|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
29-249 |
1.12e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWR 108
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLgdRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRLPLTAEIRAGRfITPDE 249
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGR-IVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
52-243 |
1.06e-58 |
|
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: 185.77 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQDFRLFEDLTALDNV 131
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDL 209
Cdd:cd03255 104 ELPLLLAGVPKKERRERAEELLERVGLgdRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELL 183
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 210 MSAAQSLSASLILVSHSDRVLKRLPLTAEIRAGR 243
Cdd:cd03255 184 RELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
29-252 |
1.71e-51 |
|
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: 167.61 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWR 108
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGtiAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLghRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRLPLTAEIRAGRFITPDELTP 252
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
29-244 |
2.48e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDgtgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTlafSQCTESVRDRWR 108
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG---KPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQhCGFLFQDFRLFEDlTALDNVLLPLTFRGtiAAHDRETAREMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRP 185
Cdd:COG4619 74 RQ-VAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdilDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 186 AVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRLPL-TAEIRAGRF 244
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADrVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
52-254 |
2.14e-40 |
|
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: 139.24 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDNV 131
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR-RQIGMIFQQFNLIERLSVLENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLP-LTFRGTIAA-------HDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEAR 201
Cdd:cd03256 100 LSGrLGRRSTWRSlfglfpkEEKQRALAALERVGLLDkaYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 202 GDIVVDDLMSAAQSLSASLILVSH--------SDRVLKrlpltaeIRAGRFI---TPDELTPSR 254
Cdd:cd03256 180 SRQVMDLLKRINREEGITVIVSLHqvdlareyADRIVG-------LKDGRIVfdgPPAELTDEV 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
52-243 |
2.22e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-----TLAFSQctesvRDRWRgQHCGFLFQDFRLFEDLT 126
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsRLKRRE-----IPYLR-RRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 127 ALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDI 204
Cdd:COG2884 96 VYENVALPLRVTGKSRKEIRRRVREVLDLVGLsdKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2575808627 205 VVdDLMSAAQSLSASLILVSHSDRVLKRLPL-TAEIRAGR 243
Cdd:COG2884 176 IM-ELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGR 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
53-251 |
7.76e-40 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.64 E-value: 7.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQDFRLFEDLTALDNVL 132
Cdd:PRK11629 30 FSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 133 LPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLM 210
Cdd:PRK11629 110 MPLLIGKKKPAEINSRALEMLAAVGLehRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLG 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2575808627 211 SAAQSLSASLILVSHSDRVLKRLPLTAEIRAGRFitPDELT 251
Cdd:PRK11629 190 ELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL--TAELS 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
52-243 |
3.30e-36 |
|
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: 127.75 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDNV 131
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFRLLPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVdDL 209
Cdd:TIGR02673 101 ALPLEVRGKKEREIQRRVGAALRQVGLehKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERIL-DL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2575808627 210 MSAAQSLSASLILVSHSDRVLKRLPL-TAEIRAGR 243
Cdd:TIGR02673 180 LKRLNKRGTTVIVATHDLSLVDRVAHrVIILDDGR 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
65-232 |
4.71e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 127.59 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAH 144
Cdd:PRK10584 43 GESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 145 DRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLIL 222
Cdd:PRK10584 123 SRNGAKALLEQLGLgkRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLIL 202
|
170
....*....|
gi 2575808627 223 VSHSDRVLKR 232
Cdd:PRK10584 203 VTHDLQLAAR 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
45-244 |
1.00e-35 |
|
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: 126.05 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwrgQHCGFLFQDFRLFED 124
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-----RRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 LTALDNVLLPLTFRGTIAahDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEArG 202
Cdd:COG4133 90 LTVRENLRFWAALYGLRA--DREAIDEALEAVGLagLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-G 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2575808627 203 DIVVDDLMSAAQSLSASLILVSHSDRvlkRLPLTAEIRAGRF 244
Cdd:COG4133 167 VALLAELIAAHLARGGAVLLTTHQPL---ELAAARVLDLGDF 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
29-230 |
4.24e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.97 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqcTESVRDrwR 108
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-------GKPVTG--P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLagFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHdvdeavflADRVV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
29-230 |
6.70e-34 |
|
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: 121.81 E-value: 6.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsQCTESVRDRwr 108
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL-------VDGEPVTGP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRTNTRA--GDLSRGEMQRTALVRVLMGRPA 186
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAypHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHdideavflADRVV 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
43-250 |
1.38e-33 |
|
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: 121.45 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLF 122
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-RRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFRGTIAAHD-RETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDE 199
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGaeDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 200 ARGDIVVDDLMSAAQSLSASLILVSH--------SDRVlkrlpltAEIRAGRFI---TPDEL 250
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHdldtafaiADRI-------AVLYDGKIVaegTPEEL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
52-195 |
1.64e-32 |
|
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: 116.21 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTEsvrdRWRGQHCGFLFQDFRLFEDLTALDNV 131
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI------RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTA 195
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLgdladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
53-243 |
3.02e-32 |
|
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: 117.51 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDNVL 132
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 133 LPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVdDLM 210
Cdd:cd03292 101 FALEVTGVPPREIRKRVPAALELVGLshKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM-NLL 179
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 211 SAAQSLSASLILVSHSDRVLKRL-PLTAEIRAGR 243
Cdd:cd03292 180 KKINKAGTTVVVATHAKELVDTTrHRVIALERGK 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
51-230 |
3.76e-32 |
|
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: 117.24 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSqcTESVRDRwrgqHCGFLFQDFRLFEDLTALDN 130
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERR----NIGMVFQDYALFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDD 208
Cdd:cd03259 93 IAFGLKLRGVPKAEIRARVRELLELVGLEGllNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREE 172
|
170 180 190
....*....|....*....|....*....|
gi 2575808627 209 LMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03259 173 LKELQRELGITTIYVTHdqeealalADRIA 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
45-250 |
5.97e-32 |
|
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: 117.39 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFED 124
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR-RRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 LTALDNVLLPLTFRGTIAAHD-RETAREMLAARGIRT--NTRAGDLSRGeMQ-RTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:COG1127 97 LTVFENVAFPLREHTDLSEAEiRELVLEKLELVGLPGaaDKMPSELSGG-MRkRVALARALALDPEILLYDEPTAGLDPI 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 201 RGDiVVDDLMSAAQ-SLSASLILVSH--------SDRVlkrlpltAEIRAGRFI---TPDEL 250
Cdd:COG1127 176 TSA-VIDELIRELRdELGLTSVVVTHdldsafaiADRV-------AVLADGKIIaegTPEEL 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
52-230 |
2.31e-30 |
|
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: 112.62 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAF---SQCTESVRdrwrgQHCGFLFQDFRLFEDLTAL 128
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELR-----QKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 129 DNVLL-PLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARGDi 204
Cdd:cd03262 95 ENITLaPIKVKGMSKAEAEERALELLEKVGLadKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpELVGE- 173
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 205 VVDDLMSAAQSlSASLILVSH--------SDRVL 230
Cdd:cd03262 174 VLDVMKDLAEE-GMTMVVVTHemgfarevADRVI 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
30-230 |
2.69e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 112.18 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 30 SLETVRLDVPDGTgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlaFSQCTESVRDRWRG 109
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 110 QHCGFLFQDFR--LFEDlTALDNVLLPLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRP 185
Cdd:cd03225 75 RKVGLVFQNPDdqFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEglRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 186 AVILADEPTANLD-EARGDIVvdDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03225 154 DILLLDEPTAGLDpAGRRELL--ELLKKLKAEGKTIIIVTHdldlllelADRVI 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
43-230 |
1.39e-29 |
|
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: 109.58 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgqHCGFLFQDFRLF 122
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR--RIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPltfrgtiaahdretaremlaargirtntragdLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARG 202
Cdd:cd03229 89 PHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 2575808627 203 DIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHdldeaarlADRVV 172
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-243 |
2.71e-29 |
|
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: 108.46 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctesVRDRWR 108
Cdd:cd03246 1 LEVENVSFRYPGAE--PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ----WDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDlTALDNVLlpltfrgtiaahdretaremlaargirtntragdlSRGEMQRTALVRVLMGRPAVI 188
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENIL-----------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 189 LADEPTANLDEArGDIVVDDLMSAAQSLSASLILVSHSDRVLKRLPLTAEIRAGR 243
Cdd:cd03246 119 VLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-233 |
4.09e-29 |
|
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: 109.59 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdRWR 108
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKEL-RKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLedKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRI 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
52-243 |
4.28e-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: 109.31 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGaMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSQCTE---SVRDRwrgqHCGFLFQDFRLFEDLTA 127
Cdd:cd03297 18 DFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLnGTVLFDSRKKinlPPQQR----KIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLLPLtfRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIV 205
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 2575808627 206 VDDLMSAAQSLSASLILVSHSDRVLKRL-PLTAEIRAGR 243
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGR 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
43-230 |
9.26e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 107.10 E-value: 9.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwrgQHCGFLFQDFRLF 122
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----RRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVllpltfrgtiaahdretaremlaargirtntragDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEarg 202
Cdd:cd03230 86 ENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP--- 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 2575808627 203 dIVVDDLMSAAQSLSA---SLILVSH--------SDRVL 230
Cdd:cd03230 129 -ESRREFWELLRELKKegkTILLSSHileeaerlCDRVA 166
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
52-230 |
2.03e-28 |
|
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: 107.91 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctESVRDRWRgqhCGFL--FQDFRLFEDLTALD 129
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG--LPPHEIAR---LGIGrtFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTFRGTIAAHD----------RETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:cd03219 95 NVMVAAQARTGSGLLLararreereaRERAEELLERVGLadLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2575808627 198 DEA-RGDIVvdDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03219 175 NPEeTEELA--ELIRELRERGITVLLVEHdmdvvmslADRVT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
51-233 |
5.39e-28 |
|
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: 107.25 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlaFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDN 130
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI----DGEDVRKEPREAR-RQIGVLPDERGLYDRLTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARgDIVVD 207
Cdd:COG4555 95 IRYFAELYGLFDEELKKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDvMAR-RLLRE 173
|
170 180
....*....|....*....|....*.
gi 2575808627 208 DLMSAAQSlSASLILVSHSDRVLKRL 233
Cdd:COG4555 174 ILRALKKE-GKTVLFSSHIMQEVEAL 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
45-225 |
2.48e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG------TLAFSQCTESVRdRWRgQHCGFLFQD 118
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIR-QLR-QHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVLL-PLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTA 195
Cdd:PRK11264 94 FNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLagKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190
....*....|....*....|....*....|.
gi 2575808627 196 NLD-EARGDiVVDDLMSAAQSlSASLILVSH 225
Cdd:PRK11264 174 ALDpELVGE-VLNTIRQLAQE-KRTMVIVTH 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
52-198 |
1.83e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.23 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSQCteSVRDRwrgqHCGFLFQDFRLFEDLTALDN 130
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLFTNL--PPRER----RVGFVFQHYALFPHMTVAEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG1118 96 IAFGLRVRPPSKAEIRARVEELLELVQLEGlaDRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
52-230 |
2.57e-26 |
|
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: 106.91 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESvRDRWRGQHCGFLFQD-FR-LFEDLTALD 129
Cdd:COG1123 285 SLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR-SLRELRRRVQMVFQDpYSsLNPRMTVGD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTFRGTIAAHDRET-AREMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIV 205
Cdd:COG1123 364 IIAEPLRLHGLLSRAERRErVAELLERVGLPPdlaDRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
170 180 190
....*....|....*....|....*....|...
gi 2575808627 206 VDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:COG1123 444 LNLLRDLQRELGLTYLFISHdlavvryiADRVA 476
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
52-233 |
3.60e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRD-RwrgQHCGFLFQDFRLFEDLTALDN 130
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiR---QEAGMVFQQFYLFPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLL-PLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARGDI-- 204
Cdd:PRK09493 98 VMFgPLRVRGASKEEAEKQARELLAKVGLaeRAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpELRHEVlk 177
|
170 180 190
....*....|....*....|....*....|...
gi 2575808627 205 VVDDLmsAAQSLsaSLILVSH----SDRVLKRL 233
Cdd:PRK09493 178 VMQDL--AEEGM--TMVIVTHeigfAEKVASRL 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
51-250 |
6.51e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 103.64 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqctesvrdrwrGQ----------HCGFLFQDFR 120
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD----------------GRdvtglppekrNVGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGlaDRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 199 -EARGDiVVDDLMSAAQSLSASLILVSH--------SDRVlkrlpltAEIRAGRFI---TPDEL 250
Cdd:COG3842 168 aKLREE-MREELRRLQRELGITFIYVTHdqeealalADRI-------AVMNDGRIEqvgTPEEI 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
51-236 |
2.99e-25 |
|
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: 103.91 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTEsvrDRWRGQhCGFLFQDFRLFEDlTALDN 130
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA---DSWRDQ-IAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLtfRGTIAAHDRETAR-----EMLAARGIRTNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLDEAR 201
Cdd:TIGR02857 416 IRLAR--PDASDAEIREALEragldEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*
gi 2575808627 202 GDIVVDDLMSAAQslSASLILVSHSDRVLKRLPLT 236
Cdd:TIGR02857 494 EAEVLEALRALAQ--GRTVLLVTHRLALAALADRI 526
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-245 |
1.18e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.49 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWR 108
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLedRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSlSASLILVSHSDRVLKRLPLTAEIRAGRFI 245
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
43-234 |
1.66e-24 |
|
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: 95.39 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctesVRDRWRGQHCGFLFQdfrlf 122
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK----LPLEELRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 edltaldnvllpltfrgtiaahdretaremlaargirtntragdLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARG 202
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190
....*....|....*....|....*....|..
