|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-220 |
8.38e-120 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 340.10 E-value: 8.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEVS-----PDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAgvsrkERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVRSVE 220
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-216 |
3.84e-108 |
|
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: 310.19 E-value: 3.84e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERreraeELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-213 |
4.29e-83 |
|
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: 247.35 E-value: 4.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENV----ELATEvsPDALDP-VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVmlplELAGR--RDARARaRALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHIND 213
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRA 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-220 |
2.43e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 237.26 E-value: 2.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGettITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEV----SPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVtgksRKEIRRRVrEVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALapIAD---RVIHINDAKVRSVE 220
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLEL--VDRmpkRVLELEDGRLVRDE 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-209 |
9.57e-73 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 221.02 E-value: 9.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfSDKQLTAYR 83
Cdd:COG1126 2 IEIENLHKSF--GDLEVL--KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELA---------TEVSPDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:COG1126 77 R-KVGMVFQQFNLFPHLTVLENVTLApikvkkmskAEAEERAM---ELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALA-PIADRVI 209
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFArEVADRVV 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
7.09e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.58 E-value: 7.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqlt 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayRRTDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:COG1116 78 --PGPDRGVVFQEPALLPWLTVLDNVALGLElrgVPKAERRERarELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNS--ALApIADRVI 209
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF-LADRVV 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-197 |
7.83e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 222.26 E-value: 7.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEiagVPKAEIRKrvAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH 197
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-216 |
4.14e-71 |
|
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: 216.68 E-value: 4.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEV--SPDALDP---VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIagVPKAEIEervLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-216 |
1.25e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 213.38 E-value: 1.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG3638 3 LELRNLSKRYP-GGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENV----------------ELATEVSPDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRV 147
Cdd:COG3638 80 R-RIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsllgLFPPEDRERAL---EALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARrYADRIIGLRDGRV 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-215 |
2.69e-69 |
|
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: 211.72 E-value: 2.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGettITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:TIGR02673 2 IEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:TIGR02673 79 RR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIqrrvgAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASrQHGNTVLIITHNSALAP-IADRVIHINDAK 215
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDrVAHRVIILDDGR 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-216 |
3.57e-67 |
|
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: 206.23 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfSDKQLTAYR 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELA---------TEVSPDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLApikvkgmskAEAEERAL---ELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.29e-66 |
|
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: 204.68 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYR 83
Cdd:cd03259 1 LELKGLSKTY--GSVRAL--DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03259 72 R-NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIrarvrELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHdqEEALA-LADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
2.26e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 208.80 E-value: 2.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLT 80
Cdd:COG3842 3 MPALELENVSKRY--GDVTAL--DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRtDVGFVFQFYNLVPNLTAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVS 148
Cdd:COG3842 74 PEKR-NVGMVFQDYALFPHLTVAENVafglrmrgvpkaEIRARVA-------ELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGKQV---LKLLQnasRQHGNTVLIITHNS--ALApIADRVIHINDAKVRSV---- 219
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMreeLRRLQ---RELGITFIYVTHDQeeALA-LADRIAVMNDGRIEQVgtpe 221
|
....*...
gi 488224859 220 ELNDHPSS 227
Cdd:COG3842 222 EIYERPAT 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
4.01e-66 |
|
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: 203.47 E-value: 4.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqltayR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEV----SPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELqgvpKAEARERAeELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN--SALApIADRVI 209
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDidEAVF-LADRVV 203
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-211 |
1.16e-65 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 202.08 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRT 85
Cdd:TIGR03608 1 LKNISKKFG----DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 86 DVGFVFQFYNLVPNLTAKENVELATEVSPDALDP-----VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLL 160
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEkrekkKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488224859 161 LCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALAPIADRVIHI 211
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-216 |
7.12e-65 |
|
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: 201.26 E-value: 7.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKMGETtitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRR 84
Cdd:cd03256 2 EVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 tDVGFVFQFYNLVPNLTAKENV------------ELATEVSP-DALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIAR 151
Cdd:cd03256 79 -QIGMIFQQFNLIERLSVLENVlsgrlgrrstwrSLFGLFPKeEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-216 |
6.29e-64 |
|
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: 198.02 E-value: 6.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGettITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVELATEVS----PDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTgvppREIRKRVpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLqNASRQHGNTVLIITHNSAL-APIADRVIHINDAKV 216
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-209 |
1.48e-63 |
|
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: 197.34 E-value: 1.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtAYR 83
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQ--FYNLVPNLTAKENVE----LATEVSPDALDPV---EVLRQVGL-AHRLNNFPSQLSGGEQQRVSIARAL 153
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAeplrIHGKLSKKEARKEavlLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVA 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-216 |
1.53e-63 |
|
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: 197.89 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG1127 6 IEVRNLTKSF--GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELA----TEVSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:COG1127 82 R-RIGMLFQGGALFDSLTVFENVAFPlrehTDLSEAEIRELvlEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHdlDSAFA-IADRVAVLADGKI 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-220 |
1.87e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 198.49 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:PRK11153 82 R-QIGMIFQHFNLLSSRTVFDNVALPLElagTPKAEIKArvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVrsVE 220
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKrICDRVAVIDAGRL--VE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-209 |
5.18e-62 |
|
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: 201.67 E-value: 5.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKM-GETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAY 82
Cdd:COG1123 261 LEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 RRtDVGFVFQ--FYNLVPNLTAKENVE----LATEVSPDALDP--VEVLRQVGL-AHRLNNFPSQLSGGEQQRVSIARAL 153
Cdd:COG1123 341 RR-RVQMVFQdpYSSLNPRMTVGDIIAeplrLHGLLSRAERRErvAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVI 209
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRyIADRVA 476
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
4.05e-60 |
|
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: 187.01 E-value: 4.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELAtevspdaldpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG-----------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488224859 164 EPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAK 215
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-224 |
4.41e-60 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 189.05 E-value: 4.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:TIGR02315 2 LEVENLSKVYPNGKQAL---KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENV---ELATE----------VSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIA 150
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVlhgRLGYKptwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKV----RSVELNDH 224
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIvfdgAPSELDDE 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-227 |
3.95e-59 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 189.97 E-value: 3.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqFSDkqLTAYR 83
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTN--LPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEVSPdaLDPVEVLRQV----------GLAHRlnnFPSQLSGGEQQRVSIARAL 153
Cdd:COG1118 75 R-RVGFVFQHYALFPHMTVAENIAFGLRVRP--PSKAEIRARVeellelvqleGLADR---YPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN--SALaPIADRVIHINDAKVRSV----ELNDHPSS 227
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeEAL-ELADRVVVMNQGRIEQVgtpdEVYDRPAT 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-218 |
6.51e-59 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 196.48 E-value: 6.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRR 84
Cdd:PRK10535 6 ELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TDVGFVFQFYNLVPNLTAKENVEL-----ATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKL 159
Cdd:PRK10535 86 EHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 160 LLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHNSALAPIADRVIHINDAKVRS 218
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-223 |
2.27e-58 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 185.01 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltayR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFY--NLVPNLTAKENVE--LATEVSPDALD-PVEVLRQVGLAHR-LNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAepLRIHGLPDREErIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSAL-APIADRVIHINDAKVrsVELND 223
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRI--VEELT 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-216 |
1.98e-57 |
|
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: 181.93 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:cd03261 1 IELRGLTKSF--GGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVELA----TEVSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPlrehTRLSEEEIREIvlEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHdlDTAFA-IADRIAVLYDGKI 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
4.12e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 181.44 E-value: 4.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTay 82
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 rRTDVGFVFQFYNLVPNLTAKENVelatevspdALDPVEV---------------LRQVGLAHRLNNFPSQLSGGEQQRV 147
Cdd:PRK09493 76 -RQEAGMVFQQFYLFPHLTALENV---------MFGPLRVrgaskeeaekqarelLAKVGLAERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALA-PIADRVIHINDAKV----RSVELN 222
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAeKVASRLIFIDKGRIaedgDPQVLI 224
|
....*
gi 488224859 223 DHPSS 227
Cdd:PRK09493 225 KNPPS 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-209 |
7.73e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 183.33 E-value: 7.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTP---DEGQIIIDDTDIAQFSDKQLT 80
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTDVGFVFQ--FYNLVPNLTAK----ENVELATEVSPDALDP--VEVLRQVGL---AHRLNNFPSQLSGGEQQRVSI 149
Cdd:COG0444 82 KIRGREIQMIFQdpMTSLNPVMTVGdqiaEPLRIHGGLSKAEAREraIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADRVA 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-213 |
1.37e-56 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 180.01 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 11 KRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFV 90
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 91 FQFYNLVPNLTAKENVE---LATEVSPDALD--PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:PRK11629 93 YQFHHLLPDFTALENVAmplLIGKKKPAEINsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 166 TGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHIND 213
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-216 |
1.46e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.87 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdKQLTAYR 83
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEAreridELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
1.51e-56 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 183.35 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYkmGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLT 80
Cdd:COG3839 1 MASLELENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRtDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:COG3839 72 PKDR-NIAMVFQSYALYPHMTVYENIAFPLKlrkVPKAEIDRrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 156 NPKLLLCDEPTGALDFETGKQV---LKLLQnasRQHGNTVLIITHNS--ALApIADRVIHINDAKVRSV----ELNDHPS 226
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMraeIKRLH---RRLGTTTIYVTHDQveAMT-LADRIAVMNDGRIQQVgtpeELYDRPA 226
|
..
gi 488224859 227 SI 228
Cdd:COG3839 227 NL 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-227 |
3.23e-55 |
|
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: 176.38 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqltaYR 83
Cdd:cd03296 3 IEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEVSPDALDP---------VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPpeaeirakvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHPSS 227
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVgtpdEVYDHPAS 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-216 |
4.74e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 175.60 E-value: 4.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTAYR 83
Cdd:COG1122 1 IELENLSFSYPGGTPAL---DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYN--LVpNLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKN 156
Cdd:COG1122 75 R-KVGLVFQNPDdqLF-APTVEEDVAFGPEnlgLPREEIRERveEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 157 PKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-215 |
5.03e-55 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 174.96 E-value: 5.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNeyKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrR 84
Cdd:cd03225 1 ELKN--LSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TDVGFVFQFynlvP-----NLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:cd03225 75 RKVGLVFQN----PddqffGPTVEEEVAFGLEnlgLPEEEIEERveEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAK 215
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-227 |
9.05e-54 |
|
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: 172.42 E-value: 9.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYR 83
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIAR 151
Cdd:cd03300 72 R-PVNTVFQNYALFPHLTVFENIafglrlkklpkaEIKERVA-------EALDLVQLEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNS--ALApIADRVIHINDAKVRSV----ELNDHP 225
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQeeALT-MSDRIAVMNKGKIQQIgtpeEIYEEP 222
|
..
gi 488224859 226 SS 227
Cdd:cd03300 223 AN 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-227 |
1.85e-53 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 175.61 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQlt 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrrTDVGFVFQFYNLVPNLTAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVS 148
Cdd:TIGR03265 76 ----RDYGIVFQSYALFPNLTVADNIayglknrgmgraEVAERVA-------ELLDLVGLPGSERKYPGQLSGGQQQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 149 IARALAKNPKLLLCDEPTGALDF---ETGKQVLKLLQnasRQHGNTVLIITHNS--ALApIADRVIHINDAKVRSV---- 219
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDArvrEHLRTEIRQLQ---RRLGVTTIMVTHDQeeALS-MADRIVVMNHGVIEQVgtpq 220
|
....*...
