEVMTL 74
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraasRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEV-LGFIF--QNYLLMENETVLENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK09536 83 PQDTsLSFEFdvRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEIR 207
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVR 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-191 |
4.36e-23 |
|
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: 91.33 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQpKKEVMTLKKEVlGFIFQN---YLLme 90
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgePLDYS-RKGLLERRQRV-GLVFQDpddQLF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLE-------NLSITGGKNRKLMIEHLEEVGMDeSYLAKKVYQLSGGEKQRIAIVRIL-LKPFQLLLaDEPTGNLDD 162
Cdd:TIGR01166 83 AADVDQdvafgplNLGLSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVaMRPDVLLL-DEPTAGLDP 160
|
170 180
....*....|....*....|....*....
gi 489821526 163 KNKHKIIELFLALKKQGKTIICVTHDPEI 191
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-206 |
1.11e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME---YQPK---KEVMTL 74
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvatTPSRelaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEvlgfifqNYLLMeNETVLENLSI-----TGGK----NRKLM---IEHLEEVGMDESYLAkkvyQLSGGEKQR--IAI 140
Cdd:COG4604 81 RQE-------NHINS-RLTVRELVAFgrfpySKGRltaeDREIIdeaIAYLDLEDLADRYLD----ELSGGQRQRafIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 141 V------RILLkpfqlllaDEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDpeI---SAKADRIIYIEGGEI 206
Cdd:COG4604 149 VlaqdtdYVLL--------DEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHD--InfaSCYADHIVAMKDGRV 214
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-206 |
1.33e-22 |
|
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: 94.72 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME-YQPKKEvmTLKKEVlG 80
Cdd:TIGR01842 319 VENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADlKQWDRE--TFGKHI-G 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENeTVLENLSITGGK--NRKL-----------MIEHLEEvGMDeSYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIARFGENadPEKIieaaklagvheLILRLPD-GYD-TVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-207 |
1.38e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.42 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEVMTLKKEVLGF 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD------GKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENL----SITGGKN---RKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIA-IVRILLKPfQLLLA 153
Cdd:cd03269 75 LPEERGLYPKMKVIDQLvylaQLKGLKKeeaRRRIDEWLERLELSE-YANKRVEELSKGNQQKVQfIAAVIHDP-ELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEIR 207
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVLLLNKGRAV 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-188 |
1.96e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEVlGFIFQN-Y---------- 86
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRM-QMVFQDpYaslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 -LLMEnetVLENLSITGGKNRKLMIEH-LEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLDDK 163
Cdd:COG4608 116 dIIAE---PLRIHGLASKAERRERVAElLELVGLRPEHADRYPHEFSGGQRQRIGIARALaLNP-KLIVCDEPVSALDVS 191
|
170 180
....*....|....*....|....*.
gi 489821526 164 NKHKIIELFLALKKQ-GKTIICVTHD 188
Cdd:COG4608 192 IQAQVLNLLEDLQDElGLTYLFISHD 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-206 |
2.22e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpkKEVMT---LKKEV 78
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-------GEDVThrsIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLEN-------LSITGGKNRKLMIEHLEEV---GMDESYlakkVYQLSGGEKQRIAIVRIL-LKP 147
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENvgyglkmLGVPKEERKQRVKEALELVdlaGFEDRY----VDQISGGQQQRVALARALiLKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK11432 156 -KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDqSEAFAVSDTVIVMNKGKI 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-189 |
2.33e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 89.73 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVLGFIFQNYLLMENETVL 95
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG---TPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLS----ITGGKNRKLMiEHLEEVGMDeSYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIEL 171
Cdd:TIGR01189 92 ENLHfwaaIHGGAQRTIE-DALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*...
gi 489821526 172 FLALKKQGKTIICVTHDP 189
Cdd:TIGR01189 170 LRAHLARGGIVLLTTHQD 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
2.97e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.29 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQpKKEVMTLKKE 77
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYD-KKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VlGFIFQNyllMENE----TVLE-------NLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLK 146
Cdd:PRK13639 80 V-GIVFQN---PDDQlfapTVEEdvafgplNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKI 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-207 |
6.51e-22 |
|
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: 89.13 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 9 KKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpkkevmtlkKEVLGFIFQNYLL 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR--------------GRVSSLLGLGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENETVLENLSITG---GKNRKLMIEHLEEVGM---DESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDD 162
Cdd:cd03220 96 NPELTGRENIYLNGrllGLSRKEIDEKIDEIIEfseLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 163 KNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEIR 207
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-206 |
7.68e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 7.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKI---QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPkkEVMTLKKE 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE--ENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGFIFQNyllMENETV-----------LENLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRIL-L 145
Cdd:PRK13650 82 KIGMVFQN---PDNQFVgatveddvafgLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVaM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 146 KPfQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13650 158 RP-KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-206 |
7.84e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEM---EYQPKKevmtLKKE 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQ----LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 vLGFIFQNYLLMENETVLE--------NLSITG---GKNRKLMIEHLEEVGMDEsyLA-KKVYQLSGGEKQRIAIVRILL 145
Cdd:PRK11231 78 -LALLPQHHLTPEGITVRElvaygrspWLSLWGrlsAEDNARVNQAMEQTRINH--LAdRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-206 |
8.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 32 VVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK------------KEVMTLKK--EVLGFIFQ--NYLLMEnETVL 95
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKknnhelitnpysKKIKNFKElrRRVSMVFQfpEYQLFK-DTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 E-------NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKI 168
Cdd:PRK13631 136 KdimfgpvALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190
....*....|....*....|....*....|....*....
gi 489821526 169 IELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHTMEhVLEVADEVIVMDKGKI 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-199 |
8.51e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQViinemeyqpkkEVMTLKKevLGFIFQNYLLMEN--ETV 94
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGAR--VAYVPQRSEVPDSlpLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLSI-----------TGGKNRKLMIEHLEEVGMDEsyLAKK-VYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDD 162
Cdd:NF040873 75 RDLVAMgrwarrglwrrLTRDDRAAVDDALERVGLAD--LAGRqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 489821526 163 KNKHKIIELFLALKKQGKTIICVTHDPEISAKADRII 199
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-206 |
9.18e-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: 89.14 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEVMTLK----KEVLGFIFQNYLL 88
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLD------GVDIRDLNlrwlRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENeTVLENlsITGGKNRKLMiEHLEEV-----------GMDESY---LAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:cd03249 89 FDG-TIAEN--IRYGKPDATD-EEVEEAakkanihdfimSLPDGYdtlVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 155 EPTGNLDDKNKHKIIElflALKK--QGKTIICVTHdpEISA--KADRIIYIEGGEI 206
Cdd:cd03249 165 EATSALDAESEKLVQE---ALDRamKGRTTIVIAH--RLSTirNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-206 |
1.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.47 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTT---LLNVIGHLDSKDSGQVIINEMEYQPKkeVMTLKKEVLGFIFQNyllME 90
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAK--TVWDIREKVGIVFQN---PD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETV-----------LENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:PRK13640 95 NQFVgatvgddvafgLENRAVPRPEMIKIVRDVLADVGMLD-YIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489821526 160 LDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-206 |
2.80e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.21 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 5 VNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQP-----KKEVMTLKKEVl 79
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG---EPlaklnRAQRKAFRRDI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMEN--ETV----------LENLSITGGKNRKLmiEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:PRK10419 92 QMVFQDSISAVNprKTVreiireplrhLLSLDKAERLARAS--EMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKT-IICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-206 |
3.09e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEV-- 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 ----LGFIFQNYLLMENETVLENLSITG---------------GKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIA 139
Cdd:PRK09984 84 sranTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfswftREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 140 IVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-204 |
4.52e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqPKKEVMtlkkevlgFIFQN-YLLME 90
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-----AGARVL--------FLPQRpYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 neTVLENLS---ITGGKNRKLMIEHLEEVGMDesYLAKKVYQ-------LSGGEKQRIAIVRILL-KPfQLLLADEPTGN 159
Cdd:COG4178 441 --TLREALLypaTAEAFSDAELREALEAVGLG--HLAERLDEeadwdqvLSLGEQQRLAFARLLLhKP-DWLFLDEATSA 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 160 LDDKNKHKIIELFLAlKKQGKTIICVTHDPEISAKADRIIYIEGG 204
Cdd:COG4178 516 LDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-207 |
7.48e-21 |
|
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: 89.42 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI--------GH--LDSKDSGQviinemeyqpkkevmtLKKEVLG- 80
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvgvwpptaGSvrLDGADLSQ----------------WDREELGr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIfqNYL-----LMENeTVLENLSitggknR-------------KL-----MIEHLEE-----VGMDESylakkvyQLSG 132
Cdd:COG4618 407 HI--GYLpqdveLFDG-TIAENIA------RfgdadpekvvaaaKLagvheMILRLPDgydtrIGEGGA-------RLSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 133 GEKQRIAIVRILL-KPFQLLLaDEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:COG4618 471 GQRQRIGLARALYgDPRLVVL-DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
8.12e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVLGF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITG------GKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGryfglsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGG 204
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-206 |
8.34e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.66 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSK-DSGQVI-----INEMEyqPKKEVmtlk 75
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKYEvTSGSILldgedILELS--PDERA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQN----------YLLMENETVLENLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQ-LSGGEKQRIAIVRIL 144
Cdd:COG0396 76 RAGIFLAFQYpveipgvsvsNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 145 -LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEI--SAKADRIIYIEGGEI 206
Cdd:COG0396 156 lLEP-KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRIldYIKPDFVHVLVDGRI 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
9.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 9.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQ--DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINE--MEYQPKKEVmtlkK 76
Cdd:PRK13648 7 IIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEKL----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVLGFIFQNyllMENETV-----------LENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILL 145
Cdd:PRK13648 83 KHIGIVFQN---PDNQFVgsivkydvafgLENHAVPYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGK-TIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-206 |