gi 2575808627 203 DIVVDDLMSAAQSlSASLILVSHSDRVLKRLP 234
Cdd:cd00267 117 ERLLELLRELAEE-GRTVIIVTHDPELAELAA 147
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-250 |
2.51e-24 |
|
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: 101.37 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 23 DPQPFDLSLETVRLDVPDGtgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTEs 102
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 103 vrDRWRgQHCGFLFQDFRLFEDlTALDNVLLpltfrGTIAAhDRETAREMLAARGIRT---------NTRAGD----LSR 169
Cdd:COG4988 407 --ASWR-RQIAWVPQNPYLFAG-TIRENLRL-----GRPDA-SDEELEAALEAAGLDEfvaalpdglDTPLGEggrgLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 170 GEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQslSASLILVSHSDRVLKRLPLTAEIRAGRFI---T 246
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVeqgT 554
|
....
gi 2575808627 247 PDEL 250
Cdd:COG4988 555 HEEL 558
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
43-225 |
2.56e-24 |
|
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: 96.45 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlAFSQCTESVRDR--WRGQHCGFLFqDFR 120
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR----VFGKPLEKERKRigYVPQRRSIDR-DFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 lfedLTALDNVLLPLT----FRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:cd03235 85 ----ISVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSelADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190
....*....|....*....|....*....|..
gi 2575808627 195 ANLD-EARGDIVvdDLMSAAQSLSASLILVSH 225
Cdd:cd03235 161 AGVDpKTQEDIY--ELLRELRREGMTILVVTH 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
47-250 |
3.13e-23 |
|
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: 98.37 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 47 IFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTesvRDRWRgQHCGFLFQDFRLFEDlT 126
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 127 ALDNVLLpltFRGTIaahDRETAREmlAAR--GIRT---------NTRAGD----LSRGEMQRTALVRVLMGRPAVILAD 191
Cdd:COG2274 565 IRENITL---GDPDA---TDEEIIE--AARlaGLHDfiealpmgyDTVVGEggsnLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 192 EPTANLDEARGDIVVDDLMSAAQslSASLILVSHSDRVLKRLPLTAEIRAGRFI---TPDEL 250
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVedgTHEEL 696
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
29-230 |
4.40e-23 |
|
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: 93.72 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GT--LAFSQctesVRD 105
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdGKdlLKLSR----RLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 106 RWRGQHCGFLFQD--------FRLFEDLTAldnvllPLTFRGTIAAHDRETAREMLAARGIRTNTRAGD-----LSRGEM 172
Cdd:cd03257 78 KIRRKEIQMVFQDpmsslnprMTIGEQIAE------PLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 173 QRTALVRVLMGRPAVILADEPTANLD---EARgdiVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDvsvQAQ---ILDLLKKLQEELGLTLLFITHdlgvvakiADRVA 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-228 |
6.22e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.42 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESvrdrwRGQHCGFLFQDFRLF 122
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNvllpLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:TIGR01189 86 PELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTgfEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*...
gi 2575808627 201 rGDIVVDDLMSAAQSLSASLILVSHSDR 228
Cdd:TIGR01189 162 -GVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-230 |
1.06e-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: 96.65 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 24 PQP-FDLSLETVRLdVPDGtGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctes 102
Cdd:TIGR01842 311 PEPeGHLSVENVTI-VPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ---- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 103 VRDRWRGQHCGFLFQDFRLFEdltaldnvllpltfrGTIAAH-----DRETAREMLAA--------------RGIRTNTR 163
Cdd:TIGR01842 385 WDRETFGKHIGYLPQDVELFP---------------GTVAENiarfgENADPEKIIEAaklagvhelilrlpDGYDTVIG 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 164 AG--DLSRGEMQRTALVRVLMGRPAVILADEPTANLDEArGDIVVDDLMSAAQSLSASLILVSHSDRVL 230
Cdd:TIGR01842 450 PGgaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE-GEQALANAIKALKARGITVVVITHRPSLL 517
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
52-229 |
1.42e-22 |
|
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: 92.11 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GT-LAFSQCTESVRdrwRGqhCGFLFQDFRLFEDLTALD 129
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRdITGLPPHERAR---AG--IGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTFRGtiAAHDRETAREMLA---ARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLdearGDIVV 206
Cdd:cd03224 95 NLLLGAYARR--RAKRKARLERVYElfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL----APKIV 168
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 207 DDLMSAAQSLSA---SLILV--------SHSDRV 229
Cdd:cd03224 169 EEIFEAIRELRDegvTILLVeqnarfalEIADRA 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
50-226 |
1.81e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 50 CFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-----TLAFSQCTESVrdrwrgqhcgfLFQDFRLFED 124
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgqdltALPPAERPVSM-----------LFQENNLFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 LTALDNVLLPLTFRGTIAAHDRETAREMLAARGI-----RtntRAGDLSRGEMQRTALVRVL-MGRPaVILADEPTANLD 198
Cdd:COG3840 86 LTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLaglldR---LPGQLSGGQRQRVALARCLvRKRP-ILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|.
gi 2575808627 199 EA-RGDIV--VDDLmsaAQSLSASLILVSHS 226
Cdd:COG3840 162 PAlRQEMLdlVDEL---CRERGLTVLMVTHD 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
52-242 |
1.89e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.77 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG-----------VVRWGTLAfsqctesvRD-RWRGQHCGFLFQDF 119
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrtVQREGRLA--------RDiRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 120 RLFEDLTALDNVLL------PLtFRGTIAAHDRETAREMLAAR---GIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:PRK09984 96 NLVNRLSVLENVLIgalgstPF-WRTCFSWFTREQKQRALQALtrvGMVhfAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 189 LADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHS-DRVLKRLPLTAEIRAG 242
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQG 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-230 |
2.07e-22 |
|
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: 95.74 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItPTEGVVRwGTLAFS-QCTESVRDRW 107
Cdd:COG1123 5 LEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-GEVLLDgRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 108 RGQHCGFLFQDFRL-FEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGR 184
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLerRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 185 PAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHdlgvvaeiADRVV 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
51-232 |
4.06e-22 |
|
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: 89.75 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTesvRDRWRgQHCGFLFQDFRLFEDlTALDN 130
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR-KNIAYVPQDPFLFSG-TIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLlpltfrgtiaahdretaremlaargirtntragdlSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLM 210
Cdd:cd03228 96 IL-----------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180
....*....|....*....|..
gi 2575808627 211 SAAQslSASLILVSHSDRVLKR 232
Cdd:cd03228 141 ALAK--GKTVIVIAHRLSTIRD 160
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
43-200 |
4.82e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQhCGFLFQDFRLF 122
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRTNTRAG--DLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
38-230 |
4.90e-22 |
|
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: 94.81 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 38 VPDGTGvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTesvRDRwRGQHCGFLFQ 117
Cdd:COG4618 339 VPPGSK-RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REE-LGRHIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRLFEdltaldnvllpltfrGTIA--------AHDR---ETAR-----EMlaargIRT-----NTRAGD----LSRGEM 172
Cdd:COG4618 414 DVELFD---------------GTIAeniarfgdADPEkvvAAAKlagvhEM-----ILRlpdgyDTRIGEggarLSGGQR 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2575808627 173 QRTALVRVLMGRPAVILADEPTANLDEArGDIVVDDLMSAAQSLSASLILVSHSDRVL 230
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDE-GEAALAAAIRALKARGATVVVITHRPSLL 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-228 |
7.87e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTlafsqcteSVRdrwrgqhCGFLFQDFRLF 122
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE--------TVK-------IGYFDQHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 -EDLTALDNVllpltfRGTIAAHDRETAREMLAA---RGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG0488 391 dPDKTVLDEL------RDGAPGGTEQEVRGYLGRflfSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 199 ----EArgdivvddLMSAAQSLSASLILVSHsDR 228
Cdd:COG0488 465 ietlEA--------LEEALDDFPGTVLLVSH-DR 489
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-198 |
1.02e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgTLAFSQCTESVRDRwr 108
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI---TLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 gqhcGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRTNTRAG--DLSRGEMQRTALVRVLMGRPA 186
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRiwQLSGGMRQRVGIARALAADPR 154
|
170
....*....|..
gi 2575808627 187 VILADEPTANLD 198
Cdd:COG4525 155 FLLMDEPFGALD 166
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
51-250 |
1.19e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.06 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-----TLAfsqctesVRDRwrgqHCGFLFQDFRLFEDL 125
Cdd:COG3839 22 IDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtDLP-------PKDR----NIAMVFQSYALYPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVLLPLTFRGT----IAAHDRETAR----EMLAARgirtntRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:COG3839 91 TVYENIAFPLKLRKVpkaeIDRRVREAAEllglEDLLDR------KPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 198 D-----EARGDIVvdDLMsaaQSLSASLILVSH--------SDRVlkrlpltAEIRAGRFI---TPDEL 250
Cdd:COG3839 165 DaklrvEMRAEIK--RLH---RRLGTTTIYVTHdqveamtlADRI-------AVMNDGRIQqvgTPEEL 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
51-233 |
1.66e-21 |
|
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: 89.09 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDrwrgqhCGFLFQDFRLFEDLTALDN 130
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDD 208
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLagLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180
....*....|....*....|....*
gi 2575808627 209 LMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRL 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
51-198 |
1.75e-21 |
|
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: 89.17 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGaMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlafsqCTESVRDRWRG--QHCGFLFQDFRLFEDLTAL 128
Cdd:cd03264 19 VSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRI-------DGQDVLKQPQKlrRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 129 DNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03264 91 EFLDYIAWLKGIPSKEVKARVDEVLELVNLgdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
52-245 |
1.91e-21 |
|
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: 92.94 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG--VVRWGTLAFSQCTESVRDRWRG-QHCGFLFQDFRLFEDLTAL 128
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWVDMTKPGPDGRGRAkRYIGILHQEYDLYPHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 129 DNVL------LPLTFRGTIAAH-------DRETAREMLaargirtNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTA 195
Cdd:TIGR03269 384 DNLTeaigleLPDELARMKAVItlkmvgfDEEKAEEIL-------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 196 NLDEARGDIVVDDLMSAAQSLSASLILVSHS-DRVLKRLPLTAEIRAGRFI 245
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-225 |
2.90e-21 |
|
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: 88.47 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDrwrgqhCGFLFQDFRLF 122
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD------IAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFRG----TIAAHDRETArEMLaarGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTAN 196
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKvpkdEIDERVREVA-ELL---QIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 197 LD-----EARGDIVvddlmSAAQSLSASLILVSH 225
Cdd:cd03301 161 LDaklrvQMRAELK-----RLQQRLGTTTIYVTH 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
52-233 |
3.73e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 90.94 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG-VVRWGTLAFSQ----CTESVRDRwrgqhCGFLFQDFRLFEDLT 126
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRTLFDSrkgiFLPPEKRR-----IGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 127 ALDNVLLPLTF-RGTIAAHDRETAREMLAArGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIV 205
Cdd:TIGR02142 92 VRGNLRYGMKRaRPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180
....*....|....*....|....*...
gi 2575808627 206 VDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRL 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
52-226 |
4.07e-21 |
|
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: 90.55 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSqcteSVRDRWRGQH---CGFLFQDFRLFEDLTA 127
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLgGEVLQD----SARGIFLPPHrrrIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLLPLTFRGTIAAH-DRETAREMLaarGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDI 204
Cdd:COG4148 95 RGNLLYGRKRAPRAERRiSFDEVVELL---GIGHllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180
....*....|....*....|..
gi 2575808627 205 VVDDLMSAAQSLSASLILVSHS 226
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHS 193
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
52-226 |
5.91e-21 |
|
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: 88.01 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGII-----TPTEGVVRW-GTLAFSQCTESVRDRWRgqhCGFLFQDFRLFeDL 125
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLdGKDIYDLDVDVLELRRR---VGMVFQKPNPF-PG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVLLPLTFRGTI-AAHDRETAREMLAARGI----RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-E 199
Cdd:cd03260 96 SIYDNVAYGLRLHGIKlKEELDERVEEALRKAALwdevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpI 175
|
170 180
....*....|....*....|....*..
gi 2575808627 200 ARGDIvvDDLMsAAQSLSASLILVSHS 226
Cdd:cd03260 176 STAKI--EELI-AELKKEYTIVIVTHN 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
43-230 |
8.67e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwrgqhcgFLFQDFRLF 122
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---------LMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLtfRGtiaaHDRETAREMLAARGIrtNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK11247 94 PWKKVIDNVGLGL--KG----QWRDAALQALAAVGL--ADRANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2575808627 199 eARGDIVVDDLM-SAAQSLSASLILVSH--------SDRVL 230
Cdd:PRK11247 166 -ALTRIEMQDLIeSLWQQHGFTVLLVTHdvseavamADRVL 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
52-229 |
1.96e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSqcteSVRDrwrGQHCG--FLFQDFRLFEDLTA 127
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFR----SPRD---AQAAGiaIIHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLL--PLTFRGTIaahD----RETAREMLAARG--IRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDE 199
Cdd:COG1129 97 AENIFLgrEPRRGGLI---DwramRRRARELLARLGldIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2575808627 200 ARgdivVDDLMSAAQSLSA---SLILVSH--------SDRV 229
Cdd:COG1129 174 RE----VERLFRIIRRLKAqgvAIIYISHrldevfeiADRV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
52-226 |
2.39e-20 |
|
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: 86.62 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDrwrgqhCGFLFQDFRLFEDLTALDNV 131
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD------ISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDL 209
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170
....*....|....*..