gi 488224859 220 ELNDHPSS 227
Cdd:TIGR03265 221 EIYRHPAT 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-217 |
5.13e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 170.73 E-value: 5.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELAT----EVSPDALD-PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPAllrgESSRQSRNgAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-209 |
1.01e-52 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 170.61 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtAyRRtdVGFVFQFYNLVPNLTAK 103
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-A-RR--IAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELA--------TEVSPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFetG 174
Cdd:COG1120 94 ELVALGryphlglfGRPSAEDREAVeEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL--A 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 175 KQ--VLKLLQNASRQHGNTVLIITH--NSALApIADRVI 209
Cdd:COG1120 172 HQleVLELLRRLARERGRTVVMVLHdlNLAAR-YADRLV 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-216 |
1.67e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 169.17 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 12 RYKMGETTITAnddiSFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYRRTdVGFVF 91
Cdd:COG3840 8 TYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----ALPPAERP-VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 92 QFYNLVPNLTAKENVELAteVSPD-ALDPVE------VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:COG3840 78 QENNLFPHLTVAQNIGLG--LRPGlKLTAEQraqveqALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 165 PTGALDFETGKQVLKLLQNASRQHGNTVLIITHN--SALApIADRVIHINDAKV 216
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpeDAAR-IADRVLLVADGRI 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-216 |
5.22e-52 |
|
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: 175.48 E-value: 5.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPD---EGQIIIDDTDIAQFSDKQlt 80
Cdd:COG1123 5 LEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayRRTDVGFVFQ--FYNLVPnLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARAL 153
Cdd:COG1123 81 --RGRRIGMVFQdpMTQLNP-VTVGDQIAEALEnlgLSRAEARArvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSAL-APIADRVIHINDAKV 216
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-219 |
6.05e-52 |
|
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: 167.43 E-value: 6.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYR 83
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03301 72 R-DIAMVFQNYALYPHMTVYDNIAFGLKlrkVPKDEIDErvREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN--SALApIADRVIHINDAKVRSV 219
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqvEAMT-MADRIAVMNDGQIQQI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-216 |
4.61e-51 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 166.66 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQFYNLVPNLT 101
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEVS--PDALD---PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:cd03294 119 VLENVAFGLEVQgvPRAEReerAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 177 VLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHdlDEALR-LGDRIAIMKDGRL 239
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
4-197 |
7.83e-51 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 168.52 E-value: 7.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:TIGR02314 2 IKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:TIGR02314 82 R-QIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIkrkvtELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH 197
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITH 199
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-213 |
1.27e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.83 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 12 RYKMGETTItaNDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYRRtDVGFVF 91
Cdd:COG4619 7 SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRR-QVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 92 QfynlVPNL---TAKENVELATEVSPDALDP---VEVLRQVGLAHRLNNFP-SQLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:COG4619 81 Q----EPALwggTVRDNLPFPFQLRERKFDReraLELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 165 PTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSA-LAPIADRVIHIND 213
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEA 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-214 |
1.43e-50 |
|
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: 164.14 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKM---GETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDD----TDIAQFSDK 77
Cdd:COG4778 6 EVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 78 QLTAYRRTDVGFVFQFYNLVPNLTAKENVE---LATEVSPD-ALDPV-EVLRQVGLAHRL-NNFPSQLSGGEQQRVSIAR 151
Cdd:COG4778 86 EILALRRRTIGYVSQFLRVIPRVSALDVVAeplLERGVDREeARARArELLARLNLPERLwDLPPATFSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDA 214
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDeEVREAVADRVVDVTPF 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
25-224 |
1.52e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI---AQFSDKQLTAYRRtDVGFVFQFYNLVPNLT 101
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQ-KVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKEN-----VELATEVSPDALD-PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGK 175
Cdd:COG4161 99 VMENlieapCKVLGLSKEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 176 QVLKLLQNASrQHGNTVLIITHNSALA-PIADRVIHINDAKVrsVELNDH 224
Cdd:COG4161 179 QVVEIIRELS-QTGITQVIVTHEVEFArKVASQVVYMEKGRI--IEQGDA 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-217 |
2.12e-50 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 172.26 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYrrtdVGFVFQ----FYNlvpn 99
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQrphlFDT---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 lTAKENVELAT-EVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:COG4987 424 -TLRENLRLARpDATDEEL--WAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 168 ALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:COG4987 501 GLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-209 |
3.90e-50 |
|
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: 163.38 E-value: 3.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYkmGEttITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYRR 84
Cdd:cd03219 2 EVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT-----GLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TDVGFV--FQFYNLVPNLTAKENVELA----TEVSPDALDPV-----------EVLRQVGLAHRLNNFPSQLSGGEQQRV 147
Cdd:cd03219 73 ARLGIGrtFQIPRLFPELTVLENVMVAaqarTGSGLLLARARreereareraeELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVT 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-215 |
1.00e-49 |
|
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: 159.72 E-value: 1.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrR 84
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TDVGFVFQfynlvpnltakenvelatevspdaldpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488224859 165 PTGALDFETGKQVLKLLQNAsRQHGNTVLIITHNSALA-PIADRVIHINDAK 215
Cdd:cd00267 107 PTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-216 |
1.78e-49 |
|
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: 171.94 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYRRtDVGFVFQ----FYNlvpn 99
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRR-QIGVVLQdvflFSG---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 lTAKENVELA-TEVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:COG2274 564 -TIRENITLGdPDATDEEI--IEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488224859 168 ALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:COG2274 641 ALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-224 |
1.90e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 161.72 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDT--DIAQ-FSDKQLTAYRRtDVGFVFQFYNLVPNLT 101
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtPSDKAIRELRR-NVGMVFQQYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELA---------TEVSPDALDPVEVLRQVGLAHRlnnFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:PRK11124 99 VQQNLIEApcrvlglskDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488224859 173 TGKQVLKLLQNASrQHGNTVLIITHNSALA-PIADRVIHINDAKVrsVELNDH 224
Cdd:PRK11124 176 ITAQIVSIIRELA-ETGITQVIVTHEVEVArKTASRVVYMENGHI--VEQGDA 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-218 |
4.22e-49 |
|
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: 160.15 E-value: 4.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEkGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdIAQFSDKQL-TAYRRTDVGFVFQFYNLVPNLTAK 103
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALD---PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL 180
Cdd:cd03297 94 ENLAFGLKRKRNREDrisVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 181 LQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKVRS 218
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQY 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
24-224 |
4.32e-49 |
|
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: 168.78 E-value: 4.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQfyN-LVPNLTA 102
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQ--NpYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELAT-EVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:COG4988 428 RENLRLGRpDASDEEL--EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 171 FETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHINDAKVrsVELNDH 224
Cdd:COG4988 506 AETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRI--VEQGTH 555
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-216 |
9.10e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 163.96 E-value: 9.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqltAYR 83
Cdd:PRK09452 15 VELRGISKSF--DGKEVI--SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-----AEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIAR 151
Cdd:PRK09452 86 R-HVNTVFQSYALFPHMTVFENVafglrmqktpaaEITPRVM-------EALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQV---LKLLQnasRQHGNTVLIITHNS--ALApIADRVIHINDAKV 216
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMqneLKALQ---RKLGITFVFVTHDQeeALT-MSDRIVVMRDGRI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-215 |
1.20e-48 |
|
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: 158.41 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDkqltAYRRtDVGFVFQFYNLVPNLTAK 103
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE----DYRR-RLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATE---VSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL 180
Cdd:COG4133 94 ENLRFWAAlygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 488224859 181 LQNAsRQHGNTVLIITHNSALAPiADRVIHINDAK 215
Cdd:COG4133 174 IAAH-LARGGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-216 |
1.74e-48 |
|
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: 159.04 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETtitanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltayr 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-----KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEVSpdALDPVEVLRQV-------GLAHRLNNFPSQLSGGEQQRVSIARALAKN 156
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKR--KVDKKEIERKVleiaemlGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 157 PKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.84e-48 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 157.21 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayRR 84
Cdd:cd03214 1 EVENLSVGY--GGRTVL--DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--RK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 tdVGFVFQfynlvpnltakenvelatevspdaldpveVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:cd03214 75 --IAYVPQ-----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 165 PTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHdlNLAAR-YADRVILLKDGRI 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
2.86e-48 |
|
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: 156.40 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdKQLTAYR 83
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtDVGFVFQFYNLVPNLTAKENVElatevspdaldpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:cd03230 73 R-RIGYLPEEPSLYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 164 EPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-209 |
5.09e-48 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 158.66 E-value: 5.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYRRTDVGFV--FQFYNLV 97
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-----GLPPHRIARLGIArtFQNPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 PNLTAKENVELATEVS-------------------PDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:COG0411 92 PELTVLENVLVAAHARlgrgllaallrlprarreeREARERAeELLERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
5.45e-48 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 158.87 E-value: 5.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqlt 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrrTDVGFVFQFYNLVPNLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:COG4525 76 ----ADRGVVFQKDALLPWLNVLDNVAFGLRlrgVPKAERRARaeELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH 197
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
1.44e-47 |
|
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: 154.46 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYR 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL--KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVpNLTAKENVelatevspdaldpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:cd03228 76 KN-IAYVPQDPFLF-SGTIRENI--------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 164 EPTGALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHIND 213
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDD 169
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-166 |
1.69e-47 |
|
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: 153.96 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQFYNLVPNLTAK 103
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 104 ENV-------ELATEVSPDALDpvEVLRQVGLAH----RLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:pfam00005 78 ENLrlglllkGLSKREKDARAE--EALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
2.32e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 2.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqlt 80
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVL--EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayRRTDVGFVFQFYNLVPN--LTAKENVEL-----------ATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRV 147
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDfpITVRDVVLMgrygrrglfrrPSRADREAVD--EALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNaSRQHGNTVLIITHN-SALAPIADRVIHIND 213
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDlGAVREYFDRVLLLNR 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-217 |
1.89e-46 |
|
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: 154.25 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltayRR 84
Cdd:COG4555 3 EVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TDVGFVFQFYNLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKL 159
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELkkrieELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 160 LLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-217 |
1.96e-46 |
|
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: 157.18 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDT---DIAQFSDkqLTAYRRtDVGFVFQFYNLVPNLT 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIF--LPPHRR-RIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELA---TEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVL 178
Cdd:COG4148 94 VRGNLLYGrkrAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 179 KLLQNASRQHGNTVLIITHNSA-LAPIADRVIHINDAKVR 217
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-216 |
2.63e-46 |
|
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: 153.61 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETtitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEV----SPDALDPV-EVLRQVGL--AHRLNNFPSQLSGGEQQRVSIARALAKN 156
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLlkwpKEKIRERAdELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 157 PKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHdiDEAFR-LADRIAIMKNGEI 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-216 |
3.22e-46 |
|
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: 152.65 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 21 TANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqFSDKQltayrRTDVGFVFQFYNLVPNL 100
Cdd:cd03298 12 EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPA-----DRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELAteVSPD-ALDPVE------VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:cd03298 86 TVEQNVGLG--LSPGlKLTAEDrqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 174 GKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRI 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
1.07e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 152.65 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITAndDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSD------- 76
Cdd:COG4598 9 LEVRDLHKSF--GDLEVLK--GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 ---KQLTAYRrTDVGFVFQFYNLVPNLTAKENVELAtevspdaldPVEVLRQ---------------VGLAHRLNNFPSQ 138
Cdd:COG4598 85 adrRQLQRIR-TRLGMVFQSFNLWSHMTVLENVIEA---------PVHVLGRpkaeaieraeallakVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 139 LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFArDVSSHVVFLHQGRI 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
4.84e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKmGETTITAnddISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQI----IIDDTDIAQFSD 76
Cdd:PRK11264 1 MSAIEVKNLVKKFH-GQTVLHG---IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdITIDTARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 KQLTAYRRTDVGFVFQFYNLVPNLTAKENV-ELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIA 150
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEAtararELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASrQHGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-216 |
1.27e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 148.87 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGM-----DTPDEGQIIIDDTDIAQfSDKQ 78
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYD-LDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 79 LTAYRRTdVGFVFQFYNLVPnLTAKENVELA----TEVSPDALDPV--EVLRQVGLAHRLNN--FPSQLSGGEQQRVSIA 150
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGlrlhGIKLKEELDERveEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAArVADRTAFLLNGRL 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-216 |
3.54e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYRRTdVGFVFQ----FynlvpN 99
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQdtflF-----S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELAtevSPDALDP--VEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:COG1132 428 GTIRENIRYG---RPDATDEevEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 167 GALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:COG1132 505 SALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-208 |
4.73e-44 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 151.00 E-value: 4.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVE-VKNEYKRYKMgettitanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkqL 79
Cdd:NF040840 1 MIRIEnLSKDWKEFKL--------RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDIT------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 80 TAYRRTDVGFVFQFYNLVPNLTAKENVELATEVSpdALDPVEVLRQV-------GLAHRLNNFPSQLSGGEQQRVSIARA 152
Cdd:NF040840 67 LPPEKRGIAYVYQNYMLFPHKTVFENIAFGLKLR--KVPKEEIERKVkeimellGISHLLHRKPRTLSGGEQQRVALARA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 153 LAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN--SALApIADRV 208
Cdd:NF040840 145 LIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfeEALS-LADRV 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-216 |
5.53e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 148.29 E-value: 5.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 11 KRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDkqltayrrtDVGFV 90
Cdd:PRK11247 20 KRY--GERTVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE---------DTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 91 FQFYNLVPNLTAKENVELATEVS--PDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQwrDAAL---QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 169 LDFETGKQVLKLLQNASRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHdvSEAVA-MADRVLLIEEGKI 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-227 |
6.40e-44 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 149.95 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 38 ILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYRRTdVGFVFQFYNLVPNLTAKENV--------ELA 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-----VPPHLRH-INMVFQSYALFPHMTVEENVafglkmrkVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 110 TEVSPDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHG 189
Cdd:TIGR01187 75 AEIKPRVL---EALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488224859 190 NTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHPSS 227
Cdd:TIGR01187 152 ITFVFVTHDQEEAmTMSDRIAIMRKGKIAQIgtpeEIYEEPAN 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
12-231 |
7.58e-44 |
|
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: 150.65 E-value: 7.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 12 RYKMGETTItandDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDK-QLTAYRRTdVGFV 90
Cdd:TIGR02142 6 SKRLGDFSL----DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRR-IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 91 FQFYNLVPNLTAKENVELA---TEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGmkrARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 168 ALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKVRSVelndhpSSIDEI 231
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVAAA------GPIAEV 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-209 |
9.13e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 149.50 E-value: 9.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRY-------KMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSD 76
Cdd:COG4608 8 LEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 KQLTAYRRtDVGFVFQ--FYNLVPNLTAK----ENVELATEVSPDALDP--VEVLRQVGL-AHRLNNFPSQLSGGEQQRV 147
Cdd:COG4608 88 RELRPLRR-RMQMVFQdpYASLNPRMTVGdiiaEPLRIHGLASKAERRErvAELLELVGLrPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlSVVRHISDRVA 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
25-212 |
1.04e-43 |
|
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: 146.14 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFsdkqltayrRTDVGFVFQFYNLVPN--LTA 102
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------RKRIGYVPQRRSIDRDfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEVSPDALDPV---------EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:cd03235 88 RDVVLMGLYGHKGLFRRLskadkakvdEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 174 GKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHIN 212
Cdd:cd03235 168 QEDIYELLREL-RREGMTILVVTHDlGLVLEYFDRVLLLN 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-208 |
1.18e-43 |
|
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: 153.69 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKS----TILNILGGMDTPDEGQIIIDDTDIAQFSDKQLT 80
Cdd:COG4172 8 SVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTDVGFVFQfynlVPnLTA-----------KENVELATEVSPDALDP--VEVLRQVGL---AHRLNNFPSQLSGGEQ 144
Cdd:COG4172 88 RIRGNRIAMIFQ----EP-MTSlnplhtigkqiAEVLRLHRGLSGAAARAraLELLERVGIpdpERRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 145 QRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSAL-APIADRV 208
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVvRRFADRV 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-211 |
3.35e-43 |
|
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: 152.44 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQFYNLVPNlTAK 103
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELAT-EVSPDALDpvEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDF 171
Cdd:TIGR02857 414 ENIRLARpDASDAEIR--EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 172 ETGKQVLKLLQNASRqhGNTVLIITHNSALAPIADRVIHI 211
Cdd:TIGR02857 492 ETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-217 |
5.09e-43 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 144.57 E-value: 5.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltayr 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVELATEV-----SPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLkglpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQnaSRQHGNTVLIITHNSALAPI-ADRVIHINDAKVR 217
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-216 |
5.40e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 147.16 E-value: 5.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYkmGETTiTANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayRR 84
Cdd:COG1125 3 EFENVTKRY--PDGT-VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 tDVGFVFQFYNLVPNLTAKENVelatevspdALDPV--------------EVLRQVGL-----AHRlnnFPSQLSGGEQQ 145
Cdd:COG1125 77 -RIGYVIQQIGLFPHMTVAENI---------ATVPRllgwdkerirarvdELLELVGLdpeeyRDR---YPHELSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 146 RVSIARALAKNPKLLLCDEPTGALDFETGKQV---LKLLQnasRQHGNTVLIITH--NSALApIADRVIHINDAKV 216
Cdd:COG1125 144 RVGVARALAADPPILLMDEPFGALDPITREQLqdeLLRLQ---RELGKTIVFVTHdiDEALK-LGDRIAVMREGRI 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-219 |
1.67e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.15 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltayRRtdVGFVFQFYNLVPNLTAKE 104
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----RK--VGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATEVSPDALDP---------VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGK 175
Cdd:PRK10851 94 NIAFGLTVLPRRERPnaaaikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488224859 176 QVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSV 219
Cdd:PRK10851 174 ELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIEQA 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-217 |
2.59e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 144.11 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfSDKQLTAYR 83
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQfyN----LVpNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:TIGR04520 77 KK-VGMVFQ--NpdnqFV-GATVEDDVAFGLEnlgVPREEMRKrvDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-220 |
4.14e-42 |
|
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: 149.45 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKST----ILNILggmdtPDEGQIIIDDTDIAQFSDKQLTAYRRtDVGFVFQ--F 93
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQdpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 YNLVPNLTAKENVELATEVSPDALDP-------VEVLRQVGL----AHRlnnFPSQLSGGEQQRVSIARALAKNPKLLLC 162
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRVHGPGLSAaerrarvAEALEEVGLdpaaRHR---YPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 163 DEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVrsVE 220
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRaLAHRVMVMKDGKV--VE 506
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-209 |
9.85e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.60 E-value: 9.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtAYRR------TD 86
Cdd:PRK13548 10 VRLGGRTLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL-ARRRavlpqhSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 87 VGFVFqfynlvpnlTAKENVELATEV---SPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA------K 155
Cdd:PRK13548 87 LSFPF---------TVEEVVAMGRAPhglSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPI-ADRVI 209
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIV 212
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-217 |
1.56e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 141.79 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR-----RTDV 87
Cdd:COG4559 9 VRLGGRTLL--DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 88 GFVFqfynlvpnlTAKENVEL-----ATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA-------K 155
Cdd:COG4559 87 AFPF---------TVEEVVALgraphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITH--NSAlAPIADRVIHINDAKVR 217
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHdlNLA-AQYADRILLLHQGRLV 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-209 |
2.22e-40 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 138.37 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayrrtdvgfVFQFYNLVPNLTAK 103
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELAT-EVSPDALDPV------EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:TIGR01184 73 ENIALAVdRVLPDLSKSErraiveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*
gi 488224859 177 VLKLLQNASRQHGNTVLIITH--NSALApIADRVI 209
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHdvDEALL-LSDRVV 186
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-216 |
6.41e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 136.57 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:cd03245 3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQ----FYNlvpnlTAKENVELATEVSPDAlDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVS 148
Cdd:cd03245 77 RRNIGYVPQdvtlFYG-----TLRDNITLGAPLADDE-RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRqhGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-227 |
7.45e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 140.24 E-value: 7.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 3 YVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltay 82
Cdd:PRK11432 6 FVVLKNITKRF--GSNTVI--DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 rrTDVGFVFQFYNLVPNLTAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIA 150
Cdd:PRK11432 78 --RDICMVFQSYALFPHMSLGENVgyglkmlgvpkeERKQRVK-------EALELVDLAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHP 225
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIgspqELYRQP 228
|
..