1.89e-20 |
|
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: 85.86 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSkDSGQVIINEMEYQPKKEVmtlkkEV- 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRP-TSGRILFDGRDITGLPPH-----RIa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 -LGFI--FQNYLLMENETVLENLSI-----TGG-----------------KNRKLMIEHLEEVGMDEsYLAKKVYQLSGG 133
Cdd:COG0411 78 rLGIArtFQNPRLFPELTVLENVLVaaharLGRgllaallrlprarreerEARERAEELLERVGLAD-RADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 134 EKQRIAIVRIL-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKK-QGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG0411 157 QQRRLEIARALaTEP-KLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDlVMGLADRIVVLDFGRV 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-205 |
2.09e-20 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 84.44 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 8 SKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDsKDSGQVIINEMeyqpkkevmtlkkevLGFIFQNY 86
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELE-KLSGSVSVPGS---------------IAYVSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 LLMeNETVLENlsITGGKnrKLMIEHLEEV--------------GMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:cd03250 76 WIQ-NGTIREN--ILFGK--PFDEERYEKVikacalepdleilpDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 153 ADEPTGNLDDKNKHKIIE-LFLALKKQGKTIICVTHDPEISAKADRIIYIEGGE 205
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-206 |
3.53e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.33 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKT-TLLNVIGHLDSkdSGQVIINEMEYQ-------PKKEVMTLKKEVLGFIFQNYLL 88
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDY--PGRVMAEKLEFNgqdlqriSEKERRNLVGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENET------VLENLSITGGKNRKLM----IEHLEEVGMD--ESYLAKKVYQLSGGEKQRIAI-VRILLKPfQLLLADE 155
Cdd:PRK11022 101 SLNPCytvgfqIMEAIKVHQGGNKKTRrqraIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIaMAIACRP-KLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 156 PTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEaAHKIIVMYAGQV 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-207 |
4.19e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEV--MTLKKEVlGFIFQNYLLMe 90
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG---VPLVQYdhHYLHRQV-ALVGQEPVLF- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENlsITGGKNRKLMIE----------HLEEVGMDESY---LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:TIGR00958 568 SGSVREN--IAYGLTDTPDEEimaaakaanaHDFIMEFPNGYdteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 158 GNLDDKNKHKIIELflaLKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:TIGR00958 646 SALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-207 |
5.10e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.08 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELvNVSKKIQDkLILEkVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINE-----MEyqpKKEVMTLK 75
Cdd:PRK11144 1 MLEL-NFKQQLGD-LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAE---KGICLPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNYLLMENETVLENLSITGGKNRK---------LMIEHLeevgmdesyLAKKVYQLSGGEKQRIAIVRILLK 146
Cdd:PRK11144 75 KRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVaqfdkivalLGIEPL---------LDRYPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKT-IICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-206 |
7.61e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.12 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-----DSKDSGQV-IINEMEYQPKKEVMTLK 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVrLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVlGFIFQNYLLMENETVLENLSItGGKNRKLM-----IEHLEEVGMDESYLAKKVY--------QLSGGEKQRIAIVR 142
Cdd:PRK14267 85 REV-GMVFQYPNPFPHLTIYDNVAI-GVKLNGLVkskkeLDERVEWALKKAALWDEVKdrlndypsNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 143 IL-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK14267 163 ALaMKP-KILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARvSDYVAFLYLGKL 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-203 |
7.70e-20 |
|
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: 82.20 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKI-QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEME---YQPKKEVM---TL 74
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEdllFLPQRPYLplgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KkEVLgfifqnyllmenetvlenlsitggknrklmiehleevgmdeSYLAKKVyqLSGGEKQRIAIVRILL-KPfQLLLA 153
Cdd:cd03223 81 R-EQL-----------------------------------------IYPWDDV--LSGGEQQRLAFARLLLhKP-KFVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 154 DEPTGNLDDKNKHKIIELflaLKKQGKTIICVTHDPEISAKADRIIYIEG 203
Cdd:cd03223 116 DEATSALDEESEDRLYQL---LKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-207 |
1.10e-19 |
|
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: 83.25 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKdSGQVIIN--EMEYQPKKEVMTLKkevLGFIFQNYLLMENE 92
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTImGLLPPR-SGSIRFDgrDITGLPPHERARAG---IGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLENLsITGGKNRKlmiEHLEEVGMDESY---------LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK 163
Cdd:cd03224 91 TVEENL-LLGAYARR---RAKRKARLERVYelfprlkerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 164 NKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEIR 207
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-206 |
1.24e-19 |
|
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: 83.29 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN-------EMEYQPKKEVMTLKKEVL--GFIF 83
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpisqyEHKYLHSKVSLVGQEPVLfaRSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 84 QN--YLL----MENETVLENLSITGGKNRKLMIEHLEEVGmdesylaKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPT 157
Cdd:cd03248 106 DNiaYGLqscsFECVKEAAQKAHAHSFISELASGYDTEVG-------EKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 158 GNLDDKNKHKiIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03248 179 SALDAESEQQ-VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-207 |
1.34e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKkevmtlKKEVLG 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE------DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 fifqnYL-----LMENETVLENLS-------ITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIA-IVRILLKP 147
Cdd:COG4152 75 -----YLpeergLYPKMKVGEQLVylarlkgLSKAEAKRRADEWLERLGLGD-RANKKVEELSKGNQQKVQlIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821526 148 fQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEIR 207
Cdd:COG4152 149 -ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMElVEELCDRIVIINKGRKV 208
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-207 |
1.44e-19 |
|
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: 82.83 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKevmtLKKevLGF 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD----LHK--IGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITG---GKNRKLMIEHLEEVGMDESYlAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:TIGR03740 75 LIESPPLYENLTARENLKVHTtllGLPDSRIDEVLNIVDLTNTG-KKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 159 NLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHIlSEVQQLADHIGIISEGVLG 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-189 |
1.72e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 85.70 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKD-SGQVIINEMeyQPKKEVMtlkkEVLGFIF 83
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNR--KPTKQIL----KRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 84 QNYLLMENETVLENL----------SITggKNRKLMIEH--LEEVGMD--ESYLAKKVY--QLSGGEKQRIAIVRILLKP 147
Cdd:PLN03211 147 QDDILYPHLTVRETLvfcsllrlpkSLT--KQEKILVAEsvISELGLTkcENTIIGNSFirGISGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDP 189
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-206 |
1.72e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKD-----SGQVIINEME-YQPKKEVMTLKKEVlGFIFQ-- 84
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNiYSPRTDTVDLRKEI-GMVFQqp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 85 NYLLME-NETVLENLSITGGKNRKLMIEHLEE--VGM---DE--SYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEP 156
Cdd:PRK14239 96 NPFPMSiYENVVYGLRLKGIKDKQVLDEAVEKslKGAsiwDEvkDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 157 TGNLDDKNKHKIIELFLALKKQgKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDD-YTMLLVTRSmQQASRISDRTGFFLDGDL 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-206 |
1.87e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 21 SLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpkkeVMTLKKEVLGFIFQNYLLMENETVLENLSI 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT----TTPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 101 -------TGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFL 173
Cdd:PRK10771 95 glnpglkLNAAQREKLHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*
gi 489821526 174 AL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10771 174 QVcQERQLTLLMVSHSLEDAARiAPRSLVVADGRI 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-206 |
2.45e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEM---EYQPKkevmTLKKEVlG 80
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleSWSSK----AFARKV-A 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSIT-----------GGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQ 149
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGrypwhgalgrfGAADREKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARyCDYLVALRGGEM 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-204 |
2.54e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.25 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLL---NVIgHLDSKDS----GQVIINEMEYQPKKEVmtlkkevlGFIFQNYL-L 88
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGI-YLPQRGRvkvmGREVNAENEKWVRSKV--------GLVFQDPDdQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENETVLE-------NLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:PRK13647 92 VFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 162 DKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGG 204
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-189 |
3.41e-19 |
|
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: 81.39 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIineMEYQPKKEVMTLKKEVLGFIFQNYLLMENETVL 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL---LNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLSITGGKNRKLMIEH-LEEVGMDeSYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLA 174
Cdd:cd03231 92 ENLRFWHADHSDEQVEEaLARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|....*
gi 489821526 175 LKKQGKTIICVTHDP 189
Cdd:cd03231 171 HCARGGMVVLTTHQD 185
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-206 |
4.13e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQ--DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKEVl 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DYTLASLRNQV- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMeNETVLENlsITGGKNRKLMIEHLEEVG-----MDesyLAKKVYQ------------LSGGEKQRIAIVR 142
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANN--IAYARTEQYSREQIEEAArmayaMD---FINKMDNgldtvigengvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 143 ILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-206 |
6.84e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEyqpkkeVMTLKKEVL----GFIFQNYLLMeNE 92
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD------IRTVTRASLrrniAVVFQDAGLF-NR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLENLSItgGKnrklmiehlEEVGMDESYLAKKVYQ----------------------LSGGEKQRIAIVRILLKPFQL 150
Cdd:PRK13657 424 SIEDNIRV--GR---------PDATDEEMRAAAERAQahdfierkpdgydtvvgergrqLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-206 |
7.62e-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: 83.70 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK---IQDKLI--LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII---NEMEYQPKKEVM 72
Cdd:TIGR03269 279 IIKVRNVSKRyisVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 73 T--LKKEVLGFIFQNYLLMENETVLENLSITGGKN------RKLMIEHLEEVGMDESY----LAKKVYQLSGGEKQRIAI 140
Cdd:TIGR03269 359 GrgRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLElpdelaRMKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 141 VRILLKPFQLLLADEPTGNLDDKNKHKIIELFL-ALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGKI 506
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-207 |
8.46e-19 |
|
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: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKK----------------------IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQV 58
Cdd:COG1134 4 MIEVENVSKSyrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 59 IINE-----MEyqpkkevmtlkkevLGFIFQNYLlmeneTVLENLSITG---GKNRKLMIEHLEEV----GMDEsYLAKK 126
Cdd:COG1134 84 EVNGrvsalLE--------------LGAGFHPEL-----TGRENIYLNGrllGLSRKEIDEKFDEIvefaELGD-FIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 127 VYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGE 205
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGaVRRLCDRAIWLEKGR 223
|
..