gi 2575808627 210 MSAAQSLSASLILVSHS 226
Cdd:cd03299 173 KKIRKEFGVTVLHVTHD 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-228 |
3.30e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgtlafsqcteSVRDRWRgqhCGFLFQDFRLF 122
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------SIPKGLR---IGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFRGTIA-------------------------------AHDRET-AREMLAARGIRT---NTRAGDL 167
Cdd:COG0488 74 DDLTVLDTVLDGDAELRALEaeleeleaklaepdedlerlaelqeefealgGWEAEArAEEILSGLGFPEedlDRPVSEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 168 SRGEMQRTALVRVLMGRPAVILADEPTANLdeargdivvdDLMSAA------QSLSASLILVSHsDR 228
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHL----------DLESIEwleeflKNYPGTVLVVSH-DR 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
53-233 |
3.67e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGI--ITPTEGVVRW-------------------------GTLA-----FSQCT 100
Cdd:TIGR03269 21 FTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvgepcpvcgGTLEpeevdFWNLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 101 ESVRDRWRGQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREML--AARGIRTNTRAGDLSRGEMQRTALV 178
Cdd:TIGR03269 101 DKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIemVQLSHRITHIARDLSGGEKQRVVLA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 179 RVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:TIGR03269 181 RQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
29-229 |
4.45e-20 |
|
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: 85.75 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIfscfDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwr 108
Cdd:cd03300 1 IELENVSKFYGGFVALDGV----SLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 gqHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 187 VILADEPTANLD-EARGDIVVdDLMSAAQSLSASLILVSH--------SDRV 229
Cdd:cd03300 151 VLLLDEPLGALDlKLRKDMQL-ELKRLQKELGITFVFVTHdqeealtmSDRI 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
52-250 |
6.51e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSQCTESVRdrwRGqhCGFLFQDFRLFEDLTALD 129
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRSPRDAIA---LG--IGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLL--PLTFRGTIaahDRETAREMLAARG------IRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL--DE 199
Cdd:COG3845 100 NIVLglEPTKGGRL---DRKAARARIRELSerygldVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpQE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 200 argdivVDDLMSAAQSLSA---SLILVSH--------SDRVlkrlpltAEIRAGRFI--------TPDEL 250
Cdd:COG3845 177 ------ADELFEILRRLAAegkSIIFITHklrevmaiADRV-------TVLRRGKVVgtvdtaetSEEEL 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-238 |
7.22e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.47 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 31 LETVRLDVPDGTgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctesVRDRWRgQ 110
Cdd:cd03231 1 LEADELTCERDG--RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIA-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 111 HCGFLFQDFRLFEDLTALDNvllpLTFRGTIaaHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:cd03231 74 GLLYLGHAPGIKTTLSVLEN----LRFWHAD--HSDEQVEEALARVGLNgfEDRPVAQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 189 LADEPTANLDEArGDIVVDDLMSAAQSLSASLILVSHSD-----RVLKRLPLTAE 238
Cdd:cd03231 148 ILDEPTTALDKA-GVARFAEAMAGHCARGGMVVLTTHQDlglseAGARELDLGFK 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
52-198 |
4.81e-19 |
|
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: 82.80 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwrgqhCGFLFQDFRLFEDLTALDNV 131
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-----LGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGtIAAHDRETAREMLAAR-GIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03266 100 EYFAGLYG-LKGDELTARLEELADRlGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
52-198 |
1.53e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDNV 131
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-RKIGMIFQHFNLLSSRTVAENV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG1135 104 ALPLEIAGVPKAEIRKRVAELLELVGLsdKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
51-233 |
1.76e-18 |
|
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: 81.33 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVR------WGTLAfsQCTESVRDRWRGQHCGFLFQDFRLFED 124
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggWVDLA--QASPREILALRRRTIGYVSQFLRVIPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 LTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRtnTRAGDL-----SRGEMQRTALVRVLMGRPAVILADEPTANLDE 199
Cdd:COG4778 108 VSALDVVAEPLLERGVDREEARARARELLARLNLP--ERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 200 ARGDIVVdDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:COG4778 186 ANRAVVV-ELIEEAKARGTAIIGIFHDEEVREAV 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
45-225 |
2.40e-18 |
|
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: 81.28 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG--VVRWG-TLAfsqcTESVRDrWRgQHCGF----LFQ 117
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndVRLFGeRRG----GEDVWE-LR-KRIGLvspaLQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRlfEDLTALDNVllpLT-FRGTIA------AHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:COG1119 90 RFP--RDETVLDVV---LSgFFDSIGlyreptDEQRERARELLELLGLahLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2575808627 189 LADEPTANLD-EARGDIV--VDDLmsaAQSLSASLILVSH 225
Cdd:COG1119 165 ILDEPTAGLDlGARELLLalLDKL---AAEGAPTLVLVTH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
43-198 |
3.14e-18 |
|
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: 80.85 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCF------DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctESVRDRwrgqHCGFLF 116
Cdd:cd03296 7 NVSKRFGDFvalddvSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQER----NVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 117 QDFRLFEDLTALDNVLLPLTFRGTI----AAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILA 190
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
....*...
gi 2575808627 191 DEPTANLD 198
Cdd:cd03296 161 DEPFGALD 168
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-256 |
3.34e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 30 SLETVRLDVPDGTGvrTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGII-----TPTEGVVR-WGTLAFSQCTESV 103
Cdd:PRK14267 4 AIETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRlFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 104 RDRwrgQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--------RTNTRAGDLSRGEMQRT 175
Cdd:PRK14267 82 EVR---REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAalwdevkdRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 176 ALVRVLMGRPAVILADEPTANLDEArGDIVVDDLMSAAQSlSASLILVSHSDRVLKRLP-LTAEIRAGRFItpdELTPSR 254
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPV-GTAKIEELLFELKK-EYTIVLVTHSPAQAARVSdYVAFLYLGKLI---EVGPTR 233
|
..
gi 2575808627 255 SI 256
Cdd:PRK14267 234 KV 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
55-198 |
1.00e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 55 LPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCteSVRDRwrgqHCGFLFQDFRLFEDLTALDNV--- 131
Cdd:PRK10851 25 IPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDR----KVGFVFQHYALFRHMTVFDNIafg 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 132 --LLPLTFRGTIAAHDRETAR--EM-----LAARgirtntRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK10851 99 ltVLPRRERPNAAAIKAKVTQllEMvqlahLADR------YPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
42-226 |
1.14e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 42 TGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgTLAFSQCTESVRDRWRgQHCGFLFQDFRL 121
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---LFEGEDISTLKPEIYR-QQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 122 FEDlTALDNVLLPLTFRGTiaAHDRETAREMLAARGIRTNT---RAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK10247 93 FGD-TVYDNLIFPWQIRNQ--QPDPAIFLDDLERFALPDTIltkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180
....*....|....*....|....*...
gi 2575808627 199 EARGDIVVDDLMSAAQSLSASLILVSHS 226
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
43-198 |
1.15e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctesvrdrWRG----QHCGFLFQD 118
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD--------WSPaelaRRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAA--------RGIRTntragdLSRGEMQRTALVRVLM------GR 184
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQvdlahlagRDYPQ------LSGGEQQRVQLARVLAqlwepdGP 158
|
170
....*....|....
gi 2575808627 185 PAVILADEPTANLD 198
Cdd:PRK13548 159 PRWLLLDEPTSALD 172
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
51-198 |
1.15e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 81.75 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-------TLafsqctESVRdrwrgQHCGFLFQDFRLFE 123
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirdlTL------ESLR-----RQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DlTALDNVLLpltfrGTIAAHD---RETAREMLAARGIRT-----NTRAGD----LSRGEMQRTALVRVLMGRPAVILAD 191
Cdd:COG1132 428 G-TIRENIRY-----GRPDATDeevEEAAKAAQAHEFIEAlpdgyDTVVGErgvnLSGGQRQRIAIARALLKDPPILILD 501
|
....*..
gi 2575808627 192 EPTANLD 198
Cdd:COG1132 502 EATSALD 508
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
45-198 |
2.69e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDR--WRGQHCGflfqdfrLF 122
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPG-------IK 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 123 EDLTALDNvllpLTFRGTIAAH-DRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK13538 87 TELTALEN----LRFYQRLHGPgDDEALWEALAQVGLagFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
51-198 |
3.45e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FD--FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPtegvvRWGTLA-------FSQCTESVRDRWRGQHCGFLFQDFRL 121
Cdd:PRK11124 19 FDitLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMP-----RSGTLNiagnhfdFSKTPSDKAIRELRRNVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 122 FEDLTALDNVL-LPLTFRGTIAAHDRETAREMLAArgIRTNTRAG----DLSRGEMQRTALVRVLMGRPAVILADEPTAN 196
Cdd:PRK11124 94 WPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLER--LRLKPYADrfplHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
..
gi 2575808627 197 LD 198
Cdd:PRK11124 172 LD 173
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-249 |
3.89e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW--GTLAFSQCTESvrdrwrgqhCGFL-FQDF 119
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEA---------CHYLgHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 120 rLFEDLTALDNVLLPLTFRGTiaahDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLM-GRPAVILaDEPTAN 196
Cdd:PRK13539 84 -MKPALTVAENLEFWAAFLGG----EELDIAAALEAVGLAplAHLPFGYLSAGQKRRVALARLLVsNRPIWIL-DEPTAA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2575808627 197 LDeARGDIVVDDLMSAAQSLSASLILVSHSDRvlkRLPLTAEIRAGRFITPDE 249
Cdd:PRK13539 158 LD-AAAVALFAELIRAHLAQGGIVIAATHIPL---GLPGARELDLGPFAAEDP 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
58-225 |
4.08e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgtLAFSQCTESVRDRwRGQ--------------HCGFLFQDFRLFE 123
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSI----VVNGQTINLVRDK-DGQlkvadknqlrllrtRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DLTALDNVL-LPLTFRGTIAAHDRETAREMLAARGIRTNTRAG---DLSRGEMQRTALVRVLMGRPAVILADEPTANLD- 198
Cdd:PRK10619 106 HMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDp 185
|
170 180
....*....|....*....|....*..
gi 2575808627 199 EARGDIVvdDLMSAAQSLSASLILVSH 225
Cdd:PRK10619 186 ELVGEVL--RIMQQLAEEGKTMVVVTH 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-225 |
4.48e-17 |
|
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: 77.32 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIfscfDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTlafSQCTESVRDRWr 108
Cdd:cd03269 1 LEVENVTKRFGRVTALDDI----SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 gqhcGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPA 186
Cdd:cd03269 73 ----GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELseYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2575808627 187 VILADEPTANLDEARGDiVVDDLMSAAQSLSASLILVSH 225
Cdd:cd03269 149 LLILDEPFSGLDPVNVE-LLKDVIRELARAGKTVILSTH 186
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
43-250 |
8.63e-17 |
|
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: 76.96 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQcTESVRDRwrgQHCGFLFQDFRLF 122
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVELR---RKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRTNTRAG----DLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03295 88 PHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryphELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 199 EARGDIVVDDLMSAAQSLSASLILVSHS-DRVLK---RLPLTAEIRAGRFITPDEL 250
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRladRIAIMKNGEIVQVGTPDEI 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-225 |
1.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFScFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQ--DFRLF 122
Cdd:PRK13643 20 RALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLTFrGTIAAHDRETAREMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDe 199
Cdd:PRK13643 99 EETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD- 176
|
170 180
....*....|....*....|....*.
gi 2575808627 200 ARGDIVVDDLMSAAQSLSASLILVSH 225
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-226 |
2.22e-16 |
|
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: 78.17 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 24 PQPFDLSLETVRLDVPDGTGVrtiFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTES- 102
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPV---LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDe 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 103 VRDRwrgqhCGFLFQDFRLFeDLTALDNVLLPltfRGTIAAHDRETARE------MLAARGIRTNTRAGD----LSRGEM 172
Cdd:TIGR02868 407 VRRR-----VSVCAQDAHLF-DTTVRENLRLA---RPDATDEELWAALErvgladWLRALPDGLDTVLGEggarLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 173 QRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLsaSLILVSHS 226
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
43-198 |
4.42e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgtlaFSQcTESVRDRWRGQH--CgFLFQDFR 120
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI------FID-GEDVTHRSIQQRdiC-MVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIrtntrAG-------DLSRGEMQRTALVRVLMGRPAVILADEP 193
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDL-----AGfedryvdQISGGQQQRVALARALILKPKVLLFDEP 163
|
....*
gi 2575808627 194 TANLD 198
Cdd:PRK11432 164 LSNLD 168
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
43-198 |
4.92e-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: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwRGqhCGFLFQDFRLF 122
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-LG--IGYLPQEASIF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575808627 123 EDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHlrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
52-250 |
6.40e-16 |
|
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: 74.33 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwrgqhCGFLFQDFRLFEDLTALDNV 131
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR-----IGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDL 209
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 210 MSAAQSLSASLILVSH--------SDRVlkrlpltAEIRAGRFI---TPDEL 250
Cdd:cd03265 175 EKLKEEFGMTILLTTHymeeaeqlCDRV-------AIIDHGRIIaegTPEEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
55-226 |
7.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.06 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 55 LPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQ--DFRLFEDLTALDNVL 132
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 133 LPLTFrGTIAAHDRETAREMLAARGIRTNTRAG---DLSRGEMQRTALVRVLMGRPAVILADEPTANLDeARGDivvDDL 209
Cdd:PRK13634 110 GPMNF-GVSEEDAKQKAREMIELVGLPEELLARspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKGR---KEM 184
|
170 180
....*....|....*....|.
gi 2575808627 210 MSAAQSL----SASLILVSHS 226
Cdd:PRK13634 185 MEMFYKLhkekGLTTVLVTHS 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
52-198 |
9.02e-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: 74.29 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVR-WGTLAFSQctesvRDRWRGQhCGFLF-QDFRLFEDLTALD 129
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvAGLVPWKR-----RKKFLRR-IGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2575808627 130 NVLLPLTFRGTIAAHDRETAR---EML-AARGIRTNTRAgdLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDelsELLdLEELLDTPVRQ--LSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
50-226 |
2.37e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 50 CFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtLAFSQCTESVRDRwrgQHCGFLFQDFRLFEDLTALD 129
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT---LNGQDHTTTPPSR---RPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA-RGDIV- 205
Cdd:PRK10771 91 NIGLGLNPGLKLNAAQREKLHAIARQMGIEDllARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlRQEMLt 170
|
170 180
....*....|....*....|..