gi 488224859 226 SS 227
Cdd:PRK11432 229 AS 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-198 |
2.33e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 136.37 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqltAYRrtdvGFVFQFYNLVPNLTAK 103
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AER----GVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVL 178
Cdd:PRK11248 89 DNVAFGLQlagVEKMQRLEIahQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180
....*....|....*....|
gi 488224859 179 KLLQNASRQHGNTVLIITHN 198
Cdd:PRK11248 169 TLLLKLWQETGKQVLLITHD 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-208 |
2.54e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.70 E-value: 2.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDD--TDIAQFSDkqltA 81
Cdd:COG3845 6 LELRGITKRF--G--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRD----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 yRRTDVGFVFQFYNLVPNLTAKENVELATEVSPDA-LDPVEVLRQVG-LAHRLnNFP-------SQLSGGEQQRVSIARA 152
Cdd:COG3845 78 -IALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGrLDRKAARARIReLSERY-GLDvdpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 153 LAKNPKLLLCDEPTGAL-DFETgKQVLKLLQNASRQhGNTVLIITH--NSALApIADRV 208
Cdd:COG3845 156 LYRGARILILDEPTAVLtPQEA-DELFEILRRLAAE-GKSIIFITHklREVMA-IADRV 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-227 |
2.75e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.20 E-value: 2.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYR 83
Cdd:PRK11607 20 LEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVelATEVSPDALDPVEVLRQV----GLAHrLNNF----PSQLSGGEQQRVSIARALAK 155
Cdd:PRK11607 91 RP-INMMFQSYALFPHMTVEQNI--AFGLKQDKLPKAEIASRVnemlGLVH-MQEFakrkPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 156 NPKLLLCDEPTGALDFETGK----QVLKLLQNAsrqhGNTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHPS 226
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDrmqlEVVDILERV----GVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIgepeEIYEHPT 242
|
.
gi 488224859 227 S 227
Cdd:PRK11607 243 T 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-216 |
5.48e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.71 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 27 SFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDtdiaqfSDKQLTAYRRTDVGFVFQFYNLVPNLTAKENV 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 107 ELAtevspdaLDP------------VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETG 174
Cdd:PRK10771 93 GLG-------LNPglklnaaqreklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488224859 175 KQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRI 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-224 |
6.97e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 141.50 E-value: 6.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQFYNLVpNLTAK 103
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVSQRVHLF-SATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELAtevSPDALDP--VEVLRQVGLAHRLNNFPS----------QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDF 171
Cdd:PRK11160 432 DNLLLA---APNASDEalIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 172 ETGKQVLKLLqnasRQH--GNTVLIITHN-SALAPIaDRVIHINDAKVRsvELNDH 224
Cdd:PRK11160 509 ETERQILELL----AEHaqNKTVLMITHRlTGLEQF-DRICVMDNGQII--EQGTH 557
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-211 |
4.21e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.84 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 19 TITAND-----DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPD---EGQIIIDDTDIAQfsdkqLTAYRRtDVGFV 90
Cdd:COG4136 8 TITLGGrpllaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA-----LPAEQR-RIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 91 FQFYNLVPNLTAKENVELATevsPDAL------DPVE-VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFAL---PPTIgraqrrARVEqALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 164 EPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:COG4136 159 EPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-217 |
4.47e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 131.57 E-value: 4.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfsDKQLTAYR 83
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY----QKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtdVGFVFQFYNLVPNLTAKENVEL---ATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLL 160
Cdd:cd03268 73 R--IGALIEAPGFYPNLTARENLRLlarLLGIRKKRID--EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 161 LCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-208 |
5.10e-38 |
|
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: 131.79 E-value: 5.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYRRTD--VGFVFQFYNLVPNLT 101
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-----LPPHERARagIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEVSPDAlDPVEVLRQV-----GLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:cd03224 92 VEENLLLGAYARRRA-KRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 177 VLKLLQnASRQHGNTVLIITHNSALA-PIADRV 208
Cdd:cd03224 171 IFEAIR-ELRDEGVTILLVEQNARFAlEIADRA 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-198 |
2.08e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 131.36 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGetTITAN---DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLT 80
Cdd:COG1101 2 LELKNLSKTFNPG--TVNEKralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-----KLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRT-DVGFVFQ--FYNLVPNLTAKENVELATE----------VSPDALDPV-EVLRQV--GLAHRLNNFPSQLSGGEQ 144
Cdd:COG1101 75 EYKRAkYIGRVFQdpMMGTAPSMTIEENLALAYRrgkrrglrrgLTKKRRELFrELLATLglGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 145 QRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN 198
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-201 |
3.54e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 129.61 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRtDVGFVFQFYNLVPNLTAKEN 105
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VELATEVSPDALDPVE-----VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL 180
Cdd:PRK10908 100 VAIPLIIAGASGDDIRrrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRL 179
|
170 180
....*....|....*....|.
gi 488224859 181 LQNASRQhGNTVLIITHNSAL 201
Cdd:PRK10908 180 FEEFNRV-GVTVLMATHDIGL 199
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-224 |
4.06e-37 |
|
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: 129.97 E-value: 4.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQfynlVPNL--- 100
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQ----EPVLfdg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELATEvSPDALDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:cd03249 92 TIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 170 DFETGKQVLKLLQNASRqhGNTVLIITHNsaLAPI--ADRVIHINDAKVrsVELNDH 224
Cdd:cd03249 171 DAESEKLVQEALDRAMK--GRTTIVIAHR--LSTIrnADLIAVLQNGQV--VEQGTH 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
7.30e-37 |
|
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: 127.16 E-value: 7.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmgeTTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqltayr 83
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 rtdvgfvfqfynlvpnltakenvelatEVSPdaLDPVEVLRQ-VGLAHrlnnfpsQLSGGEQQRVSIARALAKNPKLLLC 162
Cdd:cd03216 63 ---------------------------EVSF--ASPRDARRAgIAMVY-------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 163 DEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-216 |
1.37e-36 |
|
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: 128.50 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTAYR 83
Cdd:cd03253 1 IEFENVTFAYDPGRPVL---KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVpNLTAKENVELATevsPDALDpVEVLRQVGLAH---RLNNFPSQ-----------LSGGEQQRVSI 149
Cdd:cd03253 75 RA-IGVVPQDTVLF-NDTIGYNIRYGR---PDATD-EEVIEAAKAAQihdKIMRFPDGydtivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRqhGNTVLIITHNsaLAPI--ADRVIHINDAKV 216
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHR--LSTIvnADKIIVLKDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-216 |
1.63e-36 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 128.11 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:cd03254 3 IEFENVNFSYDEKKPVL---KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNlTAKENVELATEVSPDAlDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARA 152
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIMENIRLGRPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 153 LAKNPKLLLCDEPTGALDFETGkqvlKLLQNASR--QHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETE----KLIQEALEklMKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
1.95e-36 |
|
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: 128.12 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVpNLTAKENVELATEVSPDAlDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARA 152
Cdd:cd03251 75 RRQIGLVSQDVFLF-NDTVAENIAYGRPGATRE-EVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 153 LAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRqhGNTVLIITHNsaLAPI--ADRVIHINDAKVrsVELNDH 224
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHR--LSTIenADRIVVLEDGKI--VERGTH 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-223 |
7.11e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.54 E-value: 7.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQFYNLVPNLTAKE 104
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATEVSPDALD-----PVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLK 179
Cdd:PRK10070 126 NTAFGMELAGINAEerrekALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488224859 180 LLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSVELND 223
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVVQVGTPD 250
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-230 |
1.08e-35 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 126.45 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqFSDKqltAYR 83
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIL--DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADP---AWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQfYNLVPNLTAKENVELATEvSPDALDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARA 152
Cdd:cd03252 75 RRQVGVVLQ-ENVLFNRSIRDNIALADP-GMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 153 LAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRqhGNTVLIITHNSALAPIADRVIHINDAKVrsVELNDHPSSIDE 230
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRI--VEQGSHDELLAE 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-217 |
1.16e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.56 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdKQLTAYR 83
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtdVGFVFQFYNLVPNLTAKENVE-------LATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKN 156
Cdd:cd03266 79 R--LGFVSDSTGLYDRLTARENLEyfaglygLKGDELTARLE--ELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 157 PKLLLCDEPTGALDFETGKQVLKLLQnASRQHGNTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-209 |
1.72e-35 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 125.87 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGM-DTPD----EGQIIIDDTDIaqFSDKQ 78
Cdd:TIGR00972 2 IEIENLNLFY--GEKE--ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQDI--YDKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 79 LTAYRRTDVGFVFQFYNLVPnLTAKENVELATEV----SPDALDPV--EVLRQVGL----AHRLNNFPSQLSGGEQQRVS 148
Cdd:TIGR00972 76 DVVELRRRVGMVFQKPNPFP-MSIYDNIAYGPRLhgikDKKELDEIveESLKKAALwdevKDRLHDSALGLSGGQQQRLC 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRVI 209
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAArISDRTA 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-208 |
1.82e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 125.48 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYRRTD--VGFVFQFYNLVPNLTA 102
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-----LPPHRIARlgIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEVSPDALDPVEVLRQVG-----LAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTgaldfeTG--- 174
Cdd:COG0410 96 EENLLLGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS------LGlap 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 488224859 175 ---KQVLKLLQNASRQhGNTVLIITHNSALA-PIADRV 208
Cdd:COG0410 170 livEEIFEIIRRLNRE-GVTILLVEQNARFAlEIADRA 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-208 |
3.48e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGM--DTPD---EGQIIIDDTDIaqfSDKQLTAYR-RTDVGFVFQfynlVP 98
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDI---YDPDVDVVElRRRVGMVFQ----KP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAK---ENV----ELATEVSPDALD-PVE-VLRQVGL----AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:COG1117 102 NPFPKsiyDNVayglRLHGIKSKSELDeIVEeSLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 166 TGALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRV 208
Cdd:COG1117 182 TSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAArVSDYT 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-209 |
5.94e-35 |
|
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: 123.92 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDE---GQIIIDdtdiAQFSDKQLTAYRrtdVGFVFQFYNLVPNLT 101
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFN----GQPRKPDQFQKC---VAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENV---------ELATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:cd03234 98 VRETLtytailrlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 173 TGKQVLKLLQNASRQhGNTVLIITHN--SALAPIADRVI 209
Cdd:cd03234 178 TALNLVSTLSQLARR-NRIVILTIHQprSDLFRLFDRIL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-216 |
1.92e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.54 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYkmGETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDK--QLTAYR 83
Cdd:PRK10619 8 VIDLHKRY--GEHEVLKG--VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 -------RTDVGFVFQFYNLVPNLTAKENV-ELATEV----SPDALD-PVEVLRQVGLAHRLN-NFPSQLSGGEQQRVSI 149
Cdd:PRK10619 84 knqlrllRTRLTMVFQHFNLWSHMTVLENVmEAPIQVlglsKQEARErAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASrQHGNTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARhVSSHVIFLHQGKI 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-216 |
2.03e-34 |
|
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: 121.17 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKMGETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYRR 84
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRN--VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 TdVGFVFQFYNLVPNlTAKENVelatevspdaldpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:cd03246 77 H-VGYLPQDDELFSG-SIAENI--------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488224859 165 PTGALDFETGKQVLKLLQNAsRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
3.94e-34 |
|
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: 121.53 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGEttitANDDISFSIEKGELVIiLGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdKQLTAYR 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVE---LATEVSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDyiaWLKGIPSKEVKArvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHgnTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-224 |
3.97e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.06 E-value: 3.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKmGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLT 80
Cdd:COG1137 1 MMTLEAENLVKSYG-KRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----HLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTDVGF--------VFQfynlvpNLTAKENVELATEVSPdaLDPVEVLRQV-------GLAHRLNNFPSQLSGGEQQ 145
Cdd:COG1137 72 MHKRARLGIgylpqeasIFR------KLTVEDNILAVLELRK--LSKKEREERLeelleefGITHLRKSKAYSLSGGERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 146 RVSIARALAKNPKLLLCDEPTGALD----FETGKQVLKLlqnasRQHGNTVLIITHN--SALApIADR--VIH------- 210
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHL-----KERGIGVLITDHNvrETLG-ICDRayIISegkvlae 217
|
250 260
....*....|....*....|
gi 488224859 211 ------INDAKVRSVELNDH 224
Cdd:COG1137 218 gtpeeiLNNPLVRKVYLGED 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-216 |
5.62e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqltAYRRTDVGFVFQ--FYNLVPNlT 101
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-------KERRKSIGYVMQdvDYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEVSPDALDPVE-VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL 180
Cdd:cd03226 89 VREELLLGLKELDAGNEQAEtVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 488224859 181 LQNASRQhGNTVLIITHNSA-LAPIADRVIHINDAKV 216
Cdd:cd03226 169 IRELAAQ-GKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-219 |
5.88e-34 |
|
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: 121.32 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltaYR 83
Cdd:cd03265 1 IEVENLVKKY--GDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFYNLVPNLTAKENVELATE---VSPDALDP--VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:cd03265 73 RR-IGIVFQDLSVDDELTGWENLYIHARlygVPGAERREriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 159 LLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVRSV 219
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEqLCDRVAIIDHGRIIAE 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-224 |
7.84e-34 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 121.61 E-value: 7.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYKMGETTitanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTAYRRT 85
Cdd:TIGR04406 4 AENLIKSYKKRKVV----NDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI---THLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 86 DVGFVFQFYNLVPNLTAKENVELATEVSPDaLDP-------VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPK 158
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLEIRKD-LDRaereerlEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 159 LLLCDEPTGALD---FETGKQVLKLLqnasRQHGNTVLIITHN-SALAPIADR--VIH-------------INDAKVRSV 219
Cdd:TIGR04406 156 FILLDEPFAGVDpiaVGDIKKIIKHL----KERGIGVLITDHNvRETLDICDRayIISdgkvlaegtpaeiVANEKVRRV 231
|
....*
gi 488224859 220 ELNDH 224
Cdd:TIGR04406 232 YLGEQ 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-216 |
1.17e-33 |
|
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: 120.73 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkQLTAYR 83
Cdd:cd03218 1 LRAENLSKRY--GKRKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-----KLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVF--QFYNLVPNLTAKENVELATEVSPDA-------LDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:cd03218 72 RARLGIGYlpQEASIFRKLTVEENILAVLEIRGLSkkereekLE--ELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-198 |
1.28e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.72 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRtDVGFVFQ--FYNLVPNLT 101
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRR-DIQMVFQdsISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENV-----ELATevspdaLDPV-------EVLRQVGLAHR-LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK10419 108 VREIIreplrHLLS------LDKAerlarasEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190
....*....|....*....|....*....|
gi 488224859 169 LDFETGKQVLKLLQNASRQHGNTVLIITHN 198
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-209 |
1.51e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 121.45 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRtDVGFVFQ-FYNLV-PNLT 101
Cdd:TIGR02769 28 TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRR-DVQLVFQdSPSAVnPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AK----ENVELATEVSPDALDP--VEVLRQVGL-AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETG 174
Cdd:TIGR02769 107 VRqiigEPLRHLTSLDESEQKAriAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 488224859 175 KQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVI 209
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVA 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-208 |
1.78e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.52 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmgeTTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYR 83
Cdd:COG1129 5 LEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 rtdVGFVFQFYNLVPNLTAKENVELATE-VSPDALDP-------VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:COG1129 81 ---IAIIHQELNLVPNLSVAENIFLGREpRRGGLIDWramrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 156 NPKLLLCDEPTGALdfeTGKQVLKLLQ--NASRQHGNTVLIITH--NSALApIADRV 208
Cdd:COG1129 158 DARVLILDEPTASL---TEREVERLFRiiRRLKAQGVAIIYISHrlDEVFE-IADRV 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-197 |
2.45e-33 |
|
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: 118.81 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGG--MDTPDEGQIIIDDTDIAQFSDKQLtayrrtdVGFVFQFYNLVPNLT 101
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI-------IGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEvspdaldpvevLRQvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLL 181
Cdd:cd03213 99 VRETLMFAAK-----------LRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170
....*....|....*.