gi 489821526 206 IR 207
Cdd:COG1134 224 LV 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-206 |
1.05e-18 |
|
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: 80.62 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD--KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVmtlkKE 77
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDL----RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGFIFQNYLLMENeTVLENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQL-----------SGGEKQRIAIVRILLK 146
Cdd:cd03244 79 RISIIPQDPVLFSG-TIRSNLDPFGEYSDEELWQALERVGLKE-FVESLPGGLdtvveeggenlSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821526 147 PFQLLLADEPTGNLD---DKNKHKIIELFLAlkkqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03244 157 KSKILVLDEATASVDpetDALIQKTIREAFK----DCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-206 |
1.25e-18 |
|
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: 83.33 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVmTLK--KEVLGFIFQNYLLMe 90
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG---QDIRDV-TQAslRAAIGIVPQDTVLF- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENL-------------------SITGgknrklMIEHLEE-----VGmdESYLakkvyQLSGGEKQRIAIVRILLK 146
Cdd:COG5265 445 NDTIAYNIaygrpdaseeeveaaaraaQIHD------FIESLPDgydtrVG--ERGL-----KLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIElflALKK--QGKTIICVTHdpEIS--AKADRIIYIEGGEI 206
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQA---ALREvaRGRTTLVIAH--RLStiVDADEILVLEAGRI 570
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-203 |
1.37e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 80.28 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 22 LSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVmtlkkevLGFIFQ------NYLLMENETVL 95
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-------IGYVPQrhefawDFPISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLS-ITGGKNRKLMIEH------LEEVGMDEsyLAKK-VYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLDDKNKH 166
Cdd:TIGR03771 74 SGRTgHIGWLRRPCVADFaavrdaLRRVGLTE--LADRpVGELSGGQRQRVLVARALaTRP-SVLLLDEPFTGLDMPTQE 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 489821526 167 KIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEG 203
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDlAQAMATCDRVVLLNG 188
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-188 |
1.50e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.08 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLI--LEKVSLSIGAGEFIAVVGESGSGKT-TLLNVIGHLDS--KDSGQVIINEMEY--QPKKEVMTLKKEV 78
Cdd:PRK09473 19 RVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREIlnLPEKELNKLRAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMEN------ETVLENLSITGGKNRKLMIEH----LEEVGMDESYLAKKVY--QLSGGEKQRIAIVRILLK 146
Cdd:PRK09473 99 ISMIFQDPMTSLNpymrvgEQLMEVLMLHKGMSKAEAFEEsvrmLDAVKMPEARKRMKMYphEFSGGMRQRVMIAMALLC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKT-IICVTHD 188
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-204 |
1.58e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKT-TLLNVIGHLDSKD----SGQVIIN--EMEYQPKKEVMTLKKEVLGFIFQ 84
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHgeSLLHASEQTLRGVRGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 85 ------NYLLMENETVLENLSITGGKNRKL----MIEHLEEVGMDE--SYLAKKVYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:PRK15134 100 epmvslNPLHTLEKQLYEVLSLHRGMRREAargeILNCLDRVGIRQaaKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 153 ADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGG 204
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-207 |
2.04e-18 |
|
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: 79.72 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemEYQPKKEVMTLKKeVLGF 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA--GHDVVREPREVRR-RIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITG------GKNRKLMI-EHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHArlygvpGAERRERIdELLDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKK-QGKTIICVTHDPEISAK-ADRIIYIEGGEIR 207
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-206 |
2.18e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.00 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 7 VSKKIQDKLILEKVSLSIGA---------GEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQ--PKKEVMTLK 75
Cdd:PRK10070 25 IEQGLSKEQILEKTGLSLGVkdaslaieeGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNYLLMENETVLENLS-------ITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAfgmelagINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALK-KQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRiGDRIAIMQNGEV 243
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-206 |
2.41e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.36 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHL---------DSKDSGQVIINEMeyqPKKEVMTLK 75
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLapdagevhyRMRDGQLRDLYAL---SEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNY---LLME-----NetVLENLSITG----GKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:PRK11701 88 RTEWGFVHQHPrdgLRMQvsaggN--IGERLMAVGarhyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEIsAK--ADRIIYIEGGEI 206
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAV-ARllAHRLLVMKQGRV 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-206 |
6.29e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.32 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 11 IQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-DSKDSGQVIINEMEYQPKK----EVMTLKKEVlGFIFQN 85
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLYFGKDifqiDAIKLRKEV-GMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENLSIT----GGKNR----KLMIEHLEEVGM-DESY--LAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLA 153
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPlkshGIKEKreikKIVEECLRKVGLwKEVYdrLNSPASQLSGGQQQRLTIARALaLKP-KVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARvADYVAFLYNGEL 230
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-204 |
1.03e-17 |
|
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: 77.28 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 7 VSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGhlDSKDSGqVIINEMEYQPKKEVMTLKKEVlGFIFQNY 86
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAG-VITGEILINGRPLDKNFQRST-GYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 LLMENETVLENLSITgGKNRKLMIEHleevgmdesylakkvyqlsggeKQRIAI-VRILLKPfQLLLADEPTGNLDDKNK 165
Cdd:cd03232 89 VHSPNLTVREALRFS-ALLRGLSVEQ----------------------RKRLTIgVELAAKP-SILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 166 HKIIELFLALKKQGKTIICVTHDPEIS--AKADRIIYIEGG 204
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-206 |
2.20e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKT-TLLNVIGHLDS---KDSGQVIINEMEYQPKkevmTLKKEVLGFIFQ---- 84
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPC----ALRGRKIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 85 --NYLLMENETVLENLSITGG-KNRKLMIEHLEEVGMDESYLAKKVY--QLSGGEKQRIAIVRILL--KPFqlLLADEPT 157
Cdd:PRK10418 91 afNPLHTMHTHARETCLALGKpADDATLTAALEAVGLENAARVLKLYpfEMSGGMLQRMMIALALLceAPF--IIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 158 GNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARlADDVAVMSHGRI 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-205 |
2.73e-17 |
|
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: 79.48 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIG--HLDSKDSGQVIINEMEYQPKKEVMTLKKEV 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LgFIFQNYLLMENETVLEN------LSITGGK-NRKLMI----EHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:TIGR02633 81 V-IIHQELTLVPELSVAENiflgneITLPGGRmAYNAMYlrakNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGE 205
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-189 |
3.61e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTlkkevlgfifqnYL--- 87
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDggDIDDPDVAEACH------------YLghr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 88 --LMENETVLENLS----ITGGKNRKLMiEHLEEVGMDEsyLAKKVYQ-LSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:PRK13539 82 naMKPALTVAENLEfwaaFLGGEELDIA-AALEAVGLAP--LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*....
gi 489821526 161 DDKNKHKIIELFLALKKQGKTIICVTHDP 189
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
6.85e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYqPKKEVMTLKKEVLG 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSITGGKNRKLM--------------IEHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLK 146
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKVCgvniidwremrvraAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 147 PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGG 204
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-206 |
7.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmEYQPKKEVMTLKKEVlGFIFQNYLLMENETVLE 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG-ELLTAENVWNLRRKI-GMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 97 NLSITGGKN----RKLMIEHLEEVGMDESYL---AKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKII 169
Cdd:PRK13642 101 DDVAFGMENqgipREEMIKRVDEALLAVNMLdfkTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 489821526 170 ELFLALK-KQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK13642 181 RVIHEIKeKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-198 |
1.36e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLdSKDSGQVIINEMEYQ--------PKKEVMTLKKEVlGFIFQN-- 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNgidllklsPRERRKIIGREI-AMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 -YL---------LMEnetVLENLSITG------GKNRKLMIEHLEEVG--MDESYLAKKVYQLSGGEKQRIAIVRILLKP 147
Cdd:COG4170 100 sCLdpsakigdqLIE---AIPSWTFKGkwwqrfKWRKKRAIELLHRVGikDHKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 148 FQLLLADEPTGNLDDKNKHKIIELFLALKK-QGKTIICVTHDPE-ISAKADRI 198
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLEsISQWADTI 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-206 |
1.37e-16 |
|
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: 74.89 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKEVLGF 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSI---TGGKNRKLMIEHLEEVgMDESYLAK----KVYQLSGGEKQRIAIVRIL-LKPFQLLLa 153
Cdd:cd03218 80 LPQEASIFRKLTVEENILAvleIRGLSKKEREEKLEEL-LEEFHITHlrksKASSLSGGERRRVEIARALaTNPKFLLL- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-200 |
2.03e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLnvighldskdsgQVIINEMEYQPKKEVMTLKKEVLGf 81
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLL------------RLLAGALKGTPVAGCVDVPDNQFG- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 ifqnyllmENETVLENLSITGGKNRKlmIEHLEEVGMDESYLAKKVY-QLSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:COG2401 98 --------REASLIDAIGRKGDFKDA--VELLNAVGLSDAVLWLRRFkELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 161 DDKN----KHKIIELflaLKKQGKTIICVTHDPEISA--KADRIIY 200
Cdd:COG2401 168 DRQTakrvARNLQKL---ARRAGITLVVATHHYDVIDdlQPDLLIF 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-206 |
3.75e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.08 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkevmtlkKEVLGF 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE-------------NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQN--YLLMENETVLE-----------NLSITGGKNRKLMiehleevGMDEsyLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PRK15064 387 YAQDhaYDFENDLTLFDwmsqwrqegddEQAVRGTLGRLLF-------SQDD--IKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNkhkiIE-LFLALKKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:PRK15064 458 NVLVMDEPTNHMDMES----IEsLNMALEKYEGTLIFVSHDREfVSSLATRIIEITPDGV 513
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-198 |
3.97e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEVlGFI 82
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV-AII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQNYLLMENETVLENL------SITGGKNRKLMIEH----LEEVGMDESYLAkKVYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:PRK11288 85 YQELHLVPEMTVAENLylgqlpHKGGIVNRRLLNYEareqLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489821526 153 ADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRI 198
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRmEEIFALCDAI 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-191 |
4.15e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 9 KKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTT----LLNVIghldsKDSGQVIINEMEYQ--PKKEVMTLKKEVlGF 81
Cdd:PRK15134 293 KRTVDhNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHnlNRRQLLPVRHRI-QV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQ------NYLLMENETVLENL-----SITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQ 149
Cdd:PRK15134 367 VFQdpnsslNPRLNVLQIIEEGLrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALiLKP-S 445
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGK-TIICVTHDPEI 191
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHV 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-206 |
4.33e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKiqDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEvLGFI 82
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG-MAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 ---------FQNYLLMENETVLENLSITGGKNRKLMIEHLEEVGMDE----------SYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:PRK09700 344 tesrrdngfFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAEnqrellalkcHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-206 |
5.55e-16 |
|
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: 73.52 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 7 VSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemEYQPKKEVMTLKKEvLGFIF-QN 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA--GLVPWKRRKKFLRR-IGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENLS-------ITGGKNRKlMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:cd03267 104 TQLWWDLPVIDSFYllaaiydLPPARFKK-RLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 159 NLDDKNKHKIIELFLAL-KKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-206 |
8.63e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSK---KIQdklILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKEVMtlk 75
Cdd:PRK11614 5 MLSFDKVSAhygKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdgKDITDWQTAKIM--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVLGFIFQNYLLMENETVLENLSITG-GKNRKLMIEHLEEVGMDESYLAKKVYQ----LSGGEKQRIAIVRILLKPFQL 150
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGfFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
8.98e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.97 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkevmTLKkevLGF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----------TVK---LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNY-LLMENETVLEnlSITGGknrklmIEHLeEVGMDE----SYLA----------KKVYQLSGGEKQRIAIVRILLK 146
Cdd:TIGR03719 390 VDQSRdALDPNKTVWE--EISGG------LDII-KLGKREipsrAYVGrfnfkgsdqqKKVGQLSGGERNRVHLAKTLKS 460
|
170
....*....|....*
gi 489821526 147 PFQLLLADEPTGNLD 161
Cdd:TIGR03719 461 GGNVLLLDEPTNDLD 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-188 |
9.07e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.97 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKIQ-DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII----------NEMEYQPKKEVM 72
Cdd:TIGR03719 7 MNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikvgylpQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 73 TLKKEVLGFIFQnyLLMENETVLENLSITGGKNRKLMIEHLE-----------------EVGMDESYLA---KKVYQLSG 132
Cdd:TIGR03719 87 ENVEEGVAEIKD--ALDRFNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsqlEIAMDALRCPpwdADVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 133 GEKQRIAIVRILLKPFQLLLADEPTGNLDDKNkhkIIELFLALKKQGKTIICVTHD 188
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-188 |
9.65e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII-----------NEMEYQPKKEVMTLKKEVLgfiFQN 85
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqptrqalqkNLVAYVPQSEEVDWSFPVL---VED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMENETVLENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|...
gi 489821526 166 HKIIELFLALKKQGKTIICVTHD 188
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHN 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-206 |
4.55e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmEYQPKKEVMTLKKEVlGFIFQNYLLMENE 92
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG-EPITKENIREVRKFV-GLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLENLSITGGKNRKL---MIEH-----LEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKN 164
Cdd:PRK13652 94 PTVEQDIAFGPINLGLdeeTVAHrvssaLHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 165 KHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13652 173 VKELIDFLNDLPETyGMTVIFSTHQLDLVPEmADYIYVMDKGRI 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-205 |
4.70e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKT----TLLNVI----------GHLDSKDSGQVIinEMEYQPKKEVMTLKKEVLGFI 82
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqcdKMLLRRRSRQVI--ELSEQSAAQMRHVRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQ------NYLLMENETVLENLSITGGKNR-KLMIE---HLEEVGMDESY--LAKKVYQLSGGEKQRIAIVRILLKPFQL 150
Cdd:PRK10261 110 FQepmtslNPVFTVGEQIAESIRLHQGASReEAMVEakrMLDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 151 LLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHDPEISAK-ADRIIYIEGGE 205
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEiADRVLVMYQGE 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-188 |
4.79e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.30 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEVlGFIFQNYLLMEN--- 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqDLLKADPEAQKLLRQKI-QIVFQNPYGSLNprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 --ETVLE-----NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLDDK 163
Cdd:PRK11308 110 kvGQILEeplliNTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALmLDP-DVVVADEPVSALDVS 188
|
170 180
....*....|....*....|....*.