gi 2575808627 206 -VDDLMSAAQslsASLILVSHS 226
Cdd:PRK10771 171 lVSQVCQERQ---LTLLMVSHS 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-214 |
2.69e-15 |
|
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: 71.81 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 33 TVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSG--IITPTEGVVRW-GTlafsqcteSVRDRWRG 109
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGR--------PLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 110 QHCGFLFQDFRLFEDLTAldnvllpltfrgtiaahdRETAreMLAA--RGIrtntragdlSRGEMQRTALVRVLMGRPAV 187
Cdd:cd03213 82 KIIGYVPQDDILHPTLTV------------------RETL--MFAAklRGL---------SGGERKRVSIALELVSNPSL 132
|
170 180
....*....|....*....|....*..
gi 2575808627 188 ILADEPTANLDEARGDIVVDDLMSAAQ 214
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-233 |
2.73e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG-------VVRWGTLAFSqcTESVRDRwrgQHCGFLFQ 117
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkikvdgkVLYFGKDIFQ--IDAIKLR---KEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRLFEDLTALDNVLLPLTFRGTIAAHD-RETAREMLAARGI------RTNTRAGDLSRGEMQRTALVRVLMGRPAVILA 190
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREiKKIVEECLRKVGLwkevydRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2575808627 191 DEPTANLDEARGDiVVDDLMSAAQSlSASLILVSHSDRVLKRL 233
Cdd:PRK14246 178 DEPTSMIDIVNSQ-AIEKLITELKN-EIAIVIVSHNPQQVARV 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
53-198 |
4.52e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlafsqctESVRDRWRGQHCGFLFQDFRLFEDLTALDNVL 132
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL---------DGKPVEGPGAERGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575808627 133 LPLTFRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVGLEgaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-198 |
7.43e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVpdGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTesvrDRWR 108
Cdd:PRK11231 1 MTLRTENLTV--GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS----SRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTALDNVLL---P-LTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLM 182
Cdd:PRK11231 75 ARRLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHlaDRRLTDLSGGQRQRAFLAMVLA 154
|
170
....*....|....*.
gi 2575808627 183 GRPAVILADEPTANLD 198
Cdd:PRK11231 155 QDTPVVLLDEPTTYLD 170
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
43-225 |
1.40e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrW------GTLAFSQCTEsVRDRwrgqhCGFLF 116
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LfdgeniPAMSRSRLYT-VRKR-----MSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 117 QDFRLFEDLTALDNVLLPLTFRGTI-AAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEP 193
Cdd:PRK11831 91 QSGALFTDMNVFDNVAYPLREHTQLpAPLLHSTVMMKLEAVGLRgaAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2575808627 194 TANLDEARGDIVV---DDLMSAaqsLSASLILVSH 225
Cdd:PRK11831 171 FVGQDPITMGVLVkliSELNSA---LGVTCVVVSH 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
40-250 |
1.45e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 40 DGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQDF 119
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 120 RLFEDLTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRTNTRA--GDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSypDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 198 DEARGDIVVDDLMSAAQSLSASLILVSH----SDRVLKRLPLTAEIRAGRFITPDEL 250
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHdldeAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
52-233 |
1.74e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQDFRLFEDLTALDNV 131
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQIGMIFQHFNLLSSRTVFDNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDL 209
Cdd:PRK11153 104 ALPLELAGTPKAEIKARVTELLELVGLsdKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELL 183
|
170 180
....*....|....*....|....
gi 2575808627 210 MSAAQSLSASLILVSHSDRVLKRL 233
Cdd:PRK11153 184 KDINRELGLTIVLITHEMDVVKRI 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-200 |
1.79e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 24 PQPFDLSLETVRLDVPDGtgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsqctesv 103
Cdd:COG4178 358 SEDGALALEDLTLRTPDG---RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 104 rdRWRGQHCGFLFQdfRLFEDLTALDNVLL-PltfrGTIAAHDRETAREMLAARGI-----RTNTRAgD----LSRGEMQ 173
Cdd:COG4178 422 --RPAGARVLFLPQ--RPYLPLGTLREALLyP----ATAEAFSDAELREALEAVGLghlaeRLDEEA-DwdqvLSLGEQQ 492
|
170 180
....*....|....*....|....*..
gi 2575808627 174 RTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEE 519
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
44-245 |
2.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 44 VRTIFSCFDFKLP--------------QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW---------GTLAFSQCT 100
Cdd:PRK13651 5 VKNIVKIFNKKLPtelkaldnvsveinQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 101 ESV---RDRWRG--------QHCGFLFQ--DFRLFEDLTALDNVLLPLTFrGTIAAHDRETAREMLAARGIRTN--TRAG 165
Cdd:PRK13651 85 EKLviqKTRFKKikkikeirRRVGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESylQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 166 -DLSRGEMQRTALVRVLMGRPAVILADEPTANLDEArGDIVVDDLMSAAQSLSASLILVSHS-DRVLKRLPLTAEIRAGR 243
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ-GVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGK 242
|
..
gi 2575808627 244 FI 245
Cdd:PRK13651 243 II 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
53-232 |
3.28e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.21 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlaFSQCTESVRDRWRGQHCgFLFQDFRLFEDLTALDNVL 132
Cdd:PRK13540 22 FHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF----ERQSIKKDLCTYQKQLC-FVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 133 LPLTFRGTIAAHDrETARemLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEaRGDIVVDDLMSA 212
Cdd:PRK13540 97 YDIHFSPGAVGIT-ELCR--LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE-LSLLTIITKIQE 172
|
170 180
....*....|....*....|
gi 2575808627 213 AQSLSASLILVSHSDRVLKR 232
Cdd:PRK13540 173 HRAKGGAVLLTSHQDLPLNK 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
52-225 |
4.06e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItPTEGVVRWGTLAFSQCTESvrdRWRgQHCGFLFQDFRLFEDlTALDNV 131
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPE---SWR-KHLSWVGQNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLpltfrGTIAAHDRET--------AREMLAARGIRTNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLDE 199
Cdd:PRK11174 444 LL-----GNPDASDEQLqqalenawVSEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180
....*....|....*....|....*.
gi 2575808627 200 ARGDIVVDDLMSAAQSLsaSLILVSH 225
Cdd:PRK11174 519 HSEQLVMQALNAASRRQ--TTLMVTH 542
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
41-228 |
4.39e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 41 GTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlafsqcTESVRdrwrgqhCGFLFQD-- 118
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--------SENAN-------IGYYAQDha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 --FRlfEDLTALDnvllpLTFRGTIAAHDRETAREML-----AARGIRTNTRAgdLSRGEMQRTALVRVLMGRPAVILAD 191
Cdd:PRK15064 393 ydFE--NDLTLFD-----WMSQWRQEGDDEQAVRGTLgrllfSQDDIKKSVKV--LSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190
....*....|....*....|....*....|....*...
gi 2575808627 192 EPTANLD-EArgdivVDDLMSAAQSLSASLILVSHsDR 228
Cdd:PRK15064 464 EPTNHMDmES-----IESLNMALEKYEGTLIFVSH-DR 495
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
43-228 |
4.46e-14 |
|
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: 67.47 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG---TLA-FSQctesvrdrwrgqhcgflfqd 118
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGstvKIGyFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 frlfedltaldnvllpltfrgtiaahdretaremlaargirtntragdLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190
....*....|....*....|....*....|.
gi 2575808627 199 -EARgDIVVDDLmsaaQSLSASLILVSHsDR 228
Cdd:cd03221 103 lESI-EALEEAL----KEYPGTVILVSH-DR 127
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
52-225 |
6.64e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQ--DFRLFEDlTALD 129
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE-TVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLL-PLTFrGTIAAHDRETAREMLAARGIRTNTRAG---DLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA-Rgdi 204
Cdd:PRK13649 106 DVAFgPQNF-GVSQEEAEALAREKLALVGISESLFEKnpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKgR--- 181
|
170 180
....*....|....*....|....
gi 2575808627 205 vvDDLMSAAQSLSAS---LILVSH 225
Cdd:PRK13649 182 --KELMTLFKKLHQSgmtIVLVTH 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
46-198 |
1.43e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 46 TIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafSQCTESVRDRWRgqHCGFLFQDFRLFEDL 125
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD----GQDITHVPAENR--HVNTVFQSYALFPHM 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 126 TALDNVLLPLTFRGTIAAHDRETAREMLaaRGIR----TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK09452 102 TVFENVAFGLRMQKTPAAEITPRVMEAL--RMVQleefAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
52-230 |
1.52e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSQCTESVRD-RWRGQhcgFLFQD--FRLFEDLTA 127
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDLLGMKDDEWRAvRSDIQ---MIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLLPL-TFRGTIAAHD-RETAREMLAARGIR---TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARG 202
Cdd:PRK15079 118 GEIIAEPLrTYHPKLSRQEvKDRVKAMMLKVGLLpnlINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 2575808627 203 DIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHdlavvkhiSDRVL 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-253 |
2.35e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlafsqCTESV--RDRWRGQHCGFLFQDFR 120
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL-------CGEPVpsRARHARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFEDLTALDNVLLPLTFRGTIAAHDRETAREML--AARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK13537 91 LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLefAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 199 -EARGDI--VVDDLMSAAQSLSASLILVSHSDRVLKRLPLtaeIRAGRFIT---PDELTPS 253
Cdd:PRK13537 171 pQARHLMweRLRSLLARGKTILLTTHFMEEAERLCDRLCV---IEEGRKIAegaPHALIES 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
52-198 |
4.67e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgtlafsqctesvrdRWRGQHCGFL-------------FQD 118
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI----------------LLRGQHIEGLpghqiarmgvvrtFQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVLLPL-------TFRGTIAAHD-RETAREML--AAR-----GIR--TNTRAGDLSRGEMQRTALVRVL 181
Cdd:PRK11300 89 VRLFREMTVIENLLVAQhqqlktgLFSGLLKTPAfRRAESEALdrAATwlervGLLehANRQAGNLAYGQQRRLEIARCM 168
|
170
....*....|....*..
gi 2575808627 182 MGRPAVILADEPTANLD 198
Cdd:PRK11300 169 VTQPEILMLDEPAAGLN 185
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
52-229 |
6.47e-13 |
|
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: 64.76 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqctesvrdrwrGQhcgflfqdfrlfedltaldnv 131
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD----------------GK--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 llPLTFRGTIAAHdretaremlaARGIRTNTRagdLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVdDLMS 211
Cdd:cd03216 63 --EVSFASPRDAR----------RAGIAMVYQ---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVIR 126
|
170 180
....*....|....*....|....*.
gi 2575808627 212 AAQSLSASLILVSH--------SDRV 229
Cdd:cd03216 127 RLRAQGVAVIFISHrldevfeiADRV 152
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-233 |
7.27e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGII--TPTEGVVRWGTLAFSQctesvrdrwrgqhcgflfqdfrlf 122
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR------------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 eDLTALDNVLLPLTFrgtiaahdrETAREMLAARGIRTN----TRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG2401 99 -EASLIDAIGRKGDF---------KDAVELLNAVGLSDAvlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|....*
gi 2575808627 199 EARGDIVVDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
53-226 |
8.57e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.39 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgTLAFSQCT-----ESVRDRWRGQHCGFLFQDFRLFEDlTA 127
Cdd:PRK13641 28 FELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---TIAGYHITpetgnKNLKKLRKKVSLVFQFPEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLL-PLTFrGTIAAHDRETAREMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARG 202
Cdd:PRK13641 104 LKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLSEdliSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpEGRK 182
|
170 180
....*....|....*....|....
gi 2575808627 203 DIVvdDLMSAAQSLSASLILVSHS 226
Cdd:PRK13641 183 EMM--QLFKDYQKAGHTVILVTHN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-198 |
8.80e-13 |
|
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: 65.76 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 27 FDLSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItpTEGVVRWGTLAFSQCtESVRDR 106
Cdd:cd03234 2 RVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQ-PRKPDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 107 WRgQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTiaAHDRETAREMLAA-RGIR--TNTRAGD-----LSRGEMQRTALV 178
Cdd:cd03234 79 FQ-KCVAYVRQDDILLPGLTVRETLTYTAILRLP--RKSSDAIRKKRVEdVLLRdlALTRIGGnlvkgISGGERRRVSIA 155
|
170 180
....*....|....*....|
gi 2575808627 179 RVLMGRPAVILADEPTANLD 198
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLD 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-233 |
9.24e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 28 DLSLeTVRLDVPdGTGVRTIFscfdfklpqgamlgirGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSQCTESVRD 105
Cdd:PRK11144 12 DLCL-TVNLTLP-AQGITAIF----------------GRSGAGKTSLINAISGLTRPQKGRIVLNgrVLFDAEKGICLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 106 RWRgqHCGFLFQDFRLFEDLTALDNvlLPLTFRGTIAAH-DRETarEMLaarGIRT--NTRAGDLSRGEMQRTALVRVLM 182
Cdd:PRK11144 74 EKR--RIGYVFQDARLFPHYKVRGN--LRYGMAKSMVAQfDKIV--ALL---GIEPllDRYPGSLSGGEKQRVAIGRALL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 183 GRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHS-DRVLkRL 233
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSlDEIL-RL 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
52-225 |
2.81e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQHCGFLFQ--DFRLFEDLTALD 129
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFEDTVERE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTFRGTIAaHDRETAREMLAARGIRTNTRAGD---LSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVV 206
Cdd:PRK13646 107 IIFGPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170
....*....|....*....
gi 2575808627 207 DDLMSAAQSLSASLILVSH 225
Cdd:PRK13646 186 RLLKSLQTDENKTIILVSH 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-198 |
3.37e-12 |
|
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: 64.17 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCT-ESVRdrwrgQHCGFLFQDFRLFE 123
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLR-----RAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DlTALDNVLLpltfrGTIAAHDRETAREMLAARgIRT---------NTRAGD----LSRGEMQRTALVRVLMGRPAVILA 190
Cdd:cd03253 89 D-TIGYNIRY-----GRPDATDEEVIEAAKAAQ-IHDkimrfpdgyDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
|
....*...