gi 488224859 182 QNASRQhGNTVLIITH 197
Cdd:cd03213 155 RRLADT-GRTIICSIH 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
2.80e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETtitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFSDKQLTAYR 83
Cdd:PRK13639 2 LETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQfyNLVPNL---TAKENV------------ELATEVSpdaldpvEVLRQVGLAHRLNNFPSQLSGGEQQRVS 148
Cdd:PRK13639 78 KT-VGIVFQ--NPDDQLfapTVEEDVafgplnlglskeEVEKRVK-------EALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALAPI-ADRVIHINDAKV 216
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKI 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
6.76e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:PRK13632 8 IKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFY-NLVPNLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:PRK13632 82 RKKIGIIFQNPdNQFIGATVEDDIAFGLEnkkVPPKKMKDIidDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-209 |
7.46e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 121.22 E-value: 7.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfSDKQLTAYRRTDVGFVFQ--F 93
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQnpY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 YNLVP----------------NLTAKENVELAtevspdaldpVEVLRQVGL----AHRlnnFPSQLSGGEQQRVSIARAL 153
Cdd:PRK11308 103 GSLNPrkkvgqileepllintSLSAAERREKA----------LAMMAKVGLrpehYDR---YPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlSVVEHIADEVM 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-220 |
1.47e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 118.79 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYK-----MGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFS 75
Cdd:COG4167 2 SALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 76 DKQltaYRRTDVGFVFQFYN--LVPNLTAKENVE----LATEVSPDALDP--VEVLRQVGL-AHRLNNFPSQLSGGEQQR 146
Cdd:COG4167 81 DYK---YRCKHIRMIFQDPNtsLNPRLNIGQILEeplrLNTDLTAEEREEriFATLRLVGLlPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 147 VSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVrsVE 220
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEV--VE 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-216 |
4.23e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.76 E-value: 4.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQFYNLVpNLTAK 103
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLF-NRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELAtevSPDALDpVEVLRQVGLAH-------RLNNFP-------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PRK13657 427 DNIRVG---RPDATD-EEMRAAAERAQahdfierKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488224859 170 DFETGKQVLKLLQNASrqHGNTVLIITHNsaLAPI--ADRVIHINDAKV 216
Cdd:PRK13657 503 DVETEAKVKAALDELM--KGRTTFIIAHR--LSTVrnADRILVFDNGRV 547
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-216 |
4.27e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaQFSDKQLTAYR 83
Cdd:PRK13635 6 IRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQFY-NLVPNLTAKENVELATEVS----PDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:PRK13635 81 RQ-VGMVFQNPdNQFVGATVQDDVAFGLENIgvprEEMVERVdQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-219 |
4.89e-32 |
|
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: 121.83 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDT--PDEGQII---------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL----KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 66 --------------IDDTDIAQFSDKQLTAYRRTdVGFVFQ-FYNLVPNLTAKENVELATE----VSPDALD-PVEVLRQ 125
Cdd:TIGR03269 77 kvgepcpvcggtlePEEVDFWNLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNVLEALEeigyEGKEAVGrAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 126 VGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH-NSALAPI 204
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVIEDL 235
|
250
....*....|....*
gi 488224859 205 ADRVIHINDAKVRSV 219
Cdd:TIGR03269 236 SDKAIWLENGEIKEE 250
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-226 |
5.24e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.35 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltAYRRtDVGFVFQ 92
Cdd:PRK10247 15 YLAGDAKIL--NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQ-QVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 93 fynlVPNL---TAKENVELATEVSPDALDPVEVLR---QVGLA-HRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:PRK10247 89 ----TPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDdleRFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 166 TGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVRSVELNDHPS 226
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEARYELA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-218 |
7.66e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.82 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 38 ILGPSGAGKSTILNILGGMDTPDEGQIIIDDT---DIAQfsDKQLTAYRRtDVGFVFQFYNLVPNLTAKENVE--LATEV 112
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLPPEKR-RIGYVFQDARLFPHYKVRGNLRygMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 113 SPDALDPVEVLrqvGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTV 192
Cdd:PRK11144 106 VAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPI 182
|
170 180
....*....|....*....|....*....
gi 488224859 193 LIITHNsaLAPI---ADRVIHINDAKVRS 218
Cdd:PRK11144 183 LYVSHS--LDEIlrlADRVVVLEQGKVKA 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
8.01e-32 |
|
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: 115.46 E-value: 8.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDdtdiaqfsDKQLTAYR 83
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--------GKPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKEN-VELA-------TEVSPDALdpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQlVYLAqlkglkkEEARRRID---EWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 156 NPKLLLCDEPTGALDfETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVR 217
Cdd:cd03269 146 DPELLILDEPFSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEeLCDRVLLLNKGRAV 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-198 |
8.91e-32 |
|
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: 121.31 E-value: 8.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQfynlVPNL--- 100
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQ----DAHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELAT-EVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:TIGR02868 424 TVRENLRLARpDATDEEL--WAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 488224859 169 LDFETGKQVLKLLQNASRqhGNTVLIITHN 198
Cdd:TIGR02868 502 LDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-228 |
1.76e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.79 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDD-----TDIAQFSDKQLTAYRRTDVGFVFQfyN--- 95
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWGFVHQ--Hprd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 -LVPNLTAKENV-E--LAT---------EVSPDALDPVEVLrqvglAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLC 162
Cdd:PRK11701 101 gLRMQVSAGGNIgErlMAVgarhygdirATAGDWLERVEID-----AARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 163 DEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPI-ADRVIHINDAKVrsVE-------LND--HP------S 226
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRV--VEsgltdqvLDDpqHPytqllvS 253
|
..
gi 488224859 227 SI 228
Cdd:PRK11701 254 SV 255
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-224 |
1.87e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 120.59 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVpNLTAKENVELAtevSPDALDPVEVLRQVGLAHRL---NNFP-----------SQLSGGEQQRVSI 149
Cdd:TIGR02203 405 RRQVALVSQDVVLF-NDTIANNIAYG---RTEQADRAEIERALAAAYAQdfvDKLPlgldtpigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNAsrQHGNTVLIITHNSALAPIADRVIHINDAKVrsVELNDH 224
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLSTIEKADRIVVMDDGRI--VERGTH 551
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-216 |
3.98e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.57 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGE--TTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTA 81
Cdd:PRK13633 5 IKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT---SDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 YRRTDVGFVFQfyNLVPNLTA---KENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARAL 153
Cdd:PRK13633 82 DIRNKAGMVFQ--NPDNQIVAtivEEDVAFGPEnlgIPPEEIRERvdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-209 |
8.47e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 115.61 E-value: 8.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKS-TILNILGGMDTPDE---GQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQ--FYN 95
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLEFNGQDLQRISEKERRNLVGAEVAMIFQdpMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLTAKENVELATEVSPDALD------PVEVLRQVGL---AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKktrrqrAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 167 GALDFETGKQVLKLLQNASRQHGNTVLIITHNSAL-APIADRVI 209
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKII 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-197 |
1.17e-30 |
|
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: 113.64 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQiiiddtDIAQFsDKQLTAYR----RTDVGFV- 90
Cdd:COG1119 14 GGKTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRLF-GERRGGEDvwelRKRIGLVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 91 -FQFYNLVPNLTAKE--------NVELATEVSPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLL 160
Cdd:COG1119 85 pALQLRFPRDETVLDvvlsgffdSIGLYREPTDEQRERArELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 488224859 161 LCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH 197
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-217 |
1.70e-30 |
|
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: 117.93 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYrrtdVGFVFQFYNLVPNlTAKE 104
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATEVSPDALdpVEVLRQVGlAHRL-NNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDfE 172
Cdd:COG4618 425 NIARFGDADPEKV--VAAAKLAG-VHEMiLRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD-D 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488224859 173 TGKQVL-KLLQNAsRQHGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:COG4618 501 EGEAALaAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-216 |
1.73e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.99 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsDKQLT-AYRRTDVGFVFQF--YNLVP 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT---DKKVKlSDIRKKVGLVFQYpeYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKE------NVELATEvspDALDPV-EVLRQVGLAHR--LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PRK13637 99 ETIEKDiafgpiNLGLSEE---EIENRVkRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 170 DFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKC 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-208 |
2.90e-30 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 112.24 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMdTPDEGQIIIDDTDIAQFSDKQLTAYR-----RTDVGF---VFQFYNL- 96
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFampVFQYLALh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELAtevspdaldPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARAL-----AKNP--KLLLCDEPTGAL 169
Cdd:COG4138 94 QPAGASSEAVEQL---------LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488224859 170 DFETGKQVLKLLQNASRQhGNTVLIITH--NSALAPiADRV 208
Cdd:COG4138 165 DVAQQAALDRLLRELCQQ-GITVVMSSHdlNHTLRH-ADRV 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-197 |
5.59e-30 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 116.84 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQ----FynlvpN 99
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQdtvlF-----N 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELAtevSPDAlDPVEVLRQVGLAHrLNNFPSQ---------------LSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:COG5265 446 DTIAYNIAYG---RPDA-SEEEVEAAARAAQ-IHDFIESlpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 165 PTGALDFETGKQVLKLLQNASRQHgnTVLIITH 197
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGR--TTLVIAH 551
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-224 |
5.72e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.13 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltaYRRTDVGFVFQFYNLVpNLTAKE 104
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH----YLHRQVALVGQEPVLF-SGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATEVSPDAlDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDfet 173
Cdd:TIGR00958 574 NIAYGLTDTPDE-EIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488224859 174 gKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVrsVELNDH 224
Cdd:TIGR00958 650 -AECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV--VEMGTH 697
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-225 |
8.27e-30 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 110.66 E-value: 8.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQfynlVPNL---TAKENVELATEVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSI 149
Cdd:cd03244 77 RSRISIIPQ----DPVLfsgTIRSNLDPFGEYSDEEL--WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHgnTVLIITHNsaLAPIA--DRVIHINDAKVrsVELnDHP 225
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHR--LDTIIdsDRILVLDKGRV--VEF-DSP 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
25-223 |
1.19e-29 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 111.08 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTD-----IAQFSDKQLTAYRRTDVGFVFQ--FYNLV 97
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQnpRDGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 PNLTAKENVE---LAT---------EVSPDALDPVEVLRQvglahRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:TIGR02323 101 MRVSAGANIGerlMAIgarhygnirATAQDWLEEVEIDPT-----RIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 166 TGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKVRSVELND 223
Cdd:TIGR02323 176 TGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVESGLTD 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-197 |
1.25e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 111.26 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDE---------GQIIIDDTDIAQFSDKQltayrRTDVGFVFQFYNL 96
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKS-----RANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVEL-ATEVSP------------DALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:PRK09984 98 VNRLSVLENVLIgALGSTPfwrtcfswftreQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190
....*....|....*....|....*....|....