gi 489821526 164 NKHKIIELFLALKKQ-GKTIICVTHD 188
Cdd:PRK11308 189 VQAQVLNLMMDLQQElGLSYVFISHD 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
7.11e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQViinEMEYQP-KKEVMTLKKEvL 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI---LFERQSiKKDLCTYQKQ-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENETVLEN----LSITGGknrKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENclydIHFSPG---AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKAD 196
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-205 |
7.38e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKD-SGQVIINEMEYQPKKEVMTLKKEV 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTyEGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LgFIFQNYLLMENETVLENL----SITGGK--NRKLMI----EHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PRK13549 85 A-IIHQELALVKELSVLENIflgnEITPGGimDYDAMYlraqKLLAQLKLDIN-PATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGE 205
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-206 |
1.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.65 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQpKKEVMTLKKEVlGFIFQ---NYLLmeN 91
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYS-RKGLMKLRESV-GMVFQdpdNQLF--S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSItGGKNRKL-------MIEH-LEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK 163
Cdd:PRK13636 98 ASVYQDVSF-GAVNLKLpedevrkRVDNaLKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 164 NKHKIIELFLALKKQ-GKTIICVTHDPEISA-KADRIIYIEGGEI 206
Cdd:PRK13636 176 GVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-188 |
1.14e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEVlGFIFQN--------- 85
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqRIDTLSPGKLQALRRDI-QFIFQDpyasldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 ---YLLMENETVlENLsITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLD 161
Cdd:PRK10261 419 tvgDSIMEPLRV-HGL-LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALaLNP-KVIIADEAVSALD 495
|
170 180
....*....|....*....|....*...
gi 489821526 162 DKNKHKIIELFLALKKQ-GKTIICVTHD 188
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHD 523
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-197 |
1.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 5 VNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSK-----DSGQVIINEMEYQPKKEVMTLKKEVl 79
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQ--NYLLMeneTVLENLsITGGKNRKLMIE---------HLEEVGMDESY---LAKKVYQLSGGEKQRIAIVRILL 145
Cdd:PRK14271 104 GMLFQrpNPFPM---SIMDNV-LAGVRAHKLVPRkefrgvaqaRLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 146 KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK-ADR 197
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARiSDR 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-207 |
1.57e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTL---LNVIGHLDS--KDSGQV-IINEMEYQPKKEVMTLK 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESevRVEGRVeFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEV-LGFIFQNYLLMeneTVLENLSI---TGGKNRKLMIEHLEEVGM------DE--SYLAKKVYQLSGGEKQRIAIVRI 143
Cdd:PRK14258 88 RQVsMVHPKPNLFPM---SVYDNVAYgvkIVGWRPKLEIDDIVESALkdadlwDEikHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 144 L-LKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGK-TIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:PRK14258 165 LaVKP-KVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRLSDFTAFFKGNENR 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-206 |
4.32e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVmtlkKEVLGFIFQNYLLMEN 91
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgeHIQHYASKEV----ARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSITGGKNRKLMIEHLEEvgmDESYLAK-------------KVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWRKE---DEEAVTKamqatgithladqSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 159 NLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRyASHLIALREGKI 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-188 |
6.21e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKI-QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIInemeyQPKKEVmtlkkevlGFI 82
Cdd:PRK11819 9 MNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----APGIKV--------GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQNYLLMENETVLENL-----SITGGKNR----------------KLM---------IEHLE--------EVGMDesylA 124
Cdd:PRK11819 76 PQEPQLDPEKTVRENVeegvaEVKAALDRfneiyaayaepdadfdALAaeqgelqeiIDAADawdldsqlEIAMD----A 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 125 -------KKVYQLSGGEKQRIAIVRILL-KPfQLLLADEPTGNLDDKNKHkIIELFLAlKKQGkTIICVTHD 188
Cdd:PRK11819 152 lrcppwdAKVTKLSGGERRRVALCRLLLeKP-DMLLLDEPTNHLDAESVA-WLEQFLH-DYPG-TVVAVTHD 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-188 |
6.40e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 3 ELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNV-IGHLDSkDSGQViinemeyqpkkEVMTlKKEVLGF 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRI-----------HCGT-KLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLS------ITGGKNRKLMiehleevgmdeSYLA------KK----VYQLSGGEKQRIAIVRILL 145
Cdd:PRK11147 388 DQHRAELDPEKTVMDNLAegkqevMVNGRPRHVL-----------GYLQdflfhpKRamtpVKALSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489821526 146 KPFQLLLADEPTGNLDdknkhkiIELFLALKK-----QGkTIICVTHD 188
Cdd:PRK11147 457 KPSNLLILDEPTNDLD-------VETLELLEElldsyQG-TVLLVSHD 496
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-196 |
9.87e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKKEv 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIPAMSRSRLYTVRKR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGFIFQNYLLMENETVLENLSITGGKNRKL--------MIEHLEEVGMDESylAK-KVYQLSGGEKQRIAIVR-ILLKPf 148
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLpapllhstVMMKLEAVGLRGA--AKlMPSELSGGMARRAALARaIALEP- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 149 QLLLADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKAD 196
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDvPEVLSIAD 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-161 |
9.89e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemeyqpKKEVMTLKKEVlgfiFQNYL----- 87
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID------GKTATRGDRSR----FMAYLghlpg 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 88 LMENETVLENL----SITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:PRK13543 93 LKADLSTLENLhflcGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-206 |
1.68e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPKKEVMTLKKEVLG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG---NPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 --FIFQNYLLMENETVLENLSITGGKNRKL---MIEHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENILFGLPKRQASmqkMKQLLAALGCQLD-LDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-206 |
3.31e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeYQPKKEVMTLKKEVLGFIFQNYLLMENE-----TV 94
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--HPLHFGDYSYRSQRIRMIFQDPSTSLNPrqrisQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LE-----NLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKII 169
Cdd:PRK15112 110 LDfplrlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 489821526 170 ELFLALK-KQGKTIICVT-HDPEISAKADRIIYIEGGEI 206
Cdd:PRK15112 190 NLMLELQeKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-206 |
3.92e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTLKKEVL----GFIFQNYLL 88
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG------RPLSSLSHSVLrqgvAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MEnETVLENlsITGGKN--RKLMIEHLEEVGMDE----------SYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEP 156
Cdd:PRK10790 427 LA-DTFLAN--VTLGRDisEEQVWQALETVQLAElarslpdglyTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489821526 157 TGNLDDKNKhKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK10790 504 TANIDSGTE-QAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
4.83e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkkevmTLKkevLGF 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----------TVK---LAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENE-TVLENlsITGGknrklmIEHLeEVGMDE----SYLA----------KKVYQLSGGEKQRIAIVRILLK 146
Cdd:PRK11819 392 VDQSRDALDPNkTVWEE--ISGG------LDII-KVGNREipsrAYVGrfnfkggdqqKKVGVLSGGERNRLHLAKTLKQ 462
|
170
....*....|....*
gi 489821526 147 PFQLLLADEPTGNLD 161
Cdd:PRK11819 463 GGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-204 |
5.20e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 10 KIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGhlDSKDSGQVIINEMEYQPKKEVMTLKKEVlGFIFQNYLLM 89
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLDSSFQRSI-GYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 90 ENETVLENL----------SITggknRKLMIEHLEEV----GMdESYlAKKVYQLSGG-----EKQRIAI-VRILLKPFQ 149
Cdd:TIGR00956 849 PTSTVRESLrfsaylrqpkSVS----KSEKMEYVEEVikllEM-ESY-ADAVVGVPGEglnveQRKRLTIgVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPE--ISAKADRIIYIEGG 204
Cdd:TIGR00956 923 LLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-206 |
5.25e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKdsGQVIINEM---EYQP----KKEVMTLKKEVLGFI---FQnYLL 88
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMaGLLPGQ--GEILLNGRplsDWSAaelaRHRAYLSQQQSPPFAmpvFQ-YLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 M---------ENETVLENLSitggknRKLMIEhleevgmdeSYLAKKVYQLSGGEKQRIAIVRILLK------PF-QLLL 152
Cdd:COG4138 92 LhqpagasseAVEQLLAQLA------EALGLE---------DKLSRPLTQLSGGEWQRVRLAAVLLQvwptinPEgQLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 153 ADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRhADRVWLLKQGKL 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-203 |
6.46e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.51 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 21 SLSIGAGEF-----IAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPK----KEVMT----LKKEVLGFIFQN 85
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIelDTVSYKPQyikaDYEGTvrdlLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YLLMEnetVLENLSItggknrklmiehleevgmdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:cd03237 94 YFKTE---IAKPLQI-------------------EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489821526 166 ---HKIIELFlALKKQgKTIICVTHD-PEISAKADRIIYIEG 203
Cdd:cd03237 152 lmaSKVIRRF-AENNE-KTAFVVEHDiIMIDYLADRLIVFEG 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
110-206 |
7.44e-13 |
|
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: 64.97 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 110 IEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVR-ILLKPFQLL-LADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTH 187
Cdd:cd03270 118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATqIGSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
90 100
....*....|....*....|....*
gi 489821526 188 DPEISAKADRIIYI------EGGEI 206
Cdd:cd03270 198 DEDTIRAADHVIDIgpgagvHGGEI 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-206 |
1.02e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKevlGFIF-----QNYLLMENETV 94
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA---GIAYvpedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLSIT--------GGKNRKLMIEHLEEVgMDE-----SYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:COG1129 348 RENITLAsldrlsrgGLLDRRRERALAEEY-IKRlriktPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 162 DKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:COG1129 427 VGAKAEIYRLIRELAAEGKAVIVISSElPELLGLSDRILVMREGRI 472
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-187 |
1.68e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVI-----INEMEYQPKKEVMTLK 75
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 -----KEVLgfifqnyllmeneTVLENL----SITGGKNRKLMIEHLEEVGMD--ESYLAKkvyQLSGGEKQRIAIVRIL 144
Cdd:PRK13538 81 hqpgiKTEL-------------TALENLrfyqRLHGPGDDEALWEALAQVGLAgfEDVPVR---QLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 145 LKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTH 187
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-188 |
3.29e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKEVMTLKKEVlGFIFQNYLLMEN------ 91
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgKDLLGMKDDEWRAVRSDI-QMIFQDPLASLNprmtig 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSI-----TGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRIL-LKPfQLLLADEPTGNLDDKNK 165
Cdd:PRK15079 119 EIIAEPLRTyhpklSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALiLEP-KLIICDEPVSALDVSIQ 197
|
170 180
....*....|....*....|....