gi 2575808627 191 DEPTANLD 198
Cdd:cd03253 162 DEATSALD 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
57-225 |
5.35e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 57 QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDrwrgqhCGFLFQDFRLFEDLTALDNVLLPLT 136
Cdd:PRK11607 44 KGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP------INMMFQSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 137 FRGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQ 214
Cdd:PRK11607 118 QDKLPKAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILE 197
|
170
....*....|.
gi 2575808627 215 SLSASLILVSH 225
Cdd:PRK11607 198 RVGVTCVMVTH 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
39-225 |
7.44e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 39 PDGTGVRTIFScfdFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTEsvrdRWRGQHCGFLFQ- 117
Cdd:PRK13647 15 KDGTKALKGLS---LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE----KWVRSKVGLVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 -DFRLFEDlTALDNVLLPLTFRGTIAAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:PRK13647 88 pDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDfrDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 195 ANLDeARGDivvDDLMSAAQSLSA---SLILVSH 225
Cdd:PRK13647 167 AYLD-PRGQ---ETLMEILDRLHNqgkTVIVATH 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-231 |
1.25e-11 |
|
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: 61.40 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGtgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsqctesvrdrwR 108
Cdd:cd03223 1 IELENLSLATPDG---RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------------M 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFR-LFEDLTALDNVLLPLtfrgtiaahDREtaremlaargirtntragdLSRGEMQRTALVRVLMGRPAV 187
Cdd:cd03223 61 PEGEDLLFLPQRpYLPLGTLREQLIYPW---------DDV-------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2575808627 188 ILADEPTANLDEArgdiVVDDLMSAAQSLSASLILVSHSDRVLK 231
Cdd:cd03223 113 VFLDEATSALDEE----SEDRLYQLLKELGITVISVGHRPSLWK 152
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-230 |
1.39e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 34 VRLDVpDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSqcteSVRDRWRgQH 111
Cdd:COG1129 255 VVLEV-EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIR----SPRDAIR-AG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 112 CGFLFQDfR----LFEDLTALDNVLLP----LTFRGTI-AAHDRETAREMLAARGIRT---NTRAGDLSRGEMQRTALVR 179
Cdd:COG1129 329 IAYVPED-RkgegLVLDLSIRENITLAsldrLSRGGLLdRRRERALAEEYIKRLRIKTpspEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 180 VLMGRPAVILADEPTANLD-EARGDI--VVDDLmsAAQSLsaSLILVS--------HSDRVL 230
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDvGAKAEIyrLIREL--AAEGK--AVIVISselpellgLSDRIL 465
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
43-198 |
2.06e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.32 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAfsqcTESVRDRWRGQHCGFLFQDFRLF 122
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDD----VEALSARAASRRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLLPLT-----FRGTIAAHDRETAREMLAARGIRTNTRAGD-LSRGEMQRTALVRVLMGRPAVILADEPTAN 196
Cdd:PRK09536 90 FEFDVRQVVEMGRTphrsrFDTWTETDRAAVERAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
..
gi 2575808627 197 LD 198
Cdd:PRK09536 170 LD 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
52-198 |
2.32e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.43 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFsqcTESVRDRW------RGqhcgflfqdfrLFEDL 125
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIgylpeeRG-----------LYPKM 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 126 TALDNVLLPLTFRGTIAAHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG4152 87 KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLgdRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
45-198 |
2.47e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwRGqhCGFLFQDFRLFED 124
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-RG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 125 LTALDNVLLPLTFRGTIAAHDRET-AREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-198 |
2.58e-11 |
|
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: 63.03 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 37 DVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqctESVRDRWRGQHCGFLF 116
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ETVKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 117 QDFRLFEDLT-ALDNVLLpltfrgtiaaHDRET-AREMLAA---RGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILAD 191
Cdd:TIGR03719 399 PNKTVWEEISgGLDIIKL----------GKREIpSRAYVGRfnfKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
....*..
gi 2575808627 192 EPTANLD 198
Cdd:TIGR03719 469 EPTNDLD 475
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-198 |
2.89e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.02 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 31 LETVRL--DVPDGTGVrtiFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTES---VRd 105
Cdd:PRK13639 2 LETRDLkySYPDGTEA---LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 106 rwrgQHCGFLFQ--DFRLFEDLTALDNVLLPLTFrGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVL 181
Cdd:PRK13639 78 ----KTVGIVFQnpDDQLFAPTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEgfENKPPHHLSGGQKKRVAIAGIL 152
|
170
....*....|....*..
gi 2575808627 182 MGRPAVILADEPTANLD 198
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLD 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
47-225 |
3.34e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 47 IFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqcTESVRDRWRGQHCGFLFQDFRLFEDLT 126
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID-------GKTATRGDRSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 127 ALDNVLLPLTFRGTiaaHDRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDeARGDI 204
Cdd:PRK13543 99 TLENLHFLCGLHGR---RAKQMPGSALAIVGLagYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGIT 174
|
170 180
....*....|....*....|.
gi 2575808627 205 VVDDLMSAAQSLSASLILVSH 225
Cdd:PRK13543 175 LVNRMISAHLRGGGAALVTTH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
52-198 |
5.02e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsqctesVRDR--WR-----GQHCGFLF-QDFRLFE 123
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------------VLGYvpFKrrkefARRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DLTALDnvllplTFR--GTI-----AAHDR--ETAREMLAARGI-RTNTRagDLSRGEMQRTALVRVLMGRPAVILADEP 193
Cdd:COG4586 110 DLPAID------SFRllKAIyripdAEYKKrlDELVELLDLGELlDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEP 181
|
....*
gi 2575808627 194 TANLD 198
Cdd:COG4586 182 TIGLD 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
34-230 |
6.42e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 34 VRLDVPD--GTGVRTIfscfDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlaFSQCTESVRDRWRGQH 111
Cdd:PRK10762 256 VRLKVDNlsGPGVNDV----SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT-----LDGHEVVTRSPQDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 112 CGFLFqdfrLFED-----------------LTALDNvllpLTFRGTIAAHDRE--TAREMLAARGIRTNTR---AGDLSR 169
Cdd:PRK10762 327 NGIVY----ISEDrkrdglvlgmsvkenmsLTALRY----FSRAGGSLKHADEqqAVSDFIRLFNIKTPSMeqaIGLLSG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 170 GEMQRTALVRVLMGRPAVILADEPTANLD-EARGDIVvdDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDvGAKKEIY--QLINQFKAEGLSIILVSSempevlgmSDRIL 466
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
52-198 |
8.80e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGII-----TPTEGVVRW-GTLAFSQCTESVRDRWRgqhcgFLFQDFRLFEDL 125
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLdGQDIFKMDVIELRRRVQ-----MVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVLLPLTFRGTIAAHD--RETAREMLAARGI------RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKelQERVRWALEKAQLwdevkdRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
.
gi 2575808627 198 D 198
Cdd:PRK14247 178 D 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
46-225 |
1.35e-10 |
|
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: 58.86 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 46 TIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwrgQHCGFLFQDFRLFeDL 125
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS-----SLISVLNQRPYLF-DT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVllpltfrgtiaahdretaremlaarGIRtntragdLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIV 205
Cdd:cd03247 90 TLRNNL-------------------------GRR-------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180
....*....|....*....|
gi 2575808627 206 VDDLMSAAQslSASLILVSH 225
Cdd:cd03247 138 LSLIFEVLK--DKTLIWITH 155
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
65-226 |
1.40e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGI------ITPTEGVVRWGTLAFSQCTESVRDRwrgQHCGFLFQDFRLFEdLTALDNVLLPLTFR 138
Cdd:PRK14239 38 GPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIYSPRTDTVDLR---KEIGMVFQQPNPFP-MSIYENVVYGLRLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 139 GTiaaHDRETAREM----LAARGI------RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDD 208
Cdd:PRK14239 114 GI---KDKQVLDEAveksLKGASIwdevkdRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEET 190
|
170
....*....|....*...
gi 2575808627 209 LMSAAQSLsaSLILVSHS 226
Cdd:PRK14239 191 LLGLKDDY--TMLLVTRS 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
43-225 |
1.68e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsqctesvrdRWRGQHCGFLFQdfRLF 122
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYVPQ--KLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTaldnvlLPLT------FRGTIAAHDRETAREMLAArGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTAN 196
Cdd:PRK09544 78 LDTT------LPLTvnrflrLRPGTKKEDILPALKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|
gi 2575808627 197 LDeARGDIVVDDLMSA-AQSLSASLILVSH 225
Cdd:PRK09544 151 VD-VNGQVALYDLIDQlRRELDCAVLMVSH 179
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
58-225 |
1.83e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPteGVVRWGTLAFSQcteSVRDRWRGQH-CGFLFQDFRLFEDLTALDNVLLPLT 136
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNG---MPIDAKEMRAiSAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 137 FR---GTIAAHDRETAREMLAARGIRT--NTRAGD------LSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIV 205
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLRKcaNTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180
....*....|....*....|
gi 2575808627 206 VDDLMSAAQSlSASLILVSH 225
Cdd:TIGR00955 206 VQVLKGLAQK-GKTIICTIH 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
53-225 |
2.37e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQD------------FR 120
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQNpygslnprkkvgQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFEDL---TALDnvllpltfrgtiAAHDRETAREMLAARGIRTN--TRAGDL-SRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:PRK11308 115 LEEPLlinTSLS------------AAERREKALAMMAKVGLRPEhyDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190
....*....|....*....|....*....|.
gi 2575808627 195 ANLDEARGDIVVDDLMSAAQSLSASLILVSH 225
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
53-198 |
3.38e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG--VVRWGTLAFSQCtesvrdRWRGQHCGFLFQDfrlfeDLTALD- 129
Cdd:PRK15112 34 FTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelLIDDHPLHFGDY------SYRSQRIRMIFQD-----PSTSLNp 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 130 -----NVL-LPLTFRGTIAAHDRETA-REMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK15112 103 rqrisQILdFPLRLNTDLEPEQREKQiIETLRQVGLLPdhaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
52-233 |
4.00e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwrgQHCGFLFQDFRLFEDLTALDNV 131
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ---LGIGIIYQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 L---LPLTFRGTIAAHD----RETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARg 202
Cdd:PRK09700 102 YigrHLTKKVCGVNIIDwremRVRAAMMLLRVGLKVdlDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE- 180
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 203 divVDDL---MSAAQSLSASLILVSHSDRVLKRL 233
Cdd:PRK09700 181 ---VDYLfliMNQLRKEGTAIVYISHKLAEIRRI 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-225 |
5.67e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.32 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVrtiFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRwr 108
Cdd:PRK13636 6 LKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQ--DFRLF-----EDLT-ALDNVLLPltfrgtiAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALV 178
Cdd:PRK13636 81 RESVGMVFQdpDNQLFsasvyQDVSfGAVNLKLP-------EDEVRKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2575808627 179 RVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH 225
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
50-225 |
5.97e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 50 CFD--FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-----GTLAFSQCTESVRDRWRGQHCGFLFQDFR-- 120
Cdd:PRK11701 22 CRDvsFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERRRLLRTEWGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFEDLTALDNV---LLPLTFR--GTIaahdRETAREMLAARGIRTNtRAGDLSR---GEM-QRTALVRVLMGRPAVILAD 191
Cdd:PRK11701 102 LRMQVSAGGNIgerLMAVGARhyGDI----RATAGDWLERVEIDAA-RIDDLPTtfsGGMqQRLQIARNLVTHPRLVFMD 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 2575808627 192 EPTANLD---EARgdiVVDDLMSAAQSLSASLILVSH 225
Cdd:PRK11701 177 EPTGGLDvsvQAR---LLDLLRGLVRELGLAVVIVTH 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
47-198 |
7.24e-10 |
|
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: 57.55 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 47 IFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgTLAfsqcTESVRD---RWRGQHCGFLFQDFRLFe 123
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI---LLD----GVDIRDlnlRWLRSQIGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DLTALDNVLLPLtfRGTIAAHDRETAREMLAARGIRT-----NTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:cd03249 90 DGTIAENIRYGK--PDATDEEVEEAAKKANIHDFIMSlpdgyDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
....
gi 2575808627 195 ANLD 198
Cdd:cd03249 168 SALD 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
65-198 |
9.65e-10 |
|
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: 58.87 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRdrwrgQHCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAH 144
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-----QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEE 1037
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 145 DRETAREMLAARGI--RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-226 |
1.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 41 GTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-TLAFSQCTESVRD--RWRgQHCGFLFQ 117
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGdVLLGGRSIFNYRDvlEFR-RRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRLFEdLTALDNVLLPL---------TFRGTiaAHDRETAREMLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:PRK14271 109 RPNPFP-MSIMDNVLAGVrahklvprkEFRGV--AQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 2575808627 189 LADEPTANLDEARGDIVVDDLMSAAQSLsaSLILVSHS 226
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHN 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
43-233 |
1.30e-09 |
|
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: 56.77 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgtlafsqcTESVRDRWR-GQHCGFLfqdfrl 121
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV----------TVRGRVSSLlGLGGGFN------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 122 fEDLTALDNVLlpltFRGTIAAHDRETAREML------AARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTA 195
Cdd:cd03220 97 -PELTGRENIY----LNGRLLGLSRKEIDEKIdeiiefSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2575808627 196 NLDEA---RGDIVVDDLMSAAqslsASLILVSHSDRVLKRL 233
Cdd:cd03220 172 VGDAAfqeKCQRRLRELLKQG----KTVILVSHDPSSIKRL 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
42-205 |
1.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.73 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 42 TGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG-VVRWGTLAFSQCTESVRdrwrgQHCGFLFQ--D 118
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsVLIRGEPITKENIREVR-----KFVGLVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVLLP--LTFRGTIAAHDRETAREMLAARGIRTNTrAGDLSRGEMQRTALVRVLMGRPAVILADEPTAN 196
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPinLGLDEETVAHRVSSALHMLGLEELRDRV-PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170
....*....|
gi 2575808627 197 LD-EARGDIV 205
Cdd:PRK13652 168 LDpQGVKELI 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
65-200 |
2.00e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGIITPTEGVVRWGtlafSQCTESVRDRWRGqhCGFLFQDFRLFEDLTALDNVLLPLTFRGTIAAH 144
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIG----EKRMNDVPPAERG--VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 145 DR---ETAREMLAArGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:PRK11000 110 INqrvNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-198 |
2.47e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 31 LETVRLDVPDGTGVRTIfSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctESVRDRWRgQ 110
Cdd:COG3845 258 LEVENLSVRDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG--LSPRERRR-L 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 111 HCGFLFQDfRLFE----DLTALDNVLL------PLTFRGTI---AAhdRETAREMLAARGIRT---NTRAGDLSRGEMQR 174
Cdd:COG3845 334 GVAYIPED-RLGRglvpDMSVAENLILgryrrpPFSRGGFLdrkAI--RAFAEELIEEFDVRTpgpDTPARSLSGGNQQK 410
|
170 180
....*....|....*....|....