gi 488224859 164 EPTGALDFETGKQVLKLLQNASRQHGNTVLIITH 197
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLH 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
4.77e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 4.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmGETTITANDdISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:PRK13648 8 IVFKNVSFQYQ-SDASFTLKD-VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQF-YNLVPNLTAKENVELATE---VSPDALDPV--EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLEnhaVPYDEMHRRvsEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 158 KLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-226 |
8.27e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.27 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQlt 80
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrrTDVGFVFQFYNLVPNLTAKEN----VELATEVSPDALDPVE-VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:PRK11000 75 ----RGVGMVFQSYALYPHLSVAENmsfgLKLAGAKKEEINQRVNqVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHPS 226
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVgkplELYHYPA 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-216 |
1.24e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.25 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayR 83
Cdd:COG4604 2 IEIKNVSKRY--GGKVVL--DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RtdVGFVFQFYNLVPNLTAKENVELA---------TEVSPDALDpvEVLRQVGL---AHRlnnFPSQLSGGEQQRVSIAR 151
Cdd:COG4604 76 R--LAILRQENHINSRLTVRELVAFGrfpyskgrlTAEDREIID--EAIAYLDLedlADR---YLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITH--NSAlAPIADRVIHINDAKV 216
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHdiNFA-SCYADHIVAMKDGRV 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-209 |
1.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTAYRRtDVGFVFQF--YNLVPNl 100
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRK-KVSLVFQFpeAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELATE---VSPDALD--PVEVLRQVGLAHRL-NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETG 174
Cdd:PRK13641 102 TVLKDVEFGPKnfgFSEDEAKekALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 488224859 175 KQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK13641 182 KEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVL 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-212 |
1.99e-28 |
|
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: 107.42 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 19 TITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayRRtdVGFVF-QFYNLV 97
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL---RR--IGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 PNLTAKENVELATEVSpdALDPVEVLRQVG-------LAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:cd03267 108 WDLPVIDSFYLLAAIY--DLPPARFKKRLDelselldLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488224859 171 FETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHIN 212
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVID 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
2.49e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETtitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFY-NLVPNLTAKENVELATEVSpdALDPVEVLRQVGLAHRLNNF-------PSQLSGGEQQRVSIARALAK 155
Cdd:PRK13647 78 RSKVGLVFQDPdDQVFSSTVWDDVAFGPVNM--GLDKDEVERRVEEALKAVRMwdfrdkpPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 156 NPKLLLCDEPTGALDfETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:PRK13647 156 DPDVIVLDEPMAYLD-PRGQETLMEILDRLHNQGKTVIVATHDVDLAaEWADQVIVLKEGRV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-222 |
3.63e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.31 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIID-DTDIA-----QFSDKQLTAYrrtdvGFVFQ-FYNL 96
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGylpqePPLDDDLTVL-----DTVLDgDAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELATEVSPDALDPV--------------------EVLRQVGLAHRLNNFP-SQLSGGEQQRVSIARALAK 155
Cdd:COG0488 90 RALEAELEELEAKLAEPDEDLERLaelqeefealggweaearaeEILSGLGFPEEDLDRPvSELSGGWRRRVALARALLS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 156 NPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITHNSA-LAPIADRVIHINDAKVRSVELN 222
Cdd:COG0488 170 EPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHDRYfLDRVATRILELDRGKLTLYPGN 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
5.01e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTITANDdISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDtdiaqfsdKQLT 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLND-VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG--------DLLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYR----RTDVGFVFQFY-NLVPNLTAKENVELATEVSPDALDPV-----EVLRQVGLAHRLNNFPSQLSGGEQQRVSIA 150
Cdd:PRK13650 73 EENvwdiRHKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMkervnEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVRSV 219
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVEST 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-216 |
6.71e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.87 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKN---EYKRYKMGE--------------TTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIII 66
Cdd:COG4586 2 IEVENlskTYRVYEKEPglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 67 DDTDIAqfsdKQLTAYRRtDVGFVF-QFYNLVPNLTAKENVELATE---VSPDALDP-----VEVLrqvGLAHRLNNFPS 137
Cdd:COG4586 82 LGYVPF----KRRKEFAR-RIGVVFgQRSQLWWDLPAIDSFRLLKAiyrIPDAEYKKrldelVELL---DLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 138 QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSA-LAPIADRVIHINDAKV 216
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVIVIDHGRI 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-198 |
6.77e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.13 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKmGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLT 80
Cdd:PRK10895 1 MATLTAKNLAKAYK-GRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTDVGFVFQFYNLVPNLTAKENVELATEVSPD------ALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDlsaeqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN 198
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHN 196
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-209 |
8.50e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.87 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 19 TITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAyRRTDVGFVFQ--FYNL 96
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQdpLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELATEVSPDALDPVEV-------LRQVGLAHRL-NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK15079 112 NPRMTIGEIIAEPLRTYHPKLSRQEVkdrvkamMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 169 LDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDlAVVKHISDRVL 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-208 |
9.01e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITANDDISFSIEKGELVIILGPSGAGKS-TILNILGGMDTPD----EGQIIIDDTDIAQFSDKQLTAYRRTDV 87
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 88 GFVFQ--------FYNLVPNLTakENVELATEVSPDAL--DPVEVLRQVGL---AHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:PRK15134 95 AMIFQepmvslnpLHTLEKQLY--EVLSLHRGMRREAArgEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRV 208
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRV 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-216 |
1.23e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 109.89 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYkrYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQII-------IDDTDIAQ 73
Cdd:TIGR03269 280 IKVRNVSKRY--ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 74 FSDKQLTAYrrtdVGFVFQFYNLVPNLTAKENVELATEVS-PDAL---DPVEVLRQVGLAHR-----LNNFPSQLSGGEQ 144
Cdd:TIGR03269 358 DGRGRAKRY----IGILHQEYDLYPHRTVLDNLTEAIGLElPDELarmKAVITLKMVGFDEEkaeeiLDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 145 QRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-216 |
1.34e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDE---GQIIIDDTDIAQFSDKQLt 80
Cdd:PRK13640 6 VEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrRTDVGFVFQFY-NLVPNLTAKENVELATE----VSPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:PRK13640 83 ---REKVGIVFQNPdNQFVGATVGDDVAFGLEnravPRPEMIKIVrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-212 |
1.89e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 103.73 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdKQLTAYRRtdvgfvfqfyNLV------ 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQ----------DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 ---PNLTAKENV----ELATEVSPDALdpVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PRK13538 84 gikTELTALENLrfyqRLHGPGDDEAL--WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488224859 171 fetgKQVLKLLQNASRQH---GNTVLIITHNSaLAPIADRVIHIN 212
Cdd:PRK13538 162 ----KQGVARLEALLAQHaeqGGMVILTTHQD-LPVASDKVRKLR 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-209 |
2.49e-27 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 104.27 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGG--MDTPDEGQIIIDDTDIAQfsdkqltayrrtdvgfvfqfynlvpNLT 101
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR-------------------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATevspDALDPVEVLRQVGLAHRLNNF--PSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLK 179
Cdd:COG2401 102 LIDAIGRKG----DFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190
....*....|....*....|....*....|....
gi 488224859 180 LLQNASRQHGNTVLIITHN----SALAPiaDRVI 209
Cdd:COG2401 178 NLQKLARRAGITLVVATHHydviDDLQP--DLLI 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-216 |
3.00e-27 |
|
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: 102.90 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayRRTDVGFV---FQFYNLVPNL 100
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELatevspdaldpvevlrqvglahrlnnfPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL 180
Cdd:cd03215 94 SVAENIAL---------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 181 LqNASRQHGNTVLIIThnSALAPI---ADRVIHINDAKV 216
Cdd:cd03215 147 I-RELADAGKAVLLIS--SELDELlglCDRILVMYEGRI 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-198 |
3.47e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKST----ILNILggmdtPDEGQIIIDDTDIAQFSDKQLTAYRRTdVGFVFQFYN--LVP 98
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKENVELATEVSPDALDP-------VEVLRQVGLA----HRlnnFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:PRK15134 378 RLNVLQIIEEGLRVHQPTLSAaqreqqvIAVMEEVGLDpetrHR---YPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 168 ALDFETGKQVLKLLQNASRQHGNTVLIITHN 198
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-209 |
3.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTAYRRTdVGFVFQF--YNLVPNLT 101
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKK-VGIVFQFpeHQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKE------NVELATEvspDALDPV-EVLRQVGLAHR-LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:PRK13634 104 EKDicfgpmNFGVSEE---DAKQKArEMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 488224859 174 GKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIV 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-197 |
4.27e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILN-ILGGMdtPDEGQIIIDDTDIAQFSdkqLTAYRRTdVGFVFQfyNlvPNL---T 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD---PESWRKH-LSWVGQ--N--PQLphgT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELAtevSPDALDpvEVLRQV---------------GLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK11174 439 LRDNVLLG---NPDASD--EQLQQAlenawvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 167 GALDFETGKQVLKLLQNASRQHgnTVLIITH 197
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQ--TTLMVTH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-215 |
6.59e-27 |
|
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: 102.55 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILN-ILGGMdTPDEGQIIIDDTdiaqfsdkqltayrrtdVGFVFQFYNLVpNLTAK 103
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS-----------------IAYVSQEPWIQ-NGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALDpvEVLRQVGLAHRLNNFPSQ-----------LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:cd03250 84 ENILFGKPFDEERYE--KVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488224859 173 TGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAK 215
Cdd:cd03250 162 VGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-213 |
9.00e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 9.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDiaqfsdkqltayrrtDVGFVFQF-YnlVPNLTA 102
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------------RVLFLPQRpY--LPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENV---ELATEVSPDALdpVEVLRQVGLAH---RLN---NFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:COG4178 443 REALlypATAEAFSDAEL--REALEAVGLGHlaeRLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 174 GKQVLKLLQnaSRQHGNTVLIITHNSALAPIADRVIHIND 213
Cdd:COG4178 521 EAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-197 |
1.15e-26 |
|
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: 101.67 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDK--QLTAYRRTDVGfvfqf 93
Cdd:TIGR01189 11 GERMLFEG--LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLGHLPG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 ynLVPNLTAKENVE-LATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDfe 172
Cdd:TIGR01189 84 --LKPELSALENLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-- 159
|
170 180
....*....|....*....|....*...
gi 488224859 173 tgKQVLKLLQNASRQH---GNTVLIITH 197
Cdd:TIGR01189 160 --KAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-197 |
1.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTAYRRTdVGFVFQF-YNLVPNLTA 102
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKK-VGLVFQFpESQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATE---VSPDALDPV--EVLRQVGLAHRL-NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:PRK13649 104 LKDVAFGPQnfgVSQEEAEALarEKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180
....*....|....*....|.
gi 488224859 177 VLKLLQNAsRQHGNTVLIITH 197
Cdd:PRK13649 184 LMTLFKKL-HQSGMTIVLVTH 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-216 |
1.68e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.16 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltaYRRTDVGFVFQfynlVPNLTAK- 103
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQ----EPVLFARs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 --ENVELATEVSPDalDPVEVLRQVGLAHR-LNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:cd03248 104 lqDNIAYGLQSCSF--ECVKEAAQKAHAHSfISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488224859 170 DFETGKQVLKLLQNASRQHgnTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03248 182 DAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
16-166 |
1.93e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.83 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqLTAYRRTD--VGFVFQF 93
Cdd:TIGR03410 11 GQSHIL--RGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-----LPPHERARagIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 YNLVPNLTAKENVELATEVSPDALDPVE--------VLRQVgLAHRLNNfpsqLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLAALPRRSRKIPdeiyelfpVLKEM-LGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEP 158
|
.
gi 488224859 166 T 166
Cdd:TIGR03410 159 T 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-215 |
4.44e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.61 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayrRTDVGFVFQFYNLVPNLT 101
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELAT-------------------EVSPDALDPVEV-LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLL 161
Cdd:PRK11300 97 VIENLLVAQhqqlktglfsgllktpafrRAESEALDRAATwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 162 CDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAK 215
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGT 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-217 |
4.95e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqlTAYRRtdVGFVFQFYN 95
Cdd:PRK09536 14 GDTTVL--DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR--AASRR--VASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLTAKENVEL-----------ATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:PRK09536 88 LSFEFDVRQVVEMgrtphrsrfdtWTETDRAAVE--RAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 165 PTGALDFETGKQVLKLLQNASrQHGNTVLIITHNSALAP-IADRVIHINDAKVR 217
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAArYCDELVLLADGRVR 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-197 |
5.24e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 103.37 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDtdiAQFSDKQLTAYRRtdVGFVFQFYNLVPNLTAK 103
Cdd:PRK13536 58 NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARLARAR--IGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENV-------ELATEVSPDALDPveVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:PRK13536 133 ENLlvfgryfGMSTREIEAVIPS--LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180
....*....|....*....|.
gi 488224859 177 VLKLLQNASRQhGNTVLIITH 197
Cdd:PRK13536 211 IWERLRSLLAR-GKTILLTTH 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-216 |
5.84e-26 |
|
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: 99.31 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltayRRTDVGFVFQ 92
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 93 FYNLvpnltakenveLATEVspdaldpvevlrqvglahrLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:cd03247 83 RPYL-----------FDTTL-------------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 173 TGKQVLKLLQNASRqhGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:cd03247 133 TERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-209 |
7.28e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQiiiddtdiaqfsdkqLTAYRRTDVGFVFQFYNLVPNL--TA 102
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSEVPDSLplTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELAT------EVSPDALDPVEV---LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:NF040873 75 RDLVAMGRwarrglWRRLTRDDRAAVddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 488224859 174 GKQVLKLLQNASRQhGNTVLIITHNSALAPIADRVI 209
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-228 |
7.61e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkQLTAYRRTdVGFVFQfyNLVPNLT 101
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL-VGIVFQ--NPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKeNVELATEVSPD--ALDPVEV-------LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:PRK13644 92 GR-TVEEDLAFGPEnlCLPPIEIrkrvdraLAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 173 TGKQVLKLLQNASRQhGNTVLIITHNSALAPIADRVIHINDAKVRsveLNDHPSSI 228
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIV---LEGEPENV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
8.52e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 8.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRY-KMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSD------ 76
Cdd:PRK13631 22 LRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 -------KQLTAYRRTdVGFVFQF--YNLVpnltaKENVELATEVSPDALDPVEV---------LRQVGLAHR-LNNFPS 137
Cdd:PRK13631 102 npyskkiKNFKELRRR-VSMVFQFpeYQLF-----KDTIEKDIMFGPVALGVKKSeakklakfyLNKMGLDDSyLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 138 QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-198 |
1.04e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYrrtdVGFVFQFYn 95
Cdd:PRK11231 13 GTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR----LALLPQHH- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVP-NLTAKENVE--------LATEVSPDALDPVEV-LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:PRK11231 86 LTPeGITVRELVAygrspwlsLWGRLSAEDNARVNQaMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 166 TGALDFETGKQVLKLLQNAsRQHGNTVLIITHN 198
Cdd:PRK11231 166 TTYLDINHQVELMRLMREL-NTQGKTVVTVLHD 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-216 |
1.19e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.99 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTdVGFVFQFYNLVPNLTAK 103
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELA----TEVSPDALDPVEV--LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQV 177
Cdd:PRK11831 103 DNVAYPlrehTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 178 LKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-197 |
3.45e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltayr 83
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVV--DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQFYNLVPNLTAKENVEL------ATEVSPDALDPvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNP 157
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVfgryfgLSAAAARALVP-PLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488224859 158 KLLLCDEPTGALDfetgKQVLKLLQNASRQ---HGNTVLIITH 197
Cdd:PRK13537 158 DVLVLDEPTTGLD----PQARHLMWERLRSllaRGKTILLTTH 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
4.19e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKmgeTTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdKQLT 80
Cdd:PRK13652 1 MHLIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTdVGFVFQ------FYNLVPNLTAKENVELATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA 154
Cdd:PRK13652 75 EVRKF-VGLVFQnpddqiFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 155 KNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRI 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-208 |
5.56e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGM-----DTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQFYNLVP 98
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKENVELATEVSPDALDPVEVLRQVGLA-----------HRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVKSKKELQERVRWAlekaqlwdevkDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 168 ALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRV 208
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAArISDYV 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-208 |
9.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGM-----DTPDEGQIIIDDTDIaqFSDKQLTAYRRTDVGFVFQFYNLVPN 99
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELATEV-----SPDALDP-VE-VLRQVGL----AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK14267 100 LTIYDNVAIGVKLnglvkSKKELDErVEwALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488224859 169 LDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRV 208
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAArVSDYV 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-216 |
1.02e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 98.32 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYK--RYKMG---ETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFSDkq 78
Cdd:PRK15112 5 LEVRNLSKtfRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 79 lTAYRRTDVGFVFQfyNLVPNLTAKENV--------ELATEVSPDALDP--VEVLRQVGL-AHRLNNFPSQLSGGEQQRV 147
Cdd:PRK15112 82 -YSYRSQRIRMIFQ--DPSTSLNPRQRIsqildfplRLNTDLEPEQREKqiIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIIT-HNSALAPIADRVIHINDAKV 216
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
1.25e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqltayr 83
Cdd:COG0488 316 LELEGLSKSY--GDKTLL--DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 rTDVGFVFQFY-NLVPNLTAKENVElatEVSPDAlDPVEVLRQVGlahRLnNFP--------SQLSGGEQQRVSIARALA 154
Cdd:COG0488 378 -VKIGYFDQHQeELDPDKTVLDELR---DGAPGG-TEQEVRGYLG---RF-LFSgddafkpvGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 155 KNPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDrYFLDRVATRILEFEDGGVR 508
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-197 |
1.61e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPD---EGQIIIDDTDIAQFSDKQLTAYrrtdvgfVFQFYNLVPNLT 101
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY-------VQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENV----------ELATEVSPDALDpvEVLRQVGL---AHRLNNFPSQ---LSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:TIGR00955 116 VREHLmfqahlrmprRVTKKEKRERVD--EVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|..