gi 489821526 166 HKIIELFLALKKQ-GKTIICVTHD 188
Cdd:PRK15079 198 AQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-206 |
3.58e-12 |
|
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: 61.96 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGhldsKDSGQVIINemeyqpkKEVMTLKKEVLGFIFQnyllmenetvLE 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI-------SFLPKFSRNKLIFIDQ----------LQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 97 NLSitggknrklmiehleEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQ--LLLADEPTGNLDDKNKHKIIELFLA 174
Cdd:cd03238 70 FLI---------------DVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 489821526 175 LKKQGKTIICVTHDPEISAKADRIIYI------EGGEI 206
Cdd:cd03238 135 LIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKV 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-207 |
4.43e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLN-VIGHLDSKDSGQVIIN-EMEYQPKkevmtlkkevLGFIFqnyllme 90
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRgSVAYVPQ----------VSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENLsITGGK------NRKLMIEHLEE-----VGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:PLN03232 692 NATVRENI-LFGSDfeseryWRAIDVTALQHdldllPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489821526 160 LDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-207 |
5.20e-12 |
|
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: 64.05 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyQPkkevmtLKKEVLG-----F--IFQNYLLMEne 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG---QP------VTADNREayrqlFsaVFSDFHLFD-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 tvlENLSITGGKNRKLMIEHLEEVGMDEsylakKV---------YQLSGGEKQRIAIVRILL--KPFQLLlaDE------ 155
Cdd:COG4615 420 ---RLLGLDGEADPARARELLERLELDH-----KVsvedgrfstTDLSQGQRKRLALLVALLedRPILVF--DEwaadqd 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489821526 156 PTgnlddkNKHKIIELFL-ALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:COG4615 490 PE------FRRVFYTELLpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-161 |
7.59e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 62.29 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQPKKEVMTLKkevLGFIF 83
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqDITHLPMHERARLG---IGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 84 QNYLLMENETVLEN----LSITGGKNRKLMIEHLEEVgMDESYLA----KKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:TIGR04406 83 QEASIFRKLTVEENimavLEIRKDLDRAEREERLEAL-LEEFQIShlrdNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
....*.
gi 489821526 156 PTGNLD 161
Cdd:TIGR04406 162 PFAGVD 167
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-206 |
1.01e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHL-------DSKDSGQVIIN-EMEYQPKKEVMTLKKEVL------G 80
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLtgggaprGARVTGDVTLNgEPLAAIDAPRLARLRAVLpqaaqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQnyllmENETVL-------ENLSITGGKNRKLMIEHLEEVGMDeSYLAKKVYQLSGGEKQRIAIVRILLK------- 146
Cdd:PRK13547 96 FAFS-----AREIVLlgryphaRRAGALTHRDGEIAWQALALAGAT-ALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 147 --PFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKT-IICVTHDPEISAK-ADRIIYIEGGEI 206
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARhADRIAMLADGAI 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-187 |
1.44e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHldskDSGQVIINEMEYQpKKEVMTLKKEV- 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGH----PAYKILEGDILFK-GESILDLEPEEr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 --LGFI--FQNYLLMENETVLENLSITGGKNRK--------------LMIEHLEEVGMDESYLAKKVYQ-LSGGEKQRIA 139
Cdd:CHL00131 82 ahLGIFlaFQYPIEIPGVSNADFLRLAYNSKRKfqglpeldplefleIINEKLKLVGMDPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 140 IVR-ILLKPfQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTH 187
Cdd:CHL00131 162 ILQmALLDS-ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-201 |
1.46e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN--EMEYQpKKEVMTLKKEV 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkPLDYS-KRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 lGFIFQN------YLLMENETV--LENLSITGGKNRKLMIEHLEEVgmDESYLAKKVYQ-LSGGEKQRIAIVRILLKPFQ 149
Cdd:PRK13638 80 -ATVFQDpeqqifYTDIDSDIAfsLRNLGVPEAEITRRVDEALTLV--DAQHFRHQPIQcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489821526 150 LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYI 201
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYV 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-204 |
1.60e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVI----------------GHL-------DSKDSGQVIINemeyqpkkevmt 73
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsyegeilfdGEVcrfkdirDSEALGIVIIH------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 74 lkkevlgfifQNYLLMENETVLENLSITGGKNRKLMI----------EHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRI 143
Cdd:NF040905 85 ----------QELALIPYLSIAENIFLGNERAKRGVIdwnetnrrarELLAKVGLDES-PDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821526 144 LLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGG 204
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-198 |
1.61e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLdSKDSGQVIINEMEYQpKKEVMTL----KKEVLG----FIFQ--NY 86
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFD-DIDLLRLspreRRKLVGhnvsMIFQepQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 LLMENETVLENL--SITG-----------GKNRKLMIEHLEEVGMDESYLAKKV--YQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK15093 101 CLDPSERVGRQLmqNIPGwtykgrwwqrfGWRKRRAIELLHRVGIKDHKDAMRSfpYELTEGECQKVMIAIALANQPRLL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLAL-KKQGKTIICVTHDPEISAK-ADRI 198
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQwADKI 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-206 |
1.66e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.03 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEyqPKKEVMTLKKEVlGFIF-QNYLLMENETVLENL 98
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV--PFKRRKEFARRI-GVVFgQRSQLWWDLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 99 SITG----------GKNRKLMIEHLEEvgmdESYLAKKVYQLSGGEKQRIAIVRILL-KPfQLLLADEPTGNLDDKNKHK 167
Cdd:COG4586 118 RLLKaiyripdaeyKKRLDELVELLDL----GELLDTPVRQLSLGQRMRCELAAALLhRP-KILFLDEPTIGLDVVSKEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 168 IIELFLAL-KKQGKTIICVTHDPE-ISAKADRIIYIEGGEI 206
Cdd:COG4586 193 IREFLKEYnRERGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-206 |
1.98e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLN-VIGHLDsKDSGQVIIN-EMEYQPKKEVM---TLKKEVL-GFIFQ-NYL-- 87
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMD-KVEGHVHMKgSVAYVPQQAWIqndSLRENILfGKALNeKYYqq 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 88 LMENETVLENLSITGGKNRKlmiehleEVGmdesylaKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHK 167
Cdd:TIGR00957 733 VLEACALLPDLEILPSGDRT-------EIG-------EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 168 IIELFLALKK--QGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:TIGR00957 799 IFEHVIGPEGvlKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-201 |
2.75e-11 |
|
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: 59.30 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHldskdsgqviinemeyqpkkevmtlkkevlgfifqnyllmenet 93
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGL-------------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 vlenlsITGGKNRKLMIEHLEEVGMDESY----LAKKVYQLSGGEKQRIAIVRIL----LKPFQLLLADEPTGNLDDKNK 165
Cdd:cd03227 44 ------ALGGAQSATRRRSGVKAGCIVAAvsaeLIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 489821526 166 HKIIELFLALKKQGKTIICVTHDPEISAKADRIIYI 201
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-204 |
2.77e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKDSGQVIINEMEYQPKKE-VM--TLKKEVL-GFIFQNYL--- 87
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPSEGKIKHSGRISFSPQTSwIMpgTIKDNIIfGLSYDEYRyts 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 88 LMENETVLENLSITGGKnrklmiehleevgmDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHK 167
Cdd:TIGR01271 521 VIKACQLEEDIALFPEK--------------DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*..
gi 489821526 168 IIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGG 204
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-206 |
2.96e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKE-------------VLGF-I 82
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGivyisedrkrdglVLGMsV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQNYLLmeneTVLENLSITGGKnrklmIEHLEEVGMDESYLA----------KKVYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:PRK10762 348 KENMSL----TALRYFSRAGGS-----LKHADEQQAVSDFIRlfniktpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 153 ADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-206 |
3.11e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSK-DSGQVI-----INEMEYQPKkevmtl 74
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKYEvTEGEILfkgedITDLPPEER------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 75 KKEVLGFIFQnyllmenetvlENLSITGGKNRKLmiehLEEVGmdesylakkvYQLSGGEKQRIAIVRIL-LKPfQLLLA 153
Cdd:cd03217 75 ARLGIFLAFQ-----------YPPEIPGVKNADF----LRYVN----------EGFSGGEKKRNEILQLLlLEP-DLAIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISA--KADRIIYIEGGEI 206
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRI 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-206 |
3.31e-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: 61.95 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMtlkKEVLGFIFQNYLLMENETVLE 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV---RQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 97 NL----SITGGKNRKLMIEH---LEEVGMDESYlAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKII 169
Cdd:TIGR01257 1023 HIlfyaQLKGRSWEEAQLEMeamLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*...