gi 2575808627 175 TALVRVLMGRPAVILADEPTANLD 198
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
51-198 |
2.74e-09 |
|
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: 55.70 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCT-ESVRdrwrgQHCGFLFQDFRLFEDlTALD 129
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLR-----RQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVllpltfrgTIAAHDRETAREMLAAR-------------GIRTNT--RAGDLSRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:cd03251 95 NI--------AYGRPGATREEVEEAARaanahefimelpeGYDTVIgeRGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
....
gi 2575808627 195 ANLD 198
Cdd:cd03251 167 SALD 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
53-250 |
2.99e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCT-ESVRdrwrgQHCGFLFQDFRLFeDLTALDNV 131
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTrASLR-----RNIAVVFQDAGLF-NRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LL---PLTFRGTIAAHDRETAREMLAARGIRTNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLD---EAR 201
Cdd:PRK13657 430 RVgrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDvetEAK 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 202 GDIVVDDLMSA------AQSLS----ASLILVSHSDRVlkrlpltaeIRAGRFitpDEL 250
Cdd:PRK13657 510 VKAALDELMKGrttfiiAHRLStvrnADRILVFDNGRV---------VESGSF---DEL 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-228 |
4.62e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTlafsqctesvrdrwrGQHCGFLFQDFRLFEDLTALDNVLLPL-- 135
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP---------------GIKVGYLPQEPQLDPTKTVRENVEEGVae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 136 ------------------------------TFRGTIAAH-----DRETAREMLAARGIRTNTRAGDLSRGEMQRTALVRV 180
Cdd:TIGR03719 96 ikdaldrfneisakyaepdadfdklaaeqaELQEIIDAAdawdlDSQLEIAMDALRCPPWDADVTKLSGGERRRVALCRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2575808627 181 LMGRPAVILADEPTANLD-EArgdivVDDLMSAAQSLSASLILVSHsDR 228
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDaES-----VAWLERHLQEYPGTVVAVTH-DR 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-201 |
4.70e-09 |
|
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: 55.49 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLP-------QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW--GTLAF------SQCTESVRDRWRGQHCGFLF 116
Cdd:cd03237 12 EFTLEveggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIelDTVSYkpqyikADYEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 117 QDFRLFEdltaldnVLLPLTFRGTIaahDRETAremlaargirtntragDLSRGEMQRTALVRVLmGRPAVI-LADEPTA 195
Cdd:cd03237 92 HPYFKTE-------IAKPLQIEQIL---DREVP----------------ELSGGELQRVAIAACL-SKDADIyLLDEPSA 144
|
....*..
gi 2575808627 196 NLD-EAR 201
Cdd:cd03237 145 YLDvEQR 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
53-198 |
7.01e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLP---QGAMLGIRGPSGAGKTSFLKCLSGIITP----TEGVVRWgtlafsqctESVRDRWRGQHcgflFQDFrlFEDL 125
Cdd:PRK13409 91 YGLPipkEGKVTGILGPNGIGKTTAVKILSGELIPnlgdYEEEPSW---------DEVLKRFRGTE----LQNY--FKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TA-----------LDnvLLPLTFRGTI-----AAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMgRPA- 186
Cdd:PRK13409 156 YNgeikvvhkpqyVD--LIPKVFKGKVrellkKVDERGKLDEVVERLGLENilDRDISELSGGELQRVAIAAALL-RDAd 232
|
170
....*....|..
gi 2575808627 187 VILADEPTANLD 198
Cdd:PRK13409 233 FYFFDEPTSYLD 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-225 |
7.08e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSQCTESVrdrwrgqHCG--FLFQDFRLFEDLTAL 128
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqEMRFASTTAAL-------AAGvaIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 129 DNVLL---PLTF----RGTIaahdRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLdE 199
Cdd:PRK11288 98 ENLYLgqlPHKGgivnRRLL----NYEAREQLEHLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL-S 172
|
170 180
....*....|....*....|....*....
gi 2575808627 200 ARGdivVDDLMSAAQSLSAS---LILVSH 225
Cdd:PRK11288 173 ARE---IEQLFRVIRELRAEgrvILYVSH 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
43-198 |
9.42e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 43 GVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGtlafsqctESVRDRWRGQHCGFLFQDFRLF 122
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------ETVKLAYVDQSRDALDPNKTVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLT-ALDNVLLpltfrgtiaaHDRET-AREMLAA---RGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:PRK11819 407 EEISgGLDIIKV----------GNREIpSRAYVGRfnfKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
.
gi 2575808627 198 D 198
Cdd:PRK11819 477 D 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
58-198 |
1.11e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTlafsqctesvrdrwrGQHCGFLFQDFRLFEDLTALDNVLLPLtf 137
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP---------------GIKVGYLPQEPQLDPEKTVRENVEEGV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 138 RGTIAAHDR----------------ETAREM--------------------LAARGIRT---NTRAGDLSRGEMQRTALV 178
Cdd:PRK11819 96 AEVKAALDRfneiyaayaepdadfdALAAEQgelqeiidaadawdldsqleIAMDALRCppwDAKVTKLSGGERRRVALC 175
|
170 180
....*....|....*....|
gi 2575808627 179 RVLMGRPAVILADEPTANLD 198
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLD 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
52-233 |
1.12e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFsqctesvrdrwrgqhcgflfqdfrLFE------- 123
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRVSA------------------------LLElgagfhp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DLTALDNVLlpltFRGTIAAHDRETAREMLAA------------RGIRTntragdLSRGeMQrtalVRVLMG-----RPA 186
Cdd:COG1134 102 ELTGRENIY----LNGRLLGLSRKEIDEKFDEivefaelgdfidQPVKT------YSSG-MR----ARLAFAvatavDPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 187 VILADEPTAnldeargdiVVD--------DLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:COG1134 167 ILLVDEVLA---------VGDaafqkkclARIRELRESGRTVIFVSHSMGAVRRL 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-230 |
1.26e-08 |
|
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: 53.20 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 34 VRLDVpDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG--TLAFSqcteSVRDRwRGQH 111
Cdd:cd03215 3 PVLEV-RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkPVTRR----SPRDA-IRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 112 CGFLFQDFR---LFEDLTALDNVLLPLTfrgtiaahdretaremlaargirtntragdLSRGEMQRTALVRVLMGRPAVI 188
Cdd:cd03215 77 IAYVPEDRKregLVLDLSVAENIALSSL------------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 189 LADEPTANLD-EARGDI--VVDDLmsAAQSLSASLI------LVSHSDRVL 230
Cdd:cd03215 127 ILDEPTRGVDvGAKAEIyrLIREL--ADAGKAVLLIsseldeLLGLCDRIL 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
52-225 |
1.92e-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: 54.45 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIIT--PTEGVVRWGTLAFSqcTESVRDRWRgQHCGFLFQDFRLFEDLTALD 129
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLK--ASNIRDTER-AGIVIIHQELTLVPELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLL--PLTFRGTIAAHDRETAREMLAARGIR----TNTRA-GDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARG 202
Cdd:TIGR02633 98 NIFLgnEITLPGGRMAYNAMYLRAKNLLRELQldadNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET 177
|
170 180
....*....|....*....|...
gi 2575808627 203 DIVVdDLMSAAQSLSASLILVSH 225
Cdd:TIGR02633 178 EILL-DIIRDLKAHGVACVYISH 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
52-241 |
2.37e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESvrdrwRGQHCGFLF--QDFRLFEDLTALD 129
Cdd:PRK15439 31 DFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-----KAHQLGIYLvpQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLtfrgtiAAHDRETAR--EMLAARGIRTN--TRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARgdiv 205
Cdd:PRK15439 106 NILFGL------PKRQASMQKmkQLLAALGCQLDldSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE---- 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2575808627 206 VDDLMSAAQSLSA---SLILVSHsdrvlkRLPltaEIRA 241
Cdd:PRK15439 176 TERLFSRIRELLAqgvGIVFISH------KLP---EIRQ 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
52-230 |
2.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAfsqcTESVRDRWR-GQHCGFLFQ--DFRLFEDLTAL 128
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDEENLWDiRNKAGMVFQnpDNQIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 129 DNVLLPLTFrGTIAAHDRETAREMLAARGIRTNTRAGD--LSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVV 206
Cdd:PRK13633 106 DVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190
....*....|....*....|....*....|.
gi 2575808627 207 DDLMSAAQSLSASLILVSH-------SDRVL 230
Cdd:PRK13633 185 NTIKELNKKYGITIILITHymeeaveADRII 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
57-233 |
4.06e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 57 QGAMLGIRGPSGAGKTSFLKCLSGIiTPTEGVVRW-GTLAF-SQCTESVR---DRWRGQhCGFLFQDFRLFEdLTALDNV 131
Cdd:PRK14258 32 QSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVeGRVEFfNQNIYERRvnlNRLRRQ-VSMVHPKPNLFP-MSVYDNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRG-----------TIAAHDRETAREMLAargiRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEA 200
Cdd:PRK14258 109 AYGVKIVGwrpkleiddivESALKDADLWDEIKH----KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190
....*....|....*....|....*....|....
gi 2575808627 201 rGDIVVDDLMSAAQSLSA-SLILVSHSDRVLKRL 233
Cdd:PRK14258 185 -ASMKVESLIQSLRLRSElTMVIVSHNLHQVSRL 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
41-198 |
4.35e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 41 GTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrW--GTLAFSQCTESVRDRwrgqhCGFLFQD 118
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WldGEHIQHYASKEVARR-----IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVL------LPLTFR------GTIAAHDRETAREMLAARGIRTntragdLSRGEMQRTALVRVLMGRPA 186
Cdd:PRK10253 90 ATTPGDITVQELVArgryphQPLFTRwrkedeEAVTKAMQATGITHLADQSVDT------LSGGQRQRAWIAMVLAQETA 163
|
170
....*....|..
gi 2575808627 187 VILADEPTANLD 198
Cdd:PRK10253 164 IMLLDEPTTWLD 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
52-232 |
5.30e-08 |
|
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: 51.70 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAF-SQC----TESVRD-----------RWRG--QHC 112
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpGSIAYvSQEpwiqNGTIREnilfgkpfdeeRYEKviKAC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 113 GfLFQDFRLFE--DLTaldnvllpltfrgtiaahdretareMLAARGIrtntragDLSRGEMQRTALVRVLMGRPAVILA 190
Cdd:cd03250 105 A-LEPDLEILPdgDLT-------------------------EIGEKGI-------NLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2575808627 191 DEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKR 232
Cdd:cd03250 152 DDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-250 |
5.51e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 23 DPQPFDLSLETVRL-DVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGvvrwgTLAFSQCTE 101
Cdd:PRK13536 31 ASIPGSMSTVAIDLaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-----KITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 102 SVRDRWRGQHCGFLFQDFRLFEDLTALDNVLLPLTFRGtIAAHDRETAREML---AARGIRTNTRAGDLSRGEMQRTALV 178
Cdd:PRK13536 106 PARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFG-MSTREIEAVIPSLlefARLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 179 RVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAqSLSASLILVSH----SDRVLKRLPLtaeIRAGRFIT---PDEL 250
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHfmeeAERLCDRLCV---LEAGRKIAegrPHAL 259
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
53-198 |
6.18e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLP---QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVV----RWGTlafsqctesVRDRWRGQHcgflFQDFrlFEDL 125
Cdd:cd03236 18 HRLPvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDE---------ILDEFRGSE----LQNY--FTKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALD--------NV-LLPLTFRGTI-----AAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVIL 189
Cdd:cd03236 83 LEGDvkvivkpqYVdLIPKAVKGKVgellkKKDERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
....*....
gi 2575808627 190 ADEPTANLD 198
Cdd:cd03236 163 FDEPSSYLD 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
45-232 |
8.46e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.00 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 45 RTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDRWRGQhCGFLFQDfrlfed 124
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQD------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 ltALDNVLLPLTFRGTIA-----------AHDRETAREMLAARGIR---TNTRAGDLSRGEMQRTALVRVLMGRPAVILA 190
Cdd:PRK10419 98 --SISAVNPRKTVREIIReplrhllsldkAERLARASEMLRAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2575808627 191 DEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKR 232
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVER 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
52-201 |
1.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLP-------QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-TLAF-------------SQCTESVRDRWRGQ 110
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYkpqyikpdydgtvEDLLRSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 111 hcgFLFQDfrLFEDLtALDNVLlpltfrgtiaahDREtaremlaargirtntrAGDLSRGEMQRTALVRVLmGRPAVI-L 189
Cdd:PRK13409 432 ---YYKSE--IIKPL-QLERLL------------DKN----------------VKDLSGGELQRVAIAACL-SRDADLyL 476
|
170
....*....|...