gi 488224859 166 TGALDFETGKQVLKLLQNASrQHGNTVLIITH 197
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLA-QKGKTIICTIH 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-209 |
1.91e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPD---EGQIIIDDTDIAQFSDK 77
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 78 QLTAYRRTDVGFVFQ--FYNLVPNLTAKENV-EL-----------ATEVSPDALDPVEV--LRQvglahRLNNFPSQLSG 141
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpMTSLNPYMRVGEQLmEVlmlhkgmskaeAFEESVRMLDAVKMpeARK-----RMKMYPHEFSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 142 GEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVL 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-215 |
2.58e-24 |
|
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: 94.05 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqltayrrTDVGFVfqfynlvpnltak 103
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------VKIGYF------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 envelatevspdaldpvevlrqvglahrlnnfpSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETgkqvLKLLQN 183
Cdd:cd03221 69 ---------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES----IEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 184 ASRQHGNTVLIITHNSA-LAPIADRVIHINDAK 215
Cdd:cd03221 112 ALKEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-219 |
3.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTAYRRTDVGFVFQF--YNLVP 98
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQFpeYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAK----------ENVELATEVSPDALDPVEVLRQVglahrLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK13645 106 ETIEKdiafgpvnlgENKQEAYKKVPELLKLVQLPEDY-----VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488224859 169 LDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKVRSV 219
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVISI 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-208 |
5.05e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDT------DIAQFSDKQLtayrRTDVGFVFQFYNLVP 98
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL----RKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKENVELATEvSPDALDPVEV-------LRQVGL----AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:PRK14246 104 HLSIYDNIAYPLK-SHGIKEKREIkkiveecLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 168 ALDFETGKQVLKLLQNASRQHgnTVLIITHN-SALAPIADRV 208
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYV 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-220 |
5.81e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.94 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYrrtdVGFvfqfYN 95
Cdd:PRK13539 13 GGRVLFSG--LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LGH----RN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 -LVPNLTAKENVEL-ATEVSPDALDPVEVLRQVGLAHrLNNFPSQ-LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:PRK13539 83 aMKPALTVAENLEFwAAFLGGEELDIAAALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 173 TGKQVLKLLQNASRQhGNTVLIITHNSALAPIAdRVIHINDAKVRSVE 220
Cdd:PRK13539 162 AVALFAELIRAHLAQ-GGIVIAATHIPLGLPGA-RELDLGPFAAEDPA 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
6.19e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKyVEVKNEYKRYKMG-ETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIII---DDTDIAQFSD 76
Cdd:PRK13651 1 MQ-IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 K---------QLTAYR--------RTDVGFVFQF--YNLVpnltaKENVE-------LATEVSP-DALD-PVEVLRQVGL 128
Cdd:PRK13651 80 KekvleklviQKTRFKkikkikeiRRRVGVVFQFaeYQLF-----EQTIEkdiifgpVSMGVSKeEAKKrAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 129 AHR-LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN--SALApIA 205
Cdd:PRK13651 155 DESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDldNVLE-WT 232
|
250
....*....|.
gi 488224859 206 DRVIHINDAKV 216
Cdd:PRK13651 233 KRTIFFKDGKI 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-215 |
6.77e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.23 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMdTPD---EGQIIIDDTDIaQFSDKQLTayRRTDVGFVFQFYNL 96
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL-QASNIRDT--ERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELATEVSP------DA--LDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:PRK13549 94 VKELSVLENIFLGNEITPggimdyDAmyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 169 LDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAK 215
Cdd:PRK13549 174 LTESETAVLLDIIRDL-KAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
8.80e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 97.22 E-value: 8.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTItanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQlt 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVI---KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrRtDVGFVFQFYNLVPNLTAKENVELATEVSpdALDPVEVLRQVGLAHR-------LNNFPSQLSGGEQQRVSIARAL 153
Cdd:PRK11650 76 ---R-DIAMVFQNYALYPHMSVRENMAYGLKIR--GMPKAEIEERVAEAARileleplLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 154 AKNPKLLLCDEPTGALDFETGKQV---LKLLQnasRQHGNTVLIITHNSALA-PIADRVIHINDAKVRSV----ELNDHP 225
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMrleIQRLH---RRLKTTSLYVTHDQVEAmTLADRVVVMNGGVAEQIgtpvEVYEKP 226
|
..
gi 488224859 226 SS 227
Cdd:PRK11650 227 AS 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-202 |
1.57e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKqltAYRRtDVGFVFQFYNLVPNLTAKEN 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VELATEVSPDALDPV---------EVLRQVGL---AHRLNNfpsQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:PRK10575 106 VAIGRYPWHGALGRFgaadrekveEAISLVGLkplAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180
....*....|....*....|....*....
gi 488224859 174 GKQVLKLLQNASRQHGNTVLIITHNSALA 202
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMA 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-224 |
2.96e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayr 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTDVGFVFQ----FYNLVPNLTA--------KENVELATEVSpDALDPVEVLRQvGLAHRLNNFPSQLSGGEQQRVSIAR 151
Cdd:PRK11176 416 RNQVALVSQnvhlFNDTIANNIAyarteqysREQIEEAARMA-YAMDFINKMDN-GLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLQNAsrQHGNTVLIITHNSALAPIADRVIHINDAKVrsVELNDH 224
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEI--VERGTH 562
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-213 |
1.68e-22 |
|
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: 89.91 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIddtdiaqfsdkqltaYRRTDVGFVFQfynlVPNLtak 103
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQ----RPYL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 envelatevspdaldPVEVLRQVgLAHrlnnfPSQ--LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLL 181
Cdd:cd03223 76 ---------------PLGTLREQ-LIY-----PWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180 190
....*....|....*....|....*....|..
gi 488224859 182 qnasRQHGNTVLIITHNSALAPIADRVIHIND 213
Cdd:cd03223 135 ----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
2.38e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.22 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGettITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFSDKQLTAYR 83
Cdd:PRK13636 6 LKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQfynlvpnltAKENVELATEVSPD--------ALDPVEVLRQV-------GLAHrLNNFPSQ-LSGGEQQRV 147
Cdd:PRK13636 82 ES-VGMVFQ---------DPDNQLFSASVYQDvsfgavnlKLPEDEVRKRVdnalkrtGIEH-LKDKPTHcLSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 148 SIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPI-ADRVIHINDAKV 216
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-216 |
2.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDI-AQFSDKQLTAYRRTdVGFVFQFynlvPNL 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKR-IGMVFQF----PES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKE-NVELATEVSPD----ALDPV-----EVLRQVGLAHR-LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PRK13646 97 QLFEdTVEREIIFGPKnfkmNLDEVknyahRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 170 DFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-207 |
3.08e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.09 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayrRTDVGFVFQFYNLVPN 99
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM---REAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELATEVSPDALDPVEVLRQVGLAHRLNNFPSQ----LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGK 175
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 176 QVLKLLQNAsRQHGNTVLIITHNSALA-PIADR 207
Cdd:PRK11614 175 QIFDTIEQL-REQGMTIFLVEQNANQAlKLADR 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-210 |
3.08e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRtDVGFVFQ--FYNLVPN 99
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQdpYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELATEV------SPDALDPVEVLRQVGL----AHRlnnFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PRK10261 418 QTVGDSIMEPLRVhgllpgKAAAARVAWLLERVGLlpehAWR---YPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488224859 170 DFETGKQVLKLLQNASRQHGNTVLIITHNSAlapIADRVIH 210
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMA---VVERISH 532
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-197 |
3.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQF-YNLVPNLTAK 103
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATE---VSPDALDPV--EVLRQVGLAHRL-NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQV 177
Cdd:PRK13643 104 KDVAFGPQnfgIPKEKAEKIaaEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180
....*....|....*....|
gi 488224859 178 LKLLQNAsRQHGNTVLIITH 197
Cdd:PRK13643 184 MQLFESI-HQSGQTVVLVTH 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-216 |
3.81e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 15 MGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayRRtdVGFVFQFY 94
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 95 NLVPNLTAKENVE--------LATEVSPDALDPV-EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:PRK10253 91 TTPGDITVQELVArgryphqpLFTRWRKEDEEAVtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488224859 166 TGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALA-PIADRVIHINDAKV 216
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKI 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-216 |
4.78e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 90.76 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMdTPDEGQIIIDDTDIAQFSDKQLTAYR-----RTDVGF---VFQFYNL- 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVElatevspDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARAL-----AKNP--KLLLCDEPTGAL 169
Cdd:PRK03695 94 QPDKTRTEAVA-------SALN--EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488224859 170 DfeTGKQVL--KLLQNASRQhGNTVLIITH--NSALAPiADRVIHINDAKV 216
Cdd:PRK03695 165 D--VAQQAAldRLLSELCQQ-GIAVVMSSHdlNHTLRH-ADRVWLLKQGKL 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-207 |
5.52e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMD--TPD---EGQIIIDDTDIaqFSDKQLTAYRRTDVGFVFQFYNL 96
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNI--YSPRTDTVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPnLTAKENV----ELATEVSPDALDPV--EVLRQVGL----AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK14239 98 FP-MSIYENVvyglRLKGIKDKQVLDEAveKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 167 GALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADR 207
Cdd:PRK14239 177 SALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASrISDR 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-209 |
9.25e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 9.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKS-TILNIL------GGMDTPDE-------GQIIiddtDI 71
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqaGGLVQCDKmllrrrsRQVI----EL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 72 AQFSDKQLTAYRRTDVGFVFQ--FYNLVPNLTAKENV------------ELATEVSPDALDPVEVLRQVGLahrLNNFPS 137
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIaesirlhqgasrEEAMVEAKRMLDQVRIPEAQTI---LSRYPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 138 QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVI 209
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVL 240
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-208 |
9.38e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.51 E-value: 9.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 19 TITANDDISFSIEKGELVIILGPSGAGKS----TILNIlggmdTPDEGQIIID-----DTDIAQFSDKQLTAYRRTDVGF 89
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGI-----TKDNWHVTADrfrwnGIDLLKLSPRERRKIIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 90 VFQ--FYNLVPNLTAKENVElatEVSPD--------------ALDPVEVLRQVGLA-HR--LNNFPSQLSGGEQQRVSIA 150
Cdd:COG4170 94 IFQepSSCLDPSAKIGDQLI---EAIPSwtfkgkwwqrfkwrKKRAIELLHRVGIKdHKdiMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 151 RALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRV 208
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTI 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-230 |
1.25e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.55 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMdTPD---EGQIIIDDtDIAQFSDkqLTAYRRTDVGFVFQFYNL 96
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDG-EVCRFKD--IRDSEALGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELATEVSPDAL--------DPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:NF040905 90 IPYLSIAENIFLGNERAKRGVidwnetnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 169 LDFETGKQVLKLLQnASRQHGNTVLIITHN-SALAPIADRVIHINDAkvRSVE-LNDHPSSIDE 230
Cdd:NF040905 170 LNEEDSAALLDLLL-ELKAQGITSIIISHKlNEIRRVADSITVLRDG--RTIEtLDCRADEVTE 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-197 |
1.44e-21 |
|
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: 92.69 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 2 KYVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqlta 81
Cdd:TIGR03719 321 KVIEAENLTKAF--GDKLLI--DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 yrrTDVGFVFQFY-NLVPNLTAKEnvelatEVSpDALDPVEV-LRQVGLAHRLNNFP----------SQLSGGEQQRVSI 149
Cdd:TIGR03719 385 ---VKLAYVDQSRdALDPNKTVWE------EIS-GGLDIIKLgKREIPSRAYVGRFNfkgsdqqkkvGQLSGGERNRVHL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISH 498
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-217 |
1.48e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKmgetTITANDDISFSIEKGELVIILGPSGAGKST----ILNILggmdTPDEGQIIIDDTDIaQFSDKQL 79
Cdd:COG4152 2 LELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTtiriILGIL----APDSGEVLWDGEPL-DPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 80 TAY----RRtdvgfvfqfynLVPNLTAKENVE-------LATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVS 148
Cdd:COG4152 73 IGYlpeeRG-----------LYPKMKVGEQLVylarlkgLSKAEAKRRAD--EWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 149 IARALAKNPKLLLCDEPTGALD---FETGKQVLKLLQNAsrqhGNTVLIITHNSALAP-IADRVIHINDAKVR 217
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpvnVELLKDVIRELAAK----GTTVIFSSHQMELVEeLCDRIVIINKGRKV 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-198 |
2.35e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDtpD-------EGQIIIDDTDIAQfSDKQLTAYRRTdVGFVFQFY 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN--DlipgfrvEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 95 NLVPNlTAKENVELATEVSPDALDPVEV----LRQVGL----AHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK14243 101 NPFPK-SIYDNIAYGARINGYKGDMDELversLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|..
gi 488224859 167 GALDFETGKQVLKLLQNASRQHgnTVLIITHN 198
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHN 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-198 |
2.91e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDtdiaqfsdkqltayrRTDVGFVFQFYNLVPN--LTA 102
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQKLYLDTTlpLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEVSPDALDPVevLRQVGLAHrLNNFPSQ-LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLL 181
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPA--LKRVQAGH-LIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170
....*....|....*..
gi 488224859 182 QNASRQHGNTVLIITHN 198
Cdd:PRK09544 164 DQLRRELDCAVLMVSHD 180
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-197 |
7.03e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 86.54 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfsDKQLTAYRRtDVGFVFQFYNLVPNLTAK 103
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALDPVEVLRQVGLAHRLnNFP-SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQ 182
Cdd:PRK13540 93 ENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*
gi 488224859 183 nASRQHGNTVLIITH 197
Cdd:PRK13540 172 -EHRAKGGAVLLTSH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-232 |
9.08e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 2 KYVEVKNEYKRYkmgeTTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFsDKQLTA 81
Cdd:PRK09700 4 PYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 yrRTDVGFVFQFYNLVPNLTAKENVELATEVSPDALD-PV-----------EVLRQVGLAHRLNNFPSQLSGGEQQRVSI 149
Cdd:PRK09700 79 --QLGIGIIYQELSVIDELTVLENLYIGRHLTKKVCGvNIidwremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 150 ARALAKNPKLLLCDEPTGALdfeTGKQV--LKLLQNASRQHGNTVLIITHNSA-LAPIADRVIHIND-AKVRSVELNDhp 225
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAeIRRICDRYTVMKDgSSVCSGMVSD-- 231
|
....*..