gi 489821526 170 ELFLALkKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-206 |
3.71e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 18 EKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEV------MTL-----KKEvlGFIfqny 86
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagIMLcpedrKAE--GII---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 llmENETVLENLSITGGKNR---KLMIEHLEEVGMDESYLAK----------KVYQLSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:PRK11288 344 ---PVHSVADNINISARRHHlraGCLINNRWEAENADRFIRSlniktpsreqLIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRI 474
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-156 |
3.98e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.04 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmeyqpkKEVMTL---KKE 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG------EDITHLpmhKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGF--------IFQNyLlmeneTVLENLSI---TGGKNRKLMIEHLEEVgMDE---SYLAK-KVYQLSGGEKQRIAIVR 142
Cdd:COG1137 77 RLGIgylpqeasIFRK-L-----TVEDNILAvleLRKLSKKEREERLEEL-LEEfgiTHLRKsKAYSLSGGERRRVEIAR 149
|
170
....*....|....*
gi 489821526 143 IL-LKPfQLLLADEP 156
Cdd:COG1137 150 ALaTNP-KFILLDEP 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
77-206 |
4.62e-11 |
|
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: 61.18 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 77 EVLGFIFQNYLLMENETVLENLsITGGKNRklmIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRillkpfQ------- 149
Cdd:TIGR00630 440 EAHEFFNQLTLTPEEKKIAEEV-LKEIRER---LGFLIDVGLDYLSLSRAAGTLSGGEAQRIRLAT------Qigsgltg 509
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821526 150 -LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYI------EGGEI 206
Cdd:TIGR00630 510 vLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEV 573
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-206 |
5.45e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIG-HLDSkDSGQVIINEME-YQPKKEVMTLKKEVLG---FIFqny 86
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDV-SEGDIRFHDIPlTKLQLDSWRSRLAVVSqtpFLF--- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 87 llmeNETVLENLSITGGKNRKLMIEH---LEEVGMD--------ESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:PRK10789 402 ----SDTVANNIALGRPDATQQEIEHvarLASVHDDilrlpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 156 PTGNLDDKNKHKIIElFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PRK10789 478 ALSAVDGRTEHQILH-NLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
6.50e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQViinemEYQPKKEVmtlkkevlG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----KRNGKLRI--------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENE--TVLENLSITGGKNRKLMIEHLEEVGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRPGTKKEDILPALKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 159 NLDDKNKHKIIELFLALKKQ-GKTIICVTHDPE-ISAKADRII 199
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHlVMAKTDEVL 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-188 |
1.13e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINE-------MEYQPKKEVMTLKKEV 78
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllpLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 79 LGF----IFQNylLMENETVLENLSITGGKNRKlmIEHLEEVGMdeSYLAKKVYQ-LSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:PRK10895 88 SIFrrlsVYDN--LMAVLQIRDDLSAEQREDRA--NELMEEFHI--EHLRDSMGQsLSGGERRRVEIARALAANPKFILL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD 188
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-207 |
2.80e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.33 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDsGQVIINEMEYQPkkevMTLKK--EVLGFIFQNYLLMENeT 93
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNS----VPLQKwrKAFGVIPQKVFIFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 VLENLSITGGKNRKLMIEHLEEVGMD---ESY-------LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK 163
Cdd:cd03289 93 FRKNLDPYGKWSDEEIWKVAEEVGLKsviEQFpgqldfvLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 164 NkHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:cd03289 173 T-YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
15-204 |
3.04e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.08 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 15 LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKEVLGfIFQNYLLMENETV 94
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR-TFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLSITGGKNRKLMIEH----------------------LEEVGMDEsyLA-KKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK11300 98 IENLLVAQHQQLKTGLFSgllktpafrraesealdraatwLERVGLLE--HAnRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLALKKQ-GKTIICVTHD-PEISAKADRIIYIEGG 204
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDmKLVMGISDRIYVVNQG 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
110-204 |
3.06e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 59.07 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 110 IEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQ---LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVT 186
Cdd:PRK00635 790 IHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIE 869
|
90 100
....*....|....*....|
gi 489821526 187 HDPEISAKADRIIYI--EGG 204
Cdd:PRK00635 870 HNMHVVKVADYVLELgpEGG 889
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-194 |
3.14e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDS-----KDSGQVIINEME-YQPKKEVMTLK 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 76 KEVlGFIFQNyllmEN---ETVLENLS----ITGGKNRklmIEHLEEVGMDESYLAKKV--------YQLSGGEKQRIAI 140
Cdd:PRK14243 91 RRI-GMVFQK----PNpfpKSIYDNIAygarINGYKGD---MDELVERSLRQAALWDEVkdklkqsgLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 141 VRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQgKTIICVTHDPEISAK 194
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAAR 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-207 |
4.66e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLILEKVSLSIGAGEFIAVVGESGSGKTTLLN-VIGHLDSKDSGQVIIN-EMEYQPKkevmtlkkevLGFIFqnyllme 90
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRgTVAYVPQ----------VSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 91 NETVLENlsITGGK-------NRKLMIEHLEE-----VGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:PLN03130 692 NATVRDN--ILFGSpfdperyERAIDVTALQHdldllPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489821526 159 NLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PLN03130 770 ALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-206 |
4.92e-10 |
|
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: 56.65 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKL--ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYqpKKEVMTLKKEVL 79
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI--STIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENeTVLENLSITGgknrklmiehleEVGMDESYLAKKVYQ----LSGGEKQRIAIVRILLKPFQLLLADE 155
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLDPFD------------EYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 156 PTGNLDDKNKHKII----ELFlalkkQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03369 152 ATASIDYATDALIQktirEEF-----TNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-205 |
5.86e-10 |
|
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: 57.56 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDS-----KDSGQViinemEYQPKKE-VM--TLKKEVL-GFIFQN 85
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEPsegkiKHSGRI-----SFSSQFSwIMpgTIKENIIfGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YllmenetvlENLSITGGKNRKLMIEHLEEvgMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:cd03291 127 Y---------RYKSVVKACQLEEDITKFPE--KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489821526 166 HKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGE 205
Cdd:cd03291 196 KEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-199 |
6.15e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHL-DSKDSGQVII---------NEMEYQPKKEVMTLKKEVLGF---- 81
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFknehtndmtNEQDYQGDEEQNVGMKNVNEFsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 ---------IFQN----------------------YLLMENETVLENLSITggKNRKLMIEH--LEEVGMDESYLAKKVY 128
Cdd:PTZ00265 1263 eggsgedstVFKNsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIY--ENIKFGKEDatREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 129 -----------------QLSGGEKQRIAIVRILLKPFQLLLADEPTGNLdDKNKHKIIE-LFLALK-KQGKTIICVTHDP 189
Cdd:PTZ00265 1341 ieslpnkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKdKADKTIITIAHRI 1419
|
250
....*....|
gi 489821526 190 EISAKADRII 199
Cdd:PTZ00265 1420 ASIKRSDKIV 1429
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-188 |
6.27e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIghldskdSGQVIINEMEYQPKKEVMTLKKEVLGFIFQNYL--LMENE------------ 92
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFtkLLEGDvkvivkpqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 -------TVLENLSITGGKNRK-LMIEHLEEvgmdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKN 164
Cdd:cd03236 99 ipkavkgKVGELLKKKDERGKLdELVDQLEL----RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....
gi 489821526 165 KHKIIELFLALKKQGKTIICVTHD 188
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
81-206 |
7.83e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.92 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLEnlSITGGKNRKLMiehLEEVGMdeSYLA--KKVYQLSGGEKQRIAIVRIL---LKPFQLLLaDE 155
Cdd:PRK00635 433 FIFLSQLPSKSLSIEE--VLQGLKSRLSI---LIDLGL--PYLTpeRALATLSGGEQERTALAKHLgaeLIGITYIL-DE 504
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 156 PTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIE------GGEI 206
Cdd:PRK00635 505 PSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGpgagifGGEV 561
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-207 |
9.21e-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: 57.61 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDsGQVIINEMEYQPkkevMTLKK--EVLGFIFQNYLLMENeT 93
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNS----VTLQTwrKAFGVIPQKVFIFSG-T 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 VLENLSITGGKNRKLMIEHLEEVG---MDESY-------LAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK 163
Cdd:TIGR01271 1308 FRKNLDPYEQWSDEEIWKVAEEVGlksVIEQFpdkldfvLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489821526 164 NkHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:TIGR01271 1388 T-LQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVK 1430
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-204 |
1.18e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.80 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLL-NVIGHLDSKDSGQVIINEMEYQPKKEVMTLK-KEVLGFIFQNYLLMeNETV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLSITGGKNRKLMIEHLEEVGM----------DESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD-DK 163
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLqpdidllpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489821526 164 NKHKIIELFLA-LKKQGKTIICVTHDPEISAKADRIIYIEGG 204
Cdd:cd03290 176 SDHLMQEGILKfLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-198 |
2.11e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSkdSGQVIINE---MEY---------------QPKKEVMTlkke 77
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMaGLLPG--SGSIQFAGqplEAWsaaelarhraylsqqQTPPFAMP---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 vlgfIFQnYLLM---------ENETVLENLSitggknRKLMIEHLeevgmdesyLAKKVYQLSGGEKQRIAIVRILLK-- 146
Cdd:PRK03695 86 ----VFQ-YLTLhqpdktrteAVASALNEVA------EALGLDDK---------LGRSVNQLSGGEWQRVRLAAVVLQvw 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 147 ----PF-QLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAK-ADRI 198
Cdd:PRK03695 146 pdinPAgQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRhADRV 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-206 |
3.70e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLnvighldskdsgQVIINEMEYQpKKEVMTLKKevLGFIFQNYLLMeNET 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEIS-EGRVWAERS--IAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 94 VLEN-LSITGGKNRKLM----IEHLEE------VGMdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDD 162
Cdd:PTZ00243 737 VRGNiLFFDEEDAARLAdavrVSQLEAdlaqlgGGL-ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489821526 163 KNKHKII-ELFL-ALKkqGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PTZ00243 816 HVGERVVeECFLgALA--GKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-188 |
3.72e-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: 55.56 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIghldskdSGQVIINEMEYQPKKEvmtlKKEVL----GFIFQNYL--LMENE-------- 92
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-------SGELKPNLGDYDEEPS----WDEVLkrfrGTELQDYFkkLANGEikvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 -----------TVLENLSITGgkNRKLMIEHLEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:COG1245 168 yvdlipkvfkgTVRELLEKVD--ERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*..
gi 489821526 162 DKNKHKIIELFLALKKQGKTIICVTHD 188
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-206 |
4.43e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKEVMTLKKevlGFIF-----QNYLLMENETV 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR---GLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLS----------ITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKN 164
Cdd:PRK15439 359 AWNVCalthnrrgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 165 KHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-202 |
6.87e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 31 AVVGESGSGKTTLLNVI-----GHLD-SKDSGQviinemeyqpKKEVMTLKKEVLGFI---FQN-----YLLMENETVLE 96
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyaltGELPpNSKGGA----------HDPKLIREGEVRAQVklaFENangkkYTITRSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 97 N-LSITGGKNRKLMIEHLEevgmdesylakkvyQLSGGEKQ------RIAIVRILLKPFQLLLADEPTGNLDDKN-KHKI 168
Cdd:cd03240 96 NvIFCHQGESNWPLLDMRG--------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 489821526 169 IELFLALKKQG-KTIICVTHDPEISAKADRIIYIE 202
Cdd:cd03240 162 AEIIEERKSQKnFQLIVITHDEELVDAADHIYRVE 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-187 |
7.06e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEmEYQPKKEVMTLKKEVLGFIFQNYLLMEN 91
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKWWRSKIGVVSQDPLLFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 eTVLENL--SITGGKNRKLMIEHLEEVG---------------------------MDESYL--AKKVYQ----------- 129
Cdd:PTZ00265 475 -SIKNNIkySLYSLKDLEALSNYYNEDGndsqenknkrnscrakcagdlndmsntTDSNELieMRKNYQtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 130 --------------------------LSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALK-KQGKTI 182
Cdd:PTZ00265 554 kkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRIT 633
|
....*
gi 489821526 183 ICVTH 187
Cdd:PTZ00265 634 IIIAH 638
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
113-205 |
7.09e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.16 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 113 LEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQ---LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDP 189
Cdd:cd03271 153 LCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
90
....*....|....*...
gi 489821526 190 EISAKADRIIYI--EGGE 205
Cdd:cd03271 233 DVIKCADWIIDLgpEGGD 250
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-188 |
1.01e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 7 VSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHldskdsgqviinemEYQPKKEVMTLKKEV-LGFIFQN 85
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG--------------ELAPVSGEIGLAKGIkLGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 YL--LMENETVLENLS-ITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDD 162
Cdd:PRK10636 384 QLefLRADESPLQHLArLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170 180
....*....|....*....|....*.
gi 489821526 163 KNKHKIIElflALKKQGKTIICVTHD 188
Cdd:PRK10636 464 DMRQALTE---ALIDFEGALVVVSHD 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-206 |
1.72e-08 |
|
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: 52.26 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 6 NVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKDS--GQVIINEMEYQPKKEvmTLKKEVLgFI 82
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPYKEFAE--KYPGEII-YV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQNYLLMENETVLENL----SITGGKNrklmiehleevgmdesylakkVYQLSGGEKQRIAIVRILLKPFQLLLADEPTG 158
Cdd:cd03233 89 SEEDVHFPTLTVRETLdfalRCKGNEF---------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489821526 159 NLDDKNKHKIIELFLALKKQGKT---IICVTHDPEISAKADRIIYIEGGEI 206
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTttfVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-203 |
2.13e-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: 53.25 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN-EMEYQPK-------KEVMTLKKEVLGFIFQNYLLmENETVlenl 98
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYKPQyispdydGTVEEFLRSANTDDFGSSYY-KTEII---- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 99 sitggknRKLMIEHLeevgMDesylaKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK---NKHKIIELFlaL 175
Cdd:COG1245 441 -------KPLGLEKL----LD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRF--A 502
|
170 180
....*....|....*....|....*....