gi 2575808627 190 ADEPTANLD-EAR 201
Cdd:PRK13409 477 LDEPSAHLDvEQR 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
53-198 |
1.47e-07 |
|
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: 51.71 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLP---QGAMLGIRGPSGAGKTSFLKCLSGIITP----TEGVVRWgtlafsqctESVRDRWRGQhcgfLFQDFrlFEDL 125
Cdd:COG1245 91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPnlgdYDEEPSW---------DEVLKRFRGT----ELQDY--FKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 tALDNV----------LLPLTFRGTI-----AAHDRETAREMLAARGIRT--NTRAGDLSRGEMQRTALVRVLMgRPA-V 187
Cdd:COG1245 156 -ANGEIkvahkpqyvdLIPKVFKGTVrelleKVDERGKLDELAEKLGLENilDRDISELSGGELQRVAIAAALL-RDAdF 233
|
170
....*....|.
gi 2575808627 188 ILADEPTANLD 198
Cdd:COG1245 234 YFFDEPSSYLD 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
53-226 |
2.01e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRD-RWRgqhCGFLFQ--DFRLFEDLTALD 129
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDiRKK---VGLVFQypEYQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 130 NVLLPLTfRGTIAAHDRETAREMLAARGIRTNTRAG----DLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARgdi 204
Cdd:PRK13637 105 IAFGPIN-LGLSEEEIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGR--- 180
|
170 180
....*....|....*....|....*.
gi 2575808627 205 vvDDLMSAAQSL----SASLILVSHS 226
Cdd:PRK13637 181 --DEILNKIKELhkeyNMTIILVSHS 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
58-226 |
2.82e-07 |
|
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: 51.17 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPTEGVvrwGTLAFSQCTESVRDRwrGQHCGFLFQDFRLFEDLTALDNVLLPLTF 137
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGD---ATVAGKSILTNISDV--HQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 138 RGTIAAHDRETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQS 215
Cdd:TIGR01257 2040 RGVPAEEIEKVANWSIQSLGLSlyADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
170
....*....|.
gi 2575808627 216 LSAsLILVSHS 226
Cdd:TIGR01257 2120 GRA-VVLTSHS 2129
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-198 |
2.85e-07 |
|
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: 50.84 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKT----SFLKCLSGIITPTEGVVRWGTLAFSQCTESVR 104
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 105 DRWRGQHCGFLFQdfrlfEDLTALdNVLL--------PLTF-RGTIAAHDRETAREMLAARGIRT-NTRAGD----LSRG 170
Cdd:COG4172 87 RRIRGNRIAMIFQ-----EPMTSL-NPLHtigkqiaeVLRLhRGLSGAAARARALELLERVGIPDpERRLDAyphqLSGG 160
|
170 180
....*....|....*....|....*...
gi 2575808627 171 EMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
57-197 |
3.26e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 57 QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESvrdRWRGQHCGFLFQDFRLFEDLTALDNVLLPLT 136
Cdd:PRK11614 30 QGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA---KIMREAVAIVPEGRRVFSRMTVEENLAMGGF 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 137 FRGTIAAHDR-ETAREMLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:PRK11614 107 FAERDQFQERiKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
52-198 |
3.58e-07 |
|
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: 50.45 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItPTEGVVRWGTLAFSQCTESVRDRWRgQHCGFLFQD-F-----RlfedL 125
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQDpFgslspR----M 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575808627 126 TALDNVLLPLT--FRGTIAAHDRETAREMLAARGIRTNTRA---GDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:COG4172 380 TVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
52-230 |
4.77e-07 |
|
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: 50.17 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLP-------QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWG-TLAF------SQCTESVRDRWRgQHCGFLFQ 117
Cdd:COG1245 353 GFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYkpqyisPDYDGTVEEFLR-SANTDDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRLFEDLT---ALDNVLlpltfrgtiaahDREtaremlaargirtntrAGDLSRGEMQRTALVRVLmGRPAVI-LADEP 193
Cdd:COG1245 432 SSYYKTEIIkplGLEKLL------------DKN----------------VKDLSGGELQRVAIAACL-SRDADLyLLDEP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 194 TANLDeargdivVDDLMSAAQSLS-------ASLILVSH--------SDRVL 230
Cdd:COG1245 483 SAHLD-------VEQRLAVAKAIRrfaenrgKTAMVVDHdiylidyiSDRLM 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
52-207 |
4.89e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItPT---EGVVRWG--TLAFSqcteSVRDRwrgQHCG--FLFQDFRLFED 124
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEgeELQAS----NIRDT---ERAGiaIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 125 LTALDNVLL--PLTfRGTIAAHDRETAR--EMLAARGIRTN--TRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK13549 97 LSVLENIFLgnEIT-PGGIMDYDAMYLRaqKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
....*....
gi 2575808627 199 EARGDIVVD 207
Cdd:PRK13549 176 ESETAVLLD 184
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-232 |
5.53e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 24 PQPFdLSLETVRLdvpdGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwgTLAfsqctesv 103
Cdd:PRK10636 309 PNPL-LKMEKVSA----GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLA-------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 104 rdrwRGQHCGFLFQdfRLFEDLTALDNvllPLTFRGTIAAHDRETA-REMLAA---RGIRTNTRAGDLSRGEMQRTALVR 179
Cdd:PRK10636 373 ----KGIKLGYFAQ--HQLEFLRADES---PLQHLARLAPQELEQKlRDYLGGfgfQGDKVTEETRRFSGGEKARLVLAL 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2575808627 180 VLMGRPAVILADEPTANLD-EARgdivvDDLMSAAQSLSASLILVSHsDRVLKR 232
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDlDMR-----QALTEALIDFEGALVVVSH-DRHLLR 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
53-230 |
6.20e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIItptEGvvRW-GT-------LAFSQCTESVR--------DRWRgqhcgflf 116
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTELVQCLFGAY---PG--RWeGEifidgkpVKIRNPQQAIAqgiamvpeDRKR-------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 117 qdFRLFEDLTALDNVLLP----LTFRGTI-AAHDRETAREMLAARGIRTNT---RAGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:PRK13549 350 --DGIVPVMGVGKNITLAaldrFTGGSRIdDAAELKTILESIQRLKVKTASpelAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 189 LADEPTANLD-EARGDIVvdDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:PRK13549 428 ILDEPTRGIDvGAKYEIY--KLINQLVQQGVAIIVISSelpevlglSDRVL 476
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
58-194 |
6.36e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 58 GAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW--GTLAFSQCTESvrdrwrgQHCGF--LFQDFRLFEDLTALDNVLL 133
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSS-------QEAGIgiIHQELNLIPQLTIAENIFL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 134 PLTFRGTIAAHD----RETAREMLAARGIR--TNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPT 194
Cdd:PRK10762 103 GREFVNRFGRIDwkkmYAEADKLLARLNLRfsSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
51-231 |
7.39e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 51 FDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVR-----------WGTLAFSQCTESVRD--RWRgQHCGFLFQ 117
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknNHELITNPYSKKIKNfkELR-RRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 --DFRLFEDLTALDNVLLPLTFrGTIAAHDRETAREMLAARGIRT---NTRAGDLSRGEMQRTALVRVLMGRPAVILADE 192
Cdd:PRK13631 124 fpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDsylERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2575808627 193 PTANLDEArGDIVVDDLMSAAQSLSASLILVSHS-DRVLK 231
Cdd:PRK13631 203 PTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTmEHVLE 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
48-230 |
7.86e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 48 FSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCteSVRDRWRG---------QHCGfLFQD 118
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL--STAQRLARglvylpedrQSSG-LYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 FRLFEDLTALDNVLLPLTFRGtiaAHDRETAREMLAARGIRTN---TRAGDLSRGEMQRTALVRVLMGRPAVILADEPTA 195
Cdd:PRK15439 356 APLAWNVCALTHNRRGFWIKP---ARENAVLERYRRALNIKFNhaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2575808627 196 NLD-EARGDI--VVDDLmsAAQSLSASLI------LVSHSDRVL 230
Cdd:PRK15439 433 GVDvSARNDIyqLIRSI--AAQNVAVLFIssdleeIEQMADRVL 474
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
52-198 |
1.19e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFsqctesvrdrwRGQ--------------HCGFLFQ 117
Cdd:COG1117 31 NLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILL-----------DGEdiydpdvdvvelrrRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 118 DFRLFEdLTALDNVLLPLTFRGTiaaHDR----ETAREMLAARGI------RTNTRAGDLSRGEMQRTALVRVLMGRPAV 187
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGI---KSKseldEIVEESLRKAALwdevkdRLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 2575808627 188 ILADEPTANLD 198
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
53-238 |
1.25e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKT-SFLKCLSGIITPteGVVRWGTLAFSQ-----CTESVRDRWRGQHCGFLFQD-------- 118
Cdd:PRK11022 28 YSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGqdlqrISEKERRNLVGAEVAMIFQDpmtslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 119 ----FRLFEDLTaldnvllplTFRGTIAAHDRETAREMLAARGI-----RTNTRAGDLSRGEMQRTALVRVLMGRPAVIL 189
Cdd:PRK11022 106 ytvgFQIMEAIK---------VHQGGNKKTRRQRAIDLLNQVGIpdpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2575808627 190 ADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSdrvlkrLPLTAE 238
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD------LALVAE 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
52-226 |
1.44e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSQctesvRDRWrgqhcgflFQDFRLFEDLTaLDN 130
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkGSVAYVP-----QQAW--------IQNDSLRENIL-FGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAArGIRTNT--RAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDD 208
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLEILPS-GDRTEIgeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170
....*....|....*....
gi 2575808627 209 LMSAAQSLS-ASLILVSHS 226
Cdd:TIGR00957 803 VIGPEGVLKnKTRILVTHG 821
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
53-198 |
1.56e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQ-------------CTESVRDRwrgqhcGFlFQDF 119
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldavkkgmayITESRRDN------GF-FPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 120 RLFEDLtALDNVLLPLTFRGTIAAHDR-------ETAREMLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADE 192
Cdd:PRK09700 357 SIAQNM-AISRSLKDGGYKGAMGLFHEvdeqrtaENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
....*.
gi 2575808627 193 PTANLD 198
Cdd:PRK09700 436 PTRGID 441
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
53-250 |
1.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.17 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSqcTESVRDRWRgqHCGFLFQD-FRLFEDLTALDNV 131
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRR--KIGMVFQNpDNQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 LLPLTFRGTIAAHDRETARE-MLAARGIRTNTR-AGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARGDI---- 204
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEaLLAVNMLDFKTRePARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDpTGRQEImrvi 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 205 --VVDDLMSAAQSLSASLILVSHSDRVLKrlpltaeIRAGRFI---TPDEL 250
Cdd:PRK13642 184 heIKEKYQLTVLSITHDLDEAASSDRILV-------MKAGEIIkeaAPSEL 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
52-233 |
2.21e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTsfLKCLS--GIITP----TEGVVRWGTLAFSQCTesvrdrWRGQHCGFLFQDFRlfedl 125
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGRVLLDGKPVAPCA------LRGRKIATIMQNPR----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVLlpltfrgTIAAHDRETAR------------EMLAARGIRTNTR-----AGDLSRGEMQRTALVRVLMGRPAVI 188
Cdd:PRK10418 90 SAFNPLH-------TMHTHARETCLalgkpaddatltAALEAVGLENAARvlklyPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2575808627 189 LADEPTANLD---EARgdiVVDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:PRK10418 163 IADEPTTDLDvvaQAR---ILDLLESIVQKRALGMLLVTHDMGVVARL 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
52-198 |
2.73e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRDrwrgqhCGFLFQDFRLFEDLTALDNV 131
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD------IAMVFQNYALYPHMSVRENM 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 132 LLPLTFRGT----IAAHDRETAR-----EMLAARgirtnTRAgdLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK11650 98 AYGLKIRGMpkaeIEERVAEAARilelePLLDRK-----PRE--LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-214 |
2.76e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIItptEGVVRWGTLAFS--QCTESVRDR 106
Cdd:PLN03211 65 LGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI---QGNNFTGTILANnrKPTKQILKR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 107 wrgqhCGFLFQDFRLFEDLTALDNVLLPLTFR--GTIAAHDRETARE-MLAARGIRT--NTRAGD-----LSRGEMQRTA 176
Cdd:PLN03211 142 -----TGFVTQDDILYPHLTVRETLVFCSLLRlpKSLTKQEKILVAEsVISELGLTKceNTIIGNsfirgISGGERKRVS 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 2575808627 177 LVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQ 214
Cdd:PLN03211 217 IAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ 254
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-200 |
3.18e-06 |
|
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: 46.49 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDGTGVRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVrwGTLAFsqctesvrdrwr 108
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE--GDIHY------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 gqhCGFLFQDFRLFEDLTAL-----DNVLLPLTFRGTIaahdrETAREMLAARGIRTntragdLSRGEMQRTALVRVLMG 183
Cdd:cd03233 70 ---NGIPYKEFAEKYPGEIIyvseeDVHFPTLTVRETL-----DFALRCKGNEFVRG------ISGGERKRVSIAEALVS 135
|
170
....*....|....*..
gi 2575808627 184 RPAVILADEPTANLDEA 200
Cdd:cd03233 136 RASVLCWDNSTRGLDSS 152
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
52-223 |
3.69e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG--------VVRwgtLAFSQCTESVRDRWRGQHCGFLFQDfrlfE 123
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITR---LSFEQLQKLVSDEWQRNNTDMLSPG----E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 124 DLTALdnvllplTFRGTIAAHDRETAR-EMLAAR-GIRT--NTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD- 198
Cdd:PRK10938 96 DDTGR-------TTAEIIQDEVKDPARcEQLAQQfGITAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDv 168
|
170 180
....*....|....*....|....*
gi 2575808627 199 EARGDIVvdDLMSAAQSLSASLILV 223
Cdd:PRK10938 169 ASRQQLA--ELLASLHQSGITLVLV 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-198 |
3.93e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.03 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 34 VRLDVPDG--TGVRTIfscfDFKLPQGAMLGIRGPSGAGK--TSF----LKCLSGIITpteGVVRWGTLAFSQCTESVRD 105
Cdd:PRK09473 20 VTFSTPDGdvTAVNDL----NFSLRAGETLGIVGESGSGKsqTAFalmgLLAANGRIG---GSATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 106 RWRGQHCGFLFQD--------FRLFEDLTaldNVLLplTFRGTIAAHDRETAREMLAARGI-----RTNTRAGDLSRGEM 172
Cdd:PRK09473 93 KLRAEQISMIFQDpmtslnpyMRVGEQLM---EVLM--LHKGMSKAEAFEESVRMLDAVKMpearkRMKMYPHEFSGGMR 167
|
170 180
....*....|....*....|....*.