gi 488224859 226 SSIDEIV 232
Cdd:PRK09700 232 VSNDDIV 238
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-195 |
9.55e-21 |
|
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: 86.16 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 7 KNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGmDTPD----EGQIIIDDTDIAQFSDKqltaY 82
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGnvsvEGDIHYNGIPYKEFAEK----Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 RRtDVGFVFQFYNLVPNLTAKENVELATEVspdaldpvevlrqvglahRLNNFPSQLSGGEQQRVSIARALAKNPKLLLC 162
Cdd:cd03233 82 PG-EIIYVSEEDVHFPTLTVRETLDFALRC------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 163 DEPTGALDFETGKQVLKLLQNASRQHGNTVLII 195
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-208 |
2.06e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.94 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMdTPDEGQII-----IDDTDIAQFS 75
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrFDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 76 DKQltayRRTDVGfvfqfynlvpnltakENVELATEVSPDALDP--------------------------------VEVL 123
Cdd:PRK15093 80 PRE----RRKLVG---------------HNVSMIFQEPQSCLDPservgrqlmqnipgwtykgrwwqrfgwrkrraIELL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 124 RQVGL-AHR--LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHN-S 199
Cdd:PRK15093 141 HRVGIkDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQ 220
|
....*....
gi 488224859 200 ALAPIADRV 208
Cdd:PRK15093 221 MLSQWADKI 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-209 |
2.34e-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: 85.24 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAyrrtdVGFVFQFYNLVPNLTAKEN 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG-----LLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VEL-----ATEVSPDALDPVEVlrqVGLAHRLNNfpsQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDfetgKQVLKL 180
Cdd:cd03231 94 LRFwhadhSDEQVEEALARVGL---NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALD----KAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 181 LQNASRQH---GNTVLIITHNS-ALAPIADRVI 209
Cdd:cd03231 164 FAEAMAGHcarGGMVVLTTHQDlGLSEAGAREL 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-198 |
5.21e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.47 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPdEGQIIIDDTdiAQFSDKQLTAYR------RTDVGFVFQFYNLVPn 99
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGR--VEFFNQNIYERRvnlnrlRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELATE------------VSPDALDPVEVLRQVglAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:PRK14258 102 MSVYDNVAYGVKivgwrpkleiddIVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 168 ALDFETGKQVLKLLQNASRQHGNTVLIITHN 198
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-211 |
7.55e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMD--TPDEGQIIIDDTDIAqfsdkqltayrrtdvgfvfqfyNLVPNLTA 102
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT----------------------DLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEvspdalDPVEVlRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLq 182
Cdd:cd03217 76 RLGIFLAFQ------YPPEI-PGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI- 147
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 183 NASRQHGNTVLIITHNSALA--PIADRViHI 211
Cdd:cd03217 148 NKLREEGKSVLIITHYQRLLdyIKPDRV-HV 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-209 |
1.07e-19 |
|
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: 84.38 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYKMGETTITANDDisfSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqFSDKQLTAYRRT 85
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 86 DVGfvfqfynlvpnltakenvELATEVSPDALDP----VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLL 161
Cdd:cd03237 77 TVR------------------DLLSSITKDFYTHpyfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488224859 162 CDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVI 209
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDyLADRLI 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-216 |
1.09e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 15 MGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQ---FSDKQLTAYRRTdVGFVF 91
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrsiFNYRDVLEFRRR-VGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 92 QFYNLVPnLTAKENVelATEVSPDALDPVEVLRQVGLAH------------RLNNFPSQLSGGEQQRVSIARALAKNPKL 159
Cdd:PRK14271 108 QRPNPFP-MSIMDNV--LAGVRAHKLVPRKEFRGVAQARltevglwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 160 LLCDEPTGALDFETGKQVLKLLQNASRQHgnTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAArISDRAALFFDGRL 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-223 |
1.10e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 84.75 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKS----TILNILGGMDTPDEGQIIIDDTDIAqfsdkqLTAYRRTDVGFVFQ----FYN 95
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA------PCALRGRKIATIMQnprsAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLT--AKENVeLATEVSPDALDPVEVLRQVGLAHR---LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PRK10418 94 PLHTMHthARETC-LALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 171 FETGKQVLKLLQNASRQHGNTVLIITHN-SALAPIADRVIHINDAKVrsVELND 223
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI--VEQGD 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-197 |
1.12e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFSDKqlTAYRRTDVGFVFQFYNLVPNLT 101
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFAST--TAALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENV--------------------------ELATEVSPDAldPVevlrqvglahrlnnfpSQLSGGEQQRVSIARALAK 155
Cdd:PRK11288 96 VAENLylgqlphkggivnrrllnyeareqleHLGVDIDPDT--PL----------------KYLSIGQRQMVEIAKALAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLqNASRQHGNTVLIITH 197
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVI-RELRAEGRVILYVSH 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-197 |
2.90e-19 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 81.91 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPD--EGQIIIDdtdiaqfsDKQLTAYRRTDVGFVFQFYNLVPNLT 101
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILIN--------GRPLDKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATevspdaldpveVLRQVGLAHRlnnfpsqlsggeqQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLL 181
Cdd:cd03232 96 VREALRFSA-----------LLRGLSVEQR-------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|....*.
gi 488224859 182 QNASRqHGNTVLIITH 197
Cdd:cd03232 152 KKLAD-SGQAILCTIH 166
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-217 |
2.94e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGET------------------TITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQII 65
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 66 IDDTDIAQFsdkqltayrrtDVGFVFQfynlvPNLTAKENVELA---------------------TEVSpDALD-PVevl 123
Cdd:COG1134 85 VNGRVSALL-----------ELGAGFH-----PELTGRENIYLNgrllglsrkeidekfdeivefAELG-DFIDqPV--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 124 rqvglahrlnnfpSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALA 202
Cdd:COG1134 145 -------------KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSmGAVR 210
|
250
....*....|....*
gi 488224859 203 PIADRVIHINDAKVR 217
Cdd:COG1134 211 RLCDRAIWLEKGRLV 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-197 |
3.14e-19 |
|
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: 85.76 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqltayrrTDVGFVFQFYNLVPNLTAK 103
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG---------------IKVGYLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALDPVEVL----------------RQVGL--------AHRLNN----------FP------SQLSGGE 143
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEIsakyaepdadfdklaaEQAELqeiidaadAWDLDSqleiamdalrCPpwdadvTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 144 QQRVSIARALAKNPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-225 |
4.65e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 82.07 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYR 83
Cdd:cd03369 7 IEVENLSVRYAPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdVGFVFQfynlVPNL---TAKENVELATEVSPDaldpvevlrQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLL 160
Cdd:cd03369 82 SS-LTIIPQ----DPTLfsgTIRSNLDPFDEYSDE---------EIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 161 LCDEPTGALDFETGkqvlKLLQNASRQH--GNTVLIITHNsaLAPIA--DRVIHINDAKVRSVelnDHP 225
Cdd:cd03369 148 VLDEATASIDYATD----ALIQKTIREEftNSTILTIAHR--LRTIIdyDKILVMDAGEVKEY---DHP 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-209 |
6.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.22 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 2 KYVEVKNEYKRYKMgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDtdiaqfsdKQLTA 81
Cdd:PRK13642 3 KILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG--------ELLTA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 YR----RTDVGFVFQFY-NLVPNLTAKENVELATEvsPDALDPVEVLRQVG---LAHRLNNF----PSQLSGGEQQRVSI 149
Cdd:PRK13642 74 ENvwnlRRKIGMVFQNPdNQFVGATVEDDVAFGME--NQGIPREEMIKRVDealLAVNMLDFktrePARLSGGQKQRVAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVI 209
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRIL 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-209 |
6.97e-19 |
|
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: 84.84 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 29 SIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiidDTDIaQFSDK-QltaYRRTDVgfvfqfynlvpNLTAKENVE 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KISYKpQ---YISPDY-----------DGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 108 latEVSPDALDP----VEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQN 183
Cdd:COG1245 424 ---SANTDDFGSsyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180
....*....|....*....|....*..
gi 488224859 184 ASRQHGNTVLIITHNSALAP-IADRVI 209
Cdd:COG1245 501 FAENRGKTAMVVDHDIYLIDyISDRLM 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-215 |
1.20e-18 |
|
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: 84.11 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMdTPD---EGQIIIDDTDIAQfsdKQLTAYRRTDVGFVFQFYNL 96
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKA---SNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNLTAKENVELATEVSPDA---------LDPVEVLRQVGLAHRLNNFP-SQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:TIGR02633 90 VPELSVAENIFLGNEITLPGgrmaynamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488224859 167 GALDFETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAK 215
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDL-KAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-216 |
1.93e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMD--TPDEGQIIIDDTDIaqfsdKQLTAYRRTDVG-FV-FQ------- 92
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDI-----LELSPDERARAGiFLaFQypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 93 --FYNLVpnLTAKENVELATEVSPDALDPV-EVLRQVGL----AHR-LN-NFpsqlSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:COG0396 92 vsVSNFL--RTALNARRGEELSAREFLKLLkEKMKELGLdedfLDRyVNeGF----SGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 164 EPTGALDFETGKQVLKLLqNASRQHGNTVLIITHNSAL--APIADRVIHINDAKV 216
Cdd:COG0396 166 ETDSGLDIDALRIVAEGV-NKLRSPDRGILIITHYQRIldYIKPDFVHVLVDGRI 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-216 |
1.96e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSD---KQLTAYrrtdvgFVFQFYNLVPNLTA 102
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIY------LVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEVSPDALDPVE-VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD-FETGKQVLKL 180
Cdd:PRK15439 104 KENILFGLPKRQASMQKMKqLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 488224859 181 lqNASRQHGNTVLIITHN-SALAPIADRVIHINDAKV 216
Cdd:PRK15439 184 --RELLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-213 |
2.01e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 80.45 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITandDISFSIEKGELVIILGPSGAGKSTIL-NILGGMDTPdEGQIIIDDTDIAQFSDKQLTAY 82
Cdd:cd03290 1 VQVTNGYFSWGSGLATLS---NINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNKNESEPSFEATRSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 RRTDVGFVFQFYNLVpNLTAKENVEL--------------ATEVSPDaLDPVEVLRQVGLAHRLNNfpsqLSGGEQQRVS 148
Cdd:cd03290 77 NRYSVAYAAQKPWLL-NATVEENITFgspfnkqrykavtdACSLQPD-IDLLPFGDQTEIGERGIN----LSGGQRQRIC 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGKQ-----VLKLLQNASRqhgnTVLIITHNSALAPIADRVIHIND 213
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHlmqegILKFLQDDKR----TLVLVTHKLQYLPHADWIIAMKD 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-216 |
2.72e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQ--------LTAYRRTDvGfvfqfyn 95
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayVPEDRKGE-G------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLTAKENVELAtevSPDA------LDPVEVLRQV-GLAHRLN-NFPS------QLSGGEQQRVSIARALAKNPKLLL 161
Cdd:COG1129 341 LVLDLSIRENITLA---SLDRlsrgglLDRRRERALAeEYIKRLRiKTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 162 CDEPT-----GAldfetgKQ-VLKLLQNASRQhGNTVLIIThnSALaP----IADRVIHINDAKV 216
Cdd:COG1129 418 LDEPTrgidvGA------KAeIYRLIRELAAE-GKAVIVIS--SEL-PellgLSDRILVMREGRI 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-197 |
4.00e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.47 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 2 KYVEVKNEYKRYkmGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfsdkqlta 81
Cdd:PRK11819 323 KVIEAENLSKSF--GDRLLI--DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET------------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 82 yrrTDVGFVFQFY-NLVPNLTAKEnvelatEVSpDALDPVEVlrqvglahrlNNF--PS-------------------QL 139
Cdd:PRK11819 387 ---VKLAYVDQSRdALDPNKTVWE------EIS-GGLDIIKV----------GNReiPSrayvgrfnfkggdqqkkvgVL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 140 SGGEQQRVSIARALAKNPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISH 500
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-197 |
4.37e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.62 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 33 GELVIILGPSGAGKSTILNILGGMDTPD--EGQIIIDDTDIAqfsdKQLTayRRTdvGFVFQFYNLVPNLTAKENVELAT 110
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQIL--KRT--GFVTQDDILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 111 EVS-PDALDPVE-------VLRQVGLAHRLN-----NFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQV 177
Cdd:PLN03211 166 LLRlPKSLTKQEkilvaesVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|
gi 488224859 178 LKLLQNASrQHGNTVLIITH 197
Cdd:PLN03211 246 VLTLGSLA-QKGKTIVTSMH 264
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-197 |
8.34e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 21 TANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQI-----IIDDTDIAqfsdkqltAYRRtdVGFVFQFYN 95
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA--------TRRR--VGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLTAKENVEL-------ATEVSPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGA 168
Cdd:NF033858 350 LYGELTVRQNLELharlfhlPAAEIAARVA--EMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190
....*....|....*....|....*....|....*
gi 488224859 169 LD------FetgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:NF033858 428 VDpvardmF------WRLLIELSREDGVTIFISTH 456
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-214 |
1.11e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDdtdiaqfSDKQLTAYRRTDVGFVFQFYNLVPNLTAKEN 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID-------GKTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VELATEVS---PDALdPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFEtGKQVLKLLQ 182
Cdd:PRK13543 103 LHFLCGLHgrrAKQM-PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMI 180
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 183 NASRQHGNTVLIITHNS-ALAPIADRVIHINDA 214
Cdd:PRK13543 181 SAHLRGGGAALVTTHGAyAAPPVRTRMLTLEAA 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-213 |
1.31e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayRRTDVGFV---FQFYNLVPNL 100
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRLGVAYIpedRLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELATEVSPDA-----LDPVEVLRqvgLAHRL-----------NNFPSQLSGGEQQRVSIARALAKNPKLLLCDE 164
Cdd:COG3845 352 SVAENLILGRYRRPPFsrggfLDRKAIRA---FAEELieefdvrtpgpDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488224859 165 PTGALDFETGKQVLKLLQNAsRQHGNTVLIIthnSA-----LApIADRVIHIND 213
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLEL-RDAGAAVLLI---SEdldeiLA-LSDRIAVMYE 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-209 |
1.32e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.01 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 30 IEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiidDTDIaQFSDK-QltaYRRTDvgfvfqfynlvPNLTAKENVEL 108
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL-KISYKpQ---YIKPD-----------YDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 109 ATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQH 188
Cdd:PRK13409 424 ITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|..