gi 489821526 176 KKQGKTIICVTHDPE-ISAKADRIIYIEG 203
Cdd:COG1245 503 ENRGKTAMVVDHDIYlIDYISDRLMVFEG 531
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-187 |
2.51e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGqviinEMEYQPKKEVMTLKKEV----LGFIFQNYLLMENE 92
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAG-----SILYLGKEVTFNGPKSSqeagIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 TVLENL-------SITGGKNRKLMIEH----LEEVGMDESYlAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:PRK10762 95 TIAENIflgrefvNRFGRIDWKKMYAEadklLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180
....*....|....*....|....*.
gi 489821526 162 DKNKHKIIELFLALKKQGKTIICVTH 187
Cdd:PRK10762 174 DTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-206 |
2.57e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINemEYQPKKEVMTLKKEVLGFIFQNYLLMENeTVL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMID--DCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLSITGGKN-----RKLMIEHLEEVGMDESY-LAKKVYQ----LSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNK 165
Cdd:PLN03232 1328 FNIDPFSEHNdadlwEALERAHIKDVIDRNPFgLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489821526 166 hKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEI 206
Cdd:PLN03232 1408 -SLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-206 |
3.03e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPK--KEVMTLKkevLGFIFQNYL---LMEN 91
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLspRERRRLG---VAYIPEDRLgrgLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSIT----------GGKNRKLMIEHLEEVgMDE--------SYLAKkvyQLSGGEKQRIAIVRILLKPFQLLLA 153
Cdd:COG3845 351 MSVAENLILGryrrppfsrgGFLDRKAIRAFAEEL-IEEfdvrtpgpDTPAR---SLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489821526 154 DEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILALSDRIAVMYEGRI 480
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-205 |
3.28e-08 |
|
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: 50.83 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIInemeyqpkkevmtlkkevlgfifqnyllmenetvlenlsITGGKNR 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 107 KLMIEHLEEVGMDESYlakkvYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIE------LFLALKKQGK 180
Cdd:smart00382 43 EEVLDQLLLIIVGGKK-----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSEKNL 117
|
170 180 190
....*....|....*....|....*....|.
gi 489821526 181 TIICVTHDPEISAKA------DRIIYIEGGE 205
Cdd:smart00382 118 TVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-205 |
3.62e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 4 LVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKEVMtlkKEVLGF 81
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgKEIDFKSSKEAL---ENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 82 IFQNYLLMENETVLENLSITGGKNRKLMIEH----------LEEVGMDESyLAKKVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLGRYPTKGMFVDQdkmyrdtkaiFDELDIDID-PRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGE 205
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-207 |
3.81e-08 |
|
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: 52.52 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 20 VSLSIGAGEFIAVVGESGSGKTTLLNVI-GHLDSKDSGQVIINEMEYQPKKEVMTLKKEV---------------LGfIF 83
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIamvpedrkrhgivpiLG-VG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 84 QNYLLMENETVLENLSITGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK 163
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489821526 164 NKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:TIGR02633 438 AKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLK 482
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
106-205 |
5.22e-08 |
|
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: 52.32 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 106 RKLmiEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQ---LLLADEPTGNL--DDKNkhKIIELFLALKKQGK 180
Cdd:TIGR00630 808 RKL--QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfDDIK--KLLEVLQRLVDKGN 883
|
90 100
....*....|....*....|....*..
gi 489821526 181 TIICVTHDPEISAKADRIIYI--EGGE 205
Cdd:TIGR00630 884 TVVVIEHNLDVIKTADYIIDLgpEGGD 910
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-188 |
5.24e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 27 GEFIAVVGESGSGKTTLLNVIghldskdSGQVIINEMEYQPKKEvmtlKKEVL----GFIFQNYL--LMENE-------- 92
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------SGELIPNLGDYEEEPS----WDEVLkrfrGTELQNYFkkLYNGEikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 93 -----------TVLENLSITggKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD 161
Cdd:PRK13409 168 yvdlipkvfkgKVRELLKKV--DERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*..
gi 489821526 162 DKNKHKIIELFLALKKqGKTIICVTHD 188
Cdd:PRK13409 245 IRQRLNVARLIRELAE-GKYVLVVEHD 270
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
129-207 |
6.28e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 129 QLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-206 |
7.66e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 30 IAVVGESGSGKTTLLNVIghldskdSGqviinemEYQPKKEVMTLKKEVLGFIFQNY----LLMENETVLENLSITGGKN 105
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLI-------SG-------ELQPSSGTVFRSAKVRMAVFSQHhvdgLDLSSNPLLYMMRCFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 106 RKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIElFLALKKQGktIICV 185
Cdd:PLN03073 604 EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ-GLVLFQGG--VLMV 680
|
170 180
....*....|....*....|..
gi 489821526 186 THDPE-ISAKADRIIYIEGGEI 206
Cdd:PLN03073 681 SHDEHlISGSVDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-206 |
8.27e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIghldSKDSGQVIINEMEYQPKK----EVMTLKKE 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDHPQGYSNDLTLFGRRrgsgETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 78 VLGFIfQNYLLME---NETVLeNLSITG------------GKNRKLMIEHLEEVGMDESyLAKKVYQ-LSGGEkQRIA-I 140
Cdd:PRK10938 337 HIGYV-SSSLHLDyrvSTSVR-NVILSGffdsigiyqavsDRQQKLAQQWLDILGIDKR-TADAPFHsLSWGQ-QRLAlI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 141 VRILLKPFQLLLADEPTGNLDDKNKhKIIELFL-ALKKQGKTII------------CVTHdpeisakadRIIYIEGGEI 206
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNR-QLVRRFVdVLISEGETQLlfvshhaedapaCITH---------RLEFVPDGDI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-203 |
8.44e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 24 IGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIIN-EMEYQPKkevmtlkkevlgFIFQNYllmeNETVLENLSITG 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKPQ------------YIKPDY----DGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 103 GK----------NRKLMIEHLeevgMDesylaKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLD-------DKNK 165
Cdd:PRK13409 426 DDlgssyykseiIKPLQLERL----LD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAI 496
|
170 180 190
....*....|....*....|....*....|....*....
gi 489821526 166 HKIIElflalkKQGKTIICVTHDPE-ISAKADRIIYIEG 203
Cdd:PRK13409 497 RRIAE------EREATALVVDHDIYmIDYISDRLMVFEG 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-207 |
9.24e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQD-KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQPKKevMTLKKEVLG 80
Cdd:PRK10522 323 LELRNVTFAYQDnGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ--PEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSitggKNRKLMIEHLEEVGMDEsylakKV---------YQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKP----ANPALVEKWLERLKMAH-----KLeledgrisnLKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 152 LADEPTGnldDKNKH--KII--ELFLALKKQGKTIICVTHDPEISAKADRIIYIEGGEIR 207
Cdd:PRK10522 472 LLDEWAA---DQDPHfrREFyqVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-206 |
1.62e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 1.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 130 LSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-199 |
2.28e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINE------MEYQPKKEVM-- 72
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarLQQDPPRNVEgt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 73 --------------TLKK--EVLGFIFQNY---LLMENETVLENLSITGG---KNRklMIEHLEEVGMDESylaKKVYQL 130
Cdd:PRK11147 83 vydfvaegieeqaeYLKRyhDISHLVETDPsekNLNELAKLQEQLDHHNLwqlENR--INEVLAQLGLDPD---AALSSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 131 SGGEKQRIAIVRILLKPFQLLLADEPTGNLDdknkhkI-----IELFLaLKKQGkTIICVTHDPE-ISAKADRII 199
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IetiewLEGFL-KTFQG-SIIFISHDRSfIRNMATRIV 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-201 |
3.10e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 123 LAKKVYQLSGGEKQRIAIVRILLKPFQ---LLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRII 199
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLI 1772
|
..
gi 489821526 200 YI 201
Cdd:PRK00635 1773 EM 1774
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-202 |
3.23e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 1 MIELVNVSKKIQDKLILEkVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQViinemeYQPKKEVMTLKKEVLG 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI------YYKNCNINNIAKPYCT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSI-TGGKNRKLMIEHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGN 159
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489821526 160 LDDKNKhKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIE 202
Cdd:PRK13541 154 LSKENR-DLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-161 |
3.90e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKL--ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIINEMEYQpKKEVMTLKKeVL 79
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS-KFGLMDLRK-VL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 80 GFIFQNYLLMENeTVLENLSITGGKNRKLMIE-----HLEEV------GMDeSYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PLN03130 1316 GIIPQAPVLFSG-TVRFNLDPFNEHNDADLWEsleraHLKDVirrnslGLD-AEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170
....*....|...
gi 489821526 149 QLLLADEPTGNLD 161
Cdd:PLN03130 1394 KILVLDEATAAVD 1406
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-206 |
5.18e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 2 IELVNVSKKIQDKLILEKVSLSIGAGEFIAVVGESGSGKTTLL----------------------NVIGhlDSKDSGQVI 59
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidgipkncqilhveqEVVG--DDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 60 IN-EMEyqpkkEVMTLKKEVLGFIFQNYLLMENETVLENLSITGGKNRKLMIEHLEEV-------------GMDESYLA- 124
Cdd:PLN03073 256 LNtDIE-----RTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIykrlelidaytaeARAASILAg 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 125 ---------KKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDdknKHKIIELFLALKKQGKTIICVTHDPE-ISAK 194
Cdd:PLN03073 331 lsftpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREfLNTV 407
|
250
....*....|..
gi 489821526 195 ADRIIYIEGGEI 206
Cdd:PLN03073 408 VTDILHLHGQKL 419
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-189 |
1.32e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 13 DKLIlEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII---NEMEYQPKKEVM---TLKKEVL------G 80
Cdd:TIGR00954 465 DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpakGKLFYVPQRPYMtlgTLRDQIIypdsseD 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 81 FIFQNYLLMENETVLENLSITggknrklmieHLEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNL 160
Cdd:TIGR00954 544 MKRRGLSDKDLEQILDNVQLT----------HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*....
gi 489821526 161 DDKNKHKIIELflaLKKQGKTIICVTHDP 189
Cdd:TIGR00954 614 SVDVEGYMYRL---CREFGITLFSVSHRK 639
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
12-191 |
1.83e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKL-ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVighLDSKDSGQVIINEMEYQ--PKKEvMTLKKeVLGFIFQNYLL 88
Cdd:PLN03140 890 EDRLqLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISgfPKKQ-ETFAR-ISGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENETVLENLSITG--------GKNRKLMI--EHLEEVGMDESYLA----KKVYQLSGGEKQRIAIVRILLKPFQLLLAD 154
Cdd:PLN03140 965 SPQVTVRESLIYSAflrlpkevSKEEKMMFvdEVMELVELDNLKDAivglPGVTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*..
gi 489821526 155 EPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEI 191
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
106-205 |
2.25e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 106 RKLmiEHLEEVGMDesYLakKVYQ----LSGGEKQRIAIVRILLKPFQ---LLLADEPTGNL--DDknKHKIIELFLALK 176
Cdd:COG0178 805 RKL--QTLQDVGLG--YI--KLGQpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfHD--IRKLLEVLHRLV 876
|
90 100 110
....*....|....*....|....*....|.