gi 2575808627 173 QRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-228 |
5.90e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 31 LETVRLDVPDgtgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGT---LA-FSQCTE----- 101
Cdd:PRK11147 322 MENVNYQIDG----KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTkleVAyFDQHRAeldpe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 102 -SVRDRW-----------RGQHC-GFLfQDFrLFEDLTAldnvllpltfrgtiaahdretaremlaargiRTNTRAgdLS 168
Cdd:PRK11147 398 kTVMDNLaegkqevmvngRPRHVlGYL-QDF-LFHPKRA-------------------------------MTPVKA--LS 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 169 RGEMQRTALVRVLMgRPA--VILaDEPTANLD----EargdiVVDDLMSAAQslsASLILVSHsDR 228
Cdd:PRK11147 443 GGERNRLLLARLFL-KPSnlLIL-DEPTNDLDvetlE-----LLEELLDSYQ---GTVLLVSH-DR 497
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
174-233 |
6.15e-06 |
|
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: 45.68 E-value: 6.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 174 RTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSAS-LILVSHSDRVLKRL 233
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNFqLIVITHDEELVDAA 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
146-243 |
8.24e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 146 RETAR-EMLAAR---GIR-TNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSL 216
Cdd:PRK15134 127 REAARgEILNCLdrvGIRqAAKRLTDyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL 206
|
90 100
....*....|....*....|....*...
gi 2575808627 217 SASLILVSHSDRVLKRLPLT-AEIRAGR 243
Cdd:PRK15134 207 NMGLLFITHNLSIVRKLADRvAVMQNGR 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
53-230 |
9.93e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPT-EGVVRWG--TLAFSQCTESVR--------DRWRGQhcgfLFQDFRL 121
Cdd:TIGR02633 281 FSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNPAQAIRagiamvpeDRKRHG----IVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 122 FEDLTAldNVLLPLTFRGTI-AAHDRETAREMLAARGIRTNT---RAGDLSRGEMQRTALVRVLMGRPAVILADEPTANL 197
Cdd:TIGR02633 357 GKNITL--SVLKSFCFKMRIdAAAELQIIGSAIQRLKVKTASpflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2575808627 198 D-EARGDIVvdDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:TIGR02633 435 DvGAKYEIY--KLINQLAQEGVAIIVVSSelaevlglSDRVL 474
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-231 |
1.35e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 29 LSLETVRLDVPDgtgvRTIFS-CFDFkLPQgAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESvrdrw 107
Cdd:PRK13541 2 LSLHQLQFNIEQ----KNLFDlSITF-LPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 108 rgqHCGFLFQDFRLFEDLTALDNVLLPLTFRGTI----AAHDRETAREMLaargirtNTRAGDLSRGEMQRTALVRVLMG 183
Cdd:PRK13541 71 ---YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAetlyAAIHYFKLHDLL-------DEKCYSLSSGMQKIVAIARLIAC 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2575808627 184 RPAVILADEPTANLDEARGDIVVDDLMSAAQSlSASLILVSHSDRVLK 231
Cdd:PRK13541 141 QSDLWLLDEVETNLSKENRDLLNNLIVMKANS-GGIVLLSSHLESSIK 187
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
53-230 |
1.36e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEG-VVRWGTLAFSQCTESVRdrwrgQHCGFLFQD-FRLFEDLTALDN 130
Cdd:PRK13650 28 FHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqIIIDGDLLTEENVWDIR-----HKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 131 VLLPLTFRGTIAAHDRETAREMLAARGI-----RTNTRagdLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EARGDI 204
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMqdfkeREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpEGRLEL 179
|
170 180 190
....*....|....*....|....*....|..
gi 2575808627 205 ------VVDDLMSAAQSLSASLILVSHSDRVL 230
Cdd:PRK13650 180 iktikgIRDDYQMTVISITHDLDEVALSDRVL 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
53-230 |
1.38e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTL----------AFSQCTESVRDRWRGQHCGFLFQdfrlf 122
Cdd:PRK10261 37 FSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGADMAMIFQ----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 123 EDLTALDNVLlplTFRGTIAAHDR-----ETAREMLAARGIRTNTRAGD-----------LSRGEMQRTALVRVLMGRPA 186
Cdd:PRK10261 112 EPMTSLNPVF---TVGEQIAESIRlhqgaSREEAMVEAKRMLDQVRIPEaqtilsryphqLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 187 VILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH--------SDRVL 230
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHdmgvvaeiADRVL 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
53-198 |
2.14e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSQCTESVRDRwrgqhcgflfqdfrlfedlTALDNV 131
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHsGRISFSPQTSWIMPG-------------------TIKDNI 507
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 132 LLPLT-----FRGTIAAHDREtarEMLAARGIRTNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:TIGR01271 508 IFGLSydeyrYTSVIKACQLE---EDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
52-232 |
6.91e-05 |
|
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: 42.31 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKclsgiitptegvvrwGTLAFSQCTESVRDRWRGQHCGFLFQDfrlfeDLTALDNV 131
Cdd:cd03238 15 DVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKARLISFLPKFSRNKLIFID-----QLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 132 ---LLPLtfrgtiaahdretaremlaargirtNTRAGDLSRGEMQRTALVRVLMGRP--AVILADEPTANLDEARGDIVV 206
Cdd:cd03238 75 glgYLTL-------------------------GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....*.
gi 2575808627 207 DDLMSAAQsLSASLILVSHSDRVLKR 232
Cdd:cd03238 130 EVIKGLID-LGNTVILIEHNLDVLSS 154
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
52-231 |
9.88e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.69 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESVRD--RWRgQHCGFLFQ--DFRLFEDLTA 127
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkRLR-KEIGLVFQfpEYQLFQETIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 128 LDNVLLPLTfrgtIAAHDRETAR---EMLAARGI---RTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDeAR 201
Cdd:PRK13645 110 KDIAFGPVN----LGENKQEAYKkvpELLKLVQLpedYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD-PK 184
|
170 180 190
....*....|....*....|....*....|....*
gi 2575808627 202 GDivvDDLMSAAQSLSAS----LILVSHS-DRVLK 231
Cdd:PRK13645 185 GE---EDFINLFERLNKEykkrIIMVTHNmDQVLR 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
53-233 |
1.56e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVV-----RWGTLAFSQCTESVRDrwrgqhCGFLFQD--FRLFEDL 125
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTLSPGKLQALRRD------IQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 126 TALDNVLLPLTFRGTIaahDRETAREMLAARGIRTNTRA-------GDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK10261 419 TVGDSIMEPLRVHGLL---PGKAAAARVAWLLERVGLLPehawrypHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 2575808627 199 -EARGDIvVDDLMSAAQSLSASLILVSHSDRVLKRL 233
Cdd:PRK10261 496 vSIRGQI-INLLLDLQRDFGIAYLFISHDMAVVERI 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
65-198 |
1.65e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.40 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTESV-RdrwrgQHCGFLFQDFRLFEDlTALDNVLLPLTFRGTIAA 143
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlR-----QGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVW 447
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575808627 144 HDRETAREMLAARGIRT--NTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK10790 448 QALETVQLAELARSLPDglYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
52-198 |
1.71e-04 |
|
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: 42.15 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRW-GTLAFSqctesvrdrwrgqhcgflfQDFRLFEDLTALDN 130
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHsGRISFS-------------------SQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 131 VLLPLT-----FRGTIAAHDREtarEMLAARGIRTNTRAGD----LSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03291 118 IIFGVSydeyrYKSVVKACQLE---EDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
33-225 |
2.30e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.81 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 33 TVRLDVPDGTgVRTIfSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGV----VRWGTLAFSQCTESVRDRWR 108
Cdd:COG4170 10 TIEIDTPQGR-VKAV-DRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVtadrFRWNGIDLLKLSPRERRKII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 109 GQHCGFLFQDFRLFEDLTA-----LDNVLLPLTFRGTI---AAHDRETAREMLAARGIRT-----NTRAGDLSRGEMQRT 175
Cdd:COG4170 88 GREIAMIFQEPSSCLDPSAkigdqLIEAIPSWTFKGKWwqrFKWRKKRAIELLHRVGIKDhkdimNSYPHELTEGECQKV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2575808627 176 ALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSH 225
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
140-233 |
2.89e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 140 TIAAHDRETA-REMLAARGIRTNTR---AGDLSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQS 215
Cdd:PRK15134 395 TLSAAQREQQvIAVMEEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
90
....*....|....*...
gi 2575808627 216 LSASLILVSHSDRVLKRL 233
Cdd:PRK15134 475 HQLAYLFISHDLHVVRAL 492
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
52-198 |
2.99e-04 |
|
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: 40.63 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKlpQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWgtlafsqctESVRDRWRGQHCgflfqdfrlfedltaldnv 131
Cdd:cd03222 21 VVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---------DGITPVYKPQYI------------------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575808627 132 llpltfrgtiaahdretaremlaargirtntragDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
53-118 |
3.95e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 3.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575808627 53 FKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQctesVR-DRWRGQ-----HCGFLFQD 118
Cdd:PRK10789 336 FTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK----LQlDSWRSRlavvsQTPFLFSD 403
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-240 |
4.42e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 57 QGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlafsqctesvrdrwrgqhcgflfqdfrlfedltaldnvllplt 136
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 137 frgtIAAHDRETAREMLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-----EARGDIVVDDLMS 211
Cdd:smart00382 35 ----YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLLL 110
|
170 180
....*....|....*....|....*....
gi 2575808627 212 AAQSLSASLILVSHSDRVLKRLPLTAEIR 240
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
65-199 |
4.75e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 65 GPSGAGKTSFLKCLSGIITPTEGVVRW--GTLAFSQCTESVRDRWRGQHcgflfQDFRLFEDLTALDNVLL---PLtfRG 139
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIYQKDSGSILFqgKEIDFKSSKEALENGISMVH-----QELNLVLQRSVMDNMWLgryPT--KG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2575808627 140 TIAAHD---RETaREMLAARGIRTNTRA--GDLSRGEMQRTALVRVLMGRPAVILADEPTANLDE 199
Cdd:PRK10982 104 MFVDQDkmyRDT-KAIFDELDIDIDPRAkvATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
151-228 |
6.00e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 6.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575808627 151 EMLAARGIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD-EArgdivVDDLMSAAQSLSASLILVSHsDR 228
Cdd:PRK11147 141 EVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDiET-----IEWLEGFLKTFQGSIIFISH-DR 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
167-232 |
6.09e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 6.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 167 LSRGEMQRTALVRVLMGRPAVILADEPTANLDEARGDIVVDDLMSAAQSLSASLILVSHSDRVLKR 232
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
54-198 |
1.48e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.99 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 54 KLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAF------SQCTESVRDRWRgqhCGFLFQDFRLFEDlTA 127
Cdd:PRK14243 32 DIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFhgknlyAPDVDPVEVRRR---IGMVFQKPNPFPK-SI 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575808627 128 LDNVLLPLTFRGTIAAHDRETAREMLAAR-----GIRTNTRAGDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK14243 108 YDNIAYGARINGYKGDMDELVERSLRQAAlwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-210 |
1.57e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 48 FSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTE--GVVRWGTLAFSQ-----CTESVRDRWRgqhCGFLFQDFR 120
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGSVAYVPqvswiFNATVRENIL---FGSDFESER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 121 LFE--DLTALDNVLlpltfrGTIAAHDRETAREmlaaRGIrtntragDLSRGEMQRTALVRVLMGRPAVILADEPTANLD 198
Cdd:PLN03232 710 YWRaiDVTALQHDL------DLLPGRDLTEIGE----RGV-------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170
....*....|..
gi 2575808627 199 EARGDIVVDDLM 210
Cdd:PLN03232 773 AHVAHQVFDSCM 784
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
52-198 |
7.31e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.41 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 52 DFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRwgtlAFSQCTE----SVRDRwrgqhCGFLFQDFRLFEDLTA 127
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW----LFGQPVDagdiATRRR-----VGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575808627 128 LDNVLL--PLtFRgtIAAHDREtAR--EMLAARGIRT--NTRAGDLSRGEMQRTAL-VRVLMgRPAVILADEPTANLD 198
Cdd:NF033858 357 RQNLELhaRL-FH--LPAAEIA-ARvaEMLERFDLADvaDALPDSLPLGIRQRLSLaVAVIH-KPELLILDEPTSGVD 429
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-198 |
9.08e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 37.11 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 28 DLSLETVRLDVPDGTgvRTIFSCFDFKLPQGAMLGIRGPSGAGKTSFLKCLSGIITPTEGVVRWGTLAFSQCTES-VRdr 106
Cdd:PRK11160 338 SLTLNNVSFTYPDQP--QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAaLR-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575808627 107 wrgQHCGFLFQDFRLFEDlTALDNVLLpltfrGTIAAHDrETAREMLAARGIRT--------NTRAGD----LSRGEMQR 174
Cdd:PRK11160 414 ---QAISVVSQRVHLFSA-TLRDNLLL-----AAPNASD-EALIEVLQQVGLEKlleddkglNAWLGEggrqLSGGEQRR 483
|
170 180
....*....|....*....|....
gi 2575808627 175 TALVRVLMGRPAVILADEPTANLD 198
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLD 507
|
|
| |