gi 489821526 177 KQGKTIICVTHDPEISAKADRIIYI--EGGE 205
Cdd:COG0178 877 DKGNTVVVIEHNLDVIKTADWIIDLgpEGGD 907
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-202 |
2.59e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 14 KLILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVII--NEMEYQPKKEVMTLKKEVLGFIF---QNYLL 88
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgNWQLAWVNQETPALPQPALEYVIdgdREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 89 MENEtvlenLSITGGKNRKLMIEH--------------------LEEVGMDESYLAKKVYQLSGGEKQRIAIVRILLKPF 148
Cdd:PRK10636 94 LEAQ-----LHDANERNDGHAIATihgkldaidawtirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489821526 149 QLLLADEPTGNLDdknKHKIIELFLALKKQGKTIICVTHDPE-ISAKADRIIYIE 202
Cdd:PRK10636 169 DLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDfLDPIVDKIIHIE 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-161 |
4.78e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIG----HLDSKDSGQVIINEMeyqPKKEVMTLKKEVLGFIFQNYLLMEN 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI---TPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 92 ETVLENLSITG----------GKNRKLMIEHLEEV-----GMDESYLAKK----VYQLSGGEKQRIAIVRILLKPFQLLL 152
Cdd:TIGR00956 153 LTVGETLDFAArcktpqnrpdGVSREEYAKHIADVymatyGLSHTRNTKVgndfVRGVSGGERKRVSIAEASLGGAKIQC 232
|
....*....
gi 489821526 153 ADEPTGNLD 161
Cdd:TIGR00956 233 WDNATRGLD 241
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
15-191 |
7.40e-06 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.05 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 15 LILEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVIinemeyQPKKEVMTLKKEvlGFIFQNYLLMENETV 94
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI------GLRGDALPLGAN--SFILPGLTGEENARM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 95 LENLSITGGKNRKLMIEHLEEVgmdESYLAKKVYQLSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDKNKHKiIELFLA 174
Cdd:PRK15177 73 MASLYGLDGDEFSHFCYQLTQL---EQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLR-MQAALA 148
|
170
....*....|....*..
gi 489821526 175 LKKQGKTIICVTHDPEI 191
Cdd:PRK15177 149 CQLQQKGLIVLTHNPRL 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
130-203 |
8.88e-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: 44.49 E-value: 8.88e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 130 LSGGEKQRIAIVRILLKPFQLLLADEPTGNLDDK---NKHKIIELFlaLKKQGKTIICVTHD-PEISAKADRIIYIEG 203
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRL--SEEGKKTALVVEHDlAVLDYLSDRIHVFEG 147
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
113-206 |
1.11e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 113 LEEVGMDesYL-----AKKvyqLSGGEKQRIaivRillkpfqllLA--------------DEPTGNLDDKNKHKIIELFL 173
Cdd:COG0178 469 LVDVGLD--YLtldrsAGT---LSGGEAQRI---R---------LAtqigsglvgvlyvlDEPSIGLHQRDNDRLIETLK 531
|
90 100 110
....*....|....*....|....*....|....*....
gi 489821526 174 ALKKQGKTIICVTHDPEISAKADRIIYI------EGGEI 206
Cdd:COG0178 532 RLRDLGNTVIVVEHDEDTIRAADYIIDIgpgageHGGEV 570
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
122-205 |
1.44e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.18 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 122 YLAKKVYQLSGGEKQRIAI-VRILL---------KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEI 191
Cdd:cd03279 116 FLARPVSTLSGGETFLASLsLALALsevlqnrggARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEEL 195
|
90
....*....|....
gi 489821526 192 SAKADRIIYIEGGE 205
Cdd:cd03279 196 KERIPQRLEVIKTP 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-206 |
3.06e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 12 QDKLILEKVSLSIGAGEFIAVVGESGSGKTTL-LNVIGH-LDSKDSGQVIINEMEyqpkKEVMTLKKEV---LGFIFQN- 85
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRsYGRNISGTVFKDGKE----VDVSTVSDAIdagLAYVTEDr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 --YLLMENETVLENLSIT--GGKNRKLMIEHLEEVGMDESYLAK----------KVYQLSGGEKQRIAIVRILLKPFQLL 151
Cdd:NF040905 347 kgYGLNLIDDIKRNITLAnlGKVSRRGVIDENEEIKVAEEYRKKmniktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVL 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 152 LADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHD-PEISAKADRIIYIEGGEI 206
Cdd:NF040905 427 ILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSElPELLGMCDRIYVMNEGRI 482
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
128-191 |
5.72e-05 |
|
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: 42.76 E-value: 5.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 128 YQLSGGEKQ---RIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEI 191
Cdd:pfam13304 235 FELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-204 |
5.82e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 15 LILEKVSLSIGAGEFIAVVGESGSGKTTLL-------NVIG---HLDSKDSGQVIINEMEYQPKkevMTLKKEVL--GFI 82
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmrmvEVCGgeiRVNGREIGAYGLRELRRQFS---MIPQDPVLfdGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 83 FQN---YLLMENETVLENLSITGgknrklMIEHL--EEVGMDESYLAKKVyQLSGGEKQRIAIVRILLKPFQ-LLLADEP 156
Cdd:PTZ00243 1401 RQNvdpFLEASSAEVWAALELVG------LRERVasESEGIDSRVLEGGS-NYSVGQRQLMCMARALLKKGSgFILMDEA 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489821526 157 TGNLDDknkhkiielflALKKQ----------GKTIICVTHDPEISAKADRIIYIEGG 204
Cdd:PTZ00243 1474 TANIDP-----------ALDRQiqatvmsafsAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
129-202 |
3.52e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 129 QLSGGEKQ------RIAIVRILL------KPFQLLLADEPTGNLDDKNKHKIIELFLALKKQG-KTIICVTHDPEISAKA 195
Cdd:PRK02224 781 QLSGGERAlfnlslRCAIYRLLAegiegdAPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDDELVGAA 860
|
....*..
gi 489821526 196 DRIIYIE 202
Cdd:PRK02224 861 DDLVRVE 867
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-207 |
4.93e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGqviinEMEYQPKKEVMTLKKEVLGfifqNYLLMEN-ETVL 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-----KVDRNGEVSVIAISAGLSG----QLTGIENiEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 96 ENLSITGGKNRKLMIEHLEEVGMDEsYLAKKVYQLSGGEKQRIAI-VRILLKPfQLLLADEPTGNLDDKNKHKIIELFLA 174
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGE-FIYQPVKKYSSGMRAKLGFsINITVNP-DILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190
....*....|....*....|....*....|....
gi 489821526 175 LKKQGKTIICVTHD-PEISAKADRIIYIEGGEIR 207
Cdd:PRK13546 189 FKEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKLK 222
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
18-199 |
7.98e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 18 EKVSLSIGAGeFIAVVGESGSGKTTLLN----VIG-----HLDSKDSGQVIINEMEYQPKK---EVmTLkkevlgfIFQN 85
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIIDairwVLGeqsakSLRGEKMSDVIFAGSETRKPAnfaEV-TL-------TFDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 86 ----YLLMENETVLENLSITGGKNRKLmieHLeevgmdesylakkvyqLSGGEKQRIAIVRI----LLKPFQLLLADEPT 157
Cdd:cd03278 85 sdgrYSIISQGDVSEIIEAPGKKVQRL---SL----------------LSGGEKALTALALLfaifRVRPSPFCVLDEVD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489821526 158 GNLDDKNKHKIIELFLALKKQGKTIIcVTHDPEISAKADRII 199
Cdd:cd03278 146 AALDDANVERFARLLKEFSKETQFIV-ITHRKGTMEAADRLY 186
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
113-206 |
9.88e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 113 LEEVGMDESYLAKKVYQLSGGEKQRIaivRillkpfqllLA--------------DEPTGNLDDKNKHKIIELFLALKKQ 178
Cdd:PRK00349 473 LVDVGLDYLTLSRSAGTLSGGEAQRI---R---------LAtqigsgltgvlyvlDEPSIGLHQRDNDRLIETLKHLRDL 540
|
90 100 110
....*....|....*....|....*....|....
gi 489821526 179 GKTIICVTHDPEISAKADRIIYI------EGGEI 206
Cdd:PRK00349 541 GNTLIVVEHDEDTIRAADYIVDIgpgagvHGGEV 574
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-202 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489821526 130 LSGGEKQ------RIAIVRILLKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIE 202
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRVS 867
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
110-198 |
2.08e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 110 IEHLEEVGMDESYlakKVYQLSGGEKQRIAIVRIL----LKPFQLLLADEPTGNLDDKNKHKIIELflaLKKQGKT--II 183
Cdd:cd03272 142 INSLTNMKQDEQQ---EMQQLSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANM---IKELSDGaqFI 215
|
90
....*....|....*
gi 489821526 184 CVTHDPEISAKADRI 198
Cdd:cd03272 216 TTTFRPELLEVADKF 230
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
16-44 |
3.30e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|
gi 489821526 16 ILEKVSLSIGAGE-FIAVVGESGSGKTTLL 44
Cdd:COG3267 31 ALARLEYALAQGGgFVVLTGEVGTGKTTLL 60
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-45 |
3.39e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 3.39e-03
10 20
....*....|....*....|....*....
gi 489821526 17 LEKVSLSIGAGEFIAVVGESGSGKTTLLN 45
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
37-63 |
5.73e-03 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 36.69 E-value: 5.73e-03
10 20 30
....*....|....*....|....*....|
gi 489821526 37 GSGKTTLLNvigHLDSKDSGQ---VIINEM 63
Cdd:COG0523 14 GAGKTTLLN---HLLANPEGRriaVIVNEF 40
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
25-59 |
6.16e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 35.94 E-value: 6.16e-03
10 20 30
....*....|....*....|....*....|....*
gi 489821526 25 GAGEFIAVVGESGSGKTTLLNVIGHLDSKDSGQVI 59
Cdd:pfam13191 22 GRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFL 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-198 |
7.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 36.67 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821526 99 SITGGKNRKLMI-EHLEEVGMDESYLAKKVYQLSGGEK-Q-----RIAIVRiLLKPFQL-LLADEPTGNLDDKNKHKIIE 170
Cdd:COG4717 527 RLTDGRYRLIRIdEDLSLKVDTEDGRTRPVEELSRGTReQlylalRLALAE-LLAGEPLpLILDDAFVNFDDERLRAALE 605
|
90 100
....*....|....*....|....*...
gi 489821526 171 LFLALKKQGKtIICVTHDPEISAKADRI 198
Cdd:COG4717 606 LLAELAKGRQ-VIYFTCHEELVELFQEE 632
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
130-202 |
7.67e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 35.75 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821526 130 LSGGEKQRIAIVRIL----LKPFQLLLADEPTGNLDDKNKHKIIELFLALKKQGKTIICVTHDPEISAKADRIIYIE 202
Cdd:cd03239 95 LSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
130-196 |
7.95e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 36.80 E-value: 7.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821526 130 LSGGEKQ------RIAIVRILLKPFQLLLADEPTGNLDDKNKHK---IIELFLALKKQGKTIICVTHDPEISAKAD 196
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNlkdIIEYSLKDSSDIPQVIMISHHRELLSVAD 877
|
|
| |