gi 488224859 189 GNTVLIITHNSALAP-IADRVI 209
Cdd:PRK13409 504 EATALVVDHDIYMIDyISDRLM 525
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-217 |
2.91e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.57 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 19 TITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFsdkqltayrrtDVGFVFQfynlvP 98
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLGGGFN-----P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKENVEL-ATE--VSPDALDPVEVlRQVGLAhRLNNF---P-SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDF 171
Cdd:cd03220 98 ELTGRENIYLnGRLlgLSRKEIDEKID-EIIEFS-ELGDFidlPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488224859 172 ETGKQVLKLLQNAsRQHGNTVLIITHN-SALAPIADRVIHINDAKVR 217
Cdd:cd03220 176 AFQEKCQRRLREL-LKQGKTVILVSHDpSSIKRLCDRALVLEKGKIR 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-197 |
3.18e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.78 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQiiiddtdiAQFSDkqltAYRrtdVGFVFQFYNLVPNLTAK 103
Cdd:PRK11819 24 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAP----GIK---VGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELA-----------TEVS-----P------------------DALDPVEVLRQVGLAH---RLnnfP------SQLS 140
Cdd:PRK11819 89 ENVEEGvaevkaaldrfNEIYaayaePdadfdalaaeqgelqeiiDAADAWDLDSQLEIAMdalRC---PpwdakvTKLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 141 GGEQQRVSIARALAKNPKLLLCDEPTGALDFETgkqVLKLLQNASRQHGnTVLIITH 197
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTH 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-216 |
6.02e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfsDKQLTAYRRTdVGFVFQFYNLVPNLT 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS-LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEVSPDALDPVEV-----LRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLemeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488224859 177 VLKLLqnASRQHGNTVLIITHNSALAPI-ADRVIHINDAKV 216
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-211 |
2.22e-16 |
|
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: 77.52 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 31 EKGELVIILGPSGAGKSTILNILGGMDTPDEGqIIIDDTDIaqfsDKQLTAYRRTDVGFVF--------------QFYNL 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLG-DYDEEPSW----DEVLKRFRGTELQDYFkklangeikvahkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNL---TAKENVELATEvsPDALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:COG1245 172 IPKVfkgTVRELLEKVDE--RGKLD--ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 174 GKQVLKLLQNASRQhGNTVLIITHNSA-LAPIADrVIHI 211
Cdd:COG1245 248 RLNVARLIRELAEE-GKYVLVVEHDLAiLDYLAD-YVHI 284
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-186 |
2.34e-16 |
|
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: 76.05 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiiddtdiaQFSDKqltayrrtdVGFVFQFYNLVPNlTAKE 104
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------KHSGR---------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELAteVSPDALDPVEVLRQVGLAHRLNNFPSQ-----------LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:cd03291 117 NIIFG--VSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170
....*....|....*...
gi 488224859 174 GKQVL-----KLLQNASR 186
Cdd:cd03291 195 EKEIFescvcKLMANKTR 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-229 |
3.50e-16 |
|
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: 77.29 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILN-ILGGMDTPdEGQIIIddtdiaqfsdkqltayrRTDVGFVFQfYNLVPNLTAKE 104
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHM-----------------KGSVAYVPQ-QAWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATEVSPDALDpvEVLRQVGLAHRLNNFPS-----------QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:TIGR00957 718 NILFGKALNEKYYQ--QVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 174 GKQVLK-------LLQNASRqhgntvLIITHNSALAPIADRVIHINDAKVRsvELNDHPSSID 229
Cdd:TIGR00957 796 GKHIFEhvigpegVLKNKTR------ILVTHGISYLPQVDVIIVMSGGKIS--EMGSYQELLQ 850
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-216 |
3.72e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGmDTPD---------EGQIIIDDTDIAQFSDKQLTAYR-----RTDVGF 89
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGggaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 90 VFQFYNLV-----PNL-----TAKENVELATEV----SPDALDPVEVlrqvglahrlnnfpSQLSGGEQQRVSIARALAK 155
Cdd:PRK13547 97 AFSAREIVllgryPHArragaLTHRDGEIAWQAlalaGATALVGRDV--------------TTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 156 ---------NPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNTVLIITHNSALAP-IADRVIHINDAKV 216
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAI 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-197 |
3.76e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 1 MKYVEVKNEYKRYKMgETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDT----------- 69
Cdd:PTZ00265 380 IKKIQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkww 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 70 ---------DIAQFSDK-----QLTAYRRTDVGFVFQFYN--------------------------LVPNLTAKENVELA 109
Cdd:PTZ00265 459 rskigvvsqDPLLFSNSiknniKYSLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 110 TEVSP-DALDPVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQV 177
Cdd:PTZ00265 539 KNYQTiKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|
gi 488224859 178 LKLLQNASRQHGNTVLIITH 197
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAH 638
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-197 |
3.95e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQfynlVPNLTAK- 103
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQ----DPVVLADt 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 --ENVELATEVSPDALdpVEVLRQVGLAHRLNNFP-----------SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PRK10790 431 flANVTLGRDISEEQV--WQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180
....*....|....*....|....*..
gi 488224859 171 FETGKQVLKLLQnASRQHgNTVLIITH 197
Cdd:PRK10790 509 SGTEQAIQQALA-AVREH-TTLVVIAH 533
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-186 |
7.08e-16 |
|
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: 76.49 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiiddtdiaQFSDKqltayrrtdVGFVFQFYNLVPNlTAKE 104
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------KHSGR---------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELAteVSPDALDPVEVLRQVGLAHRLNNFPSQ-----------LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFET 173
Cdd:TIGR01271 506 NIIFG--LSYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170
....*....|....*...
gi 488224859 174 GKQVL-----KLLQNASR 186
Cdd:TIGR01271 584 EKEIFesclcKLMSNKTR 601
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-211 |
7.41e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 30 IEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTdiaqfSDKQLTAYRRTDVGFVF--------------QFYN 95
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS-----WDEVLKRFRGTELQNYFkklyngeikvvhkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNL---TAKENVELATEVSpdALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:PRK13409 171 LIPKVfkgKVRELLKKVDERG--KLD--EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 173 TGKQVLKLLQNASRqhGNTVLIITHNSA-LAPIADrVIHI 211
Cdd:PRK13409 247 QRLNVARLIRELAE--GKYVLVVEHDLAvLDYLAD-NVHI 283
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-173 |
9.38e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 22 ANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqFSDKQltAYRRTDVGFVFQFYNLVPNLT 101
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPK--SSQEAGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATE-VSP-------------DALdpvevLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:PRK10762 96 IAENIFLGREfVNRfgridwkkmyaeaDKL-----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
....*..
gi 488224859 168 AL-DFET 173
Cdd:PRK10762 171 ALtDTET 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-211 |
1.23e-15 |
|
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: 73.55 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 33 GELVIILGPSGAGKSTILNILGGMDTPDEGQIiiddtDIAQFSDKQLTAYRRTDVGFVF--------------QFYNLVP 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-----DDPPDWDEILDEFRGSELQNYFtkllegdvkvivkpQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NlTAKENV-ELATEVSP-DALDpvEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:cd03236 101 K-AVKGKVgELLKKKDErGKLD--ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 488224859 177 VLKLLQNASrQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:cd03236 178 AARLIRELA-EDDNYVLVVEHDLAVLDYLSDYIHC 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-217 |
1.67e-15 |
|
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: 75.37 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITAndDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFS----DKQL 79
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLR--HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 80 TAYRRTDVGFVFQF-YNLVP-NLTAKENVELATEVS---------PDALDpvevlrqvglaHRLNNFPSQLSGGEQQRVS 148
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLrMNLDPfSQYSDEEVWWALELAhlktfvsalPDKLD-----------HECAEGGENLSVGQRQLVC 1431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFETGkqvlKLLQNASRQHGN--TVLIITHNsaLAPIAD--RVIHINDAKVR 217
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETD----NLIQSTIRTQFEdcTVLTIAHR--LNTIMDytRVIVLDKGEVA 1498
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-211 |
3.85e-15 |
|
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: 70.81 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNilGGMDTPDEGQIIiddtdiaqfsdKQLTAYRRTDVGFVFQFYNLVpnltake 104
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLI-----------SFLPKFSRNKLIFIDQLQFLI------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 nvelatevspdaldpvevlrQVGLAH-RLNNFPSQLSGGEQQRVSIARALAKNPK--LLLCDEPTGALDFETGKQVLKLL 181
Cdd:cd03238 73 --------------------DVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190
....*....|....*....|....*....|
gi 488224859 182 qNASRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:cd03238 133 -KGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-173 |
4.70e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDdtdiaqfsdKQLTAYR------RTDVGFVFQF---- 93
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE---------QDLIVARlqqdppRNVEGTVYDFvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 ----------YNLVPNLTAKE----NVELATEVSpDALDPV----------EVLRQVGL-AHRLnnfPSQLSGGEQQRVS 148
Cdd:PRK11147 91 ieeqaeylkrYHDISHLVETDpsekNLNELAKLQ-EQLDHHnlwqlenrinEVLAQLGLdPDAA---LSSLSGGWLRKAA 166
|
170 180
....*....|....*....|....*
gi 488224859 149 IARALAKNPKLLLCDEPTGALDFET 173
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-217 |
5.19e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTAYRRTdVGFVFQFYNLVPNLTAKEN 105
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKL-FSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VELATEVSPDALDPVEVLRQVGLA-HRLNNFpsQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNA 184
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLELEdGRISNL--KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPL 495
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 185 SRQHGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:PRK10522 496 LQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-217 |
1.21e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILN-ILGGMDTPDEGQIIIddtdiaqfsdkqltayrRTDVGFVFQFyNLVPNLTAK 103
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-----------------RGTVAYVPQV-SWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALDpvEVLRQVGLAHRLNNFPS-----------QLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:PLN03130 697 DNILFGSPFDPERYE--RAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488224859 173 TGKQVL-KLLQNASRqhGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:PLN03130 775 VGRQVFdKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-213 |
1.72e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYkMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILG----------------------------- 54
Cdd:PTZ00265 1166 IEIMDVNFRY-ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 55 ------GMDTPDE-------------------GQIIIDDTDIAQFSDKQLtayrRTDVGFVFQfYNLVPNLTAKENVELA 109
Cdd:PTZ00265 1245 deeqnvGMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDL----RNLFSIVSQ-EPMLFNMSIYENIKFG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 110 TEvspDAL--DPVEVLRQVGLAHRLNNFPSQ-----------LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQ 176
Cdd:PTZ00265 1320 KE---DATreDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*..
gi 488224859 177 VLKLLQNASRQHGNTVLIITHNSALAPIADRVIHIND 213
Cdd:PTZ00265 1397 IEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-198 |
2.13e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 21 TANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQFYNLVPNL 100
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TA----------KENVELATEVSPDALDPVEVL----RQVGlahrlnnfpsQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK15056 101 VMmgryghmgwlRRAKKRDRQIVTAALARVDMVefrhRQIG----------ELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|..
gi 488224859 167 GALDFETGKQVLKLLQNAsRQHGNTVLIITHN 198
Cdd:PRK15056 171 TGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-194 |
2.58e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 30 IEKGELVIILGPSGAGKSTILNILG----GMDTPDEGQIIIDDTDIAQFSdKQLTAyrrtDVGFVFQFYNLVPNLTAKEN 105
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIK-KHYRG----DVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 106 VELATEVSPDALDPVEVLRQV-------------GLAHRL-----NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTG 167
Cdd:TIGR00956 159 LDFAARCKTPQNRPDGVSREEyakhiadvymatyGLSHTRntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180
....*....|....*....|....*..
gi 488224859 168 ALDFETGKQVLKLLQNASRQHGNTVLI 194
Cdd:TIGR00956 239 GLDSATALEFIRALKTSANILDTTPLV 265
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-211 |
2.70e-14 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 69.21 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTIL---------------------NILGGMDTPD----EG---QIIIDDTDIAQFSd 76
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsiEGlspAIAIDQKTTSRNP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 77 kqltayrRTDVGFVFQFYNLVPNLTAKENVElatevspdalDPVEVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARALAK 155
Cdd:cd03270 92 -------RSTVGTVTEIYDYLRLLFARVGIR----------ERLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 156 NPK--LLLCDEPTGALDFETGKQVLKLLQNAsRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:cd03270 155 GLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-225 |
2.78e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 71.37 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaqfSDKQLTAYRRTdvgF--VFQFYNLVPNLtak 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQL---FsaVFSDFHLFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 enVELATEVSPDALDpvEVLRQVGLAHRL----NNFPS-QLSGGEQQRVSIARALAKNPKLLLCDE------PTgaldFe 172
Cdd:COG4615 422 --LGLDGEADPARAR--ELLERLELDHKVsvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE----F- 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 173 tgKQV--LKLLQnASRQHGNTVLIITHNSALAPIADRVIHINDAKVRSVELNDHP 225
Cdd:COG4615 493 --RRVfyTELLP-ELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-231 |
3.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltayrRTDVGFVF-----QFYNLVPN 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENV-ELATEVSPDALDPVEVLRQVGLAHR-LN---NFPSQ----LSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PRK15439 356 APLAWNVcALTHNRRGFWIKPARENAVLERYRRaLNikfNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488224859 171 FETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVrSVELNDHPSSIDEI 231
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI-SGALTGAAINVDTI 495
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-217 |
3.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRY--KMGETTITandDISFSIEKGELVIILGPSGAGKSTILN-ILGGMDTPDEGQIIIddtdiaqfsdkqlt 80
Cdd:PLN03232 615 ISIKNGYFSWdsKTSKPTLS---DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 ayrRTDVGFVFQFyNLVPNLTAKENVELATEVSPD----ALDpvevlrQVGLAHRLNNFPSQ-----------LSGGEQQ 145
Cdd:PLN03232 678 ---RGSVAYVPQV-SWIFNATVRENILFGSDFESErywrAID------VTALQHDLDLLPGRdlteigergvnISGGQKQ 747
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 146 RVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALAPIADRVIHINDAKVR 217
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-233 |
4.40e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 17 ETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFsdkQLTAYRRTdvgfvFQFYNL 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-----LAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPNL---TAKENVELAtevSPDALDpvevlRQVGLAHRLNN-------FPS-----------QLSGGEQQRVSIARALAK 155
Cdd:PRK10789 397 TPFLfsdTVANNIALG---RPDATQ-----QEIEHVARLASvhddilrLPQgydtevgergvMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 156 NPKLLLCDEPTGALDFETGKQVLKLLqnasRQ--HGNTVLIITHN-SALAPiADRVIHINDAKVrsVELNDHPSSIDEIV 232
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNL----RQwgEGRTVIISAHRlSALTE-ASEILVMQHGHI--AQRGNHDQLAQQSG 541
|
.
gi 488224859 233 W 233
Cdd:PRK10789 542 W 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-232 |
5.95e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNeYKRYKMGETtitanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSD----KQLT 80
Cdd:PRK09700 267 EVRN-VTSRDRKKV-----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AY---RRTDVGFVfqfynlvPNLTAKENVELATEVSPDAL-------DPVEVLR-----QVGLA---HRLNNFPSQLSGG 142
Cdd:PRK09700 341 AYiteSRRDNGFF-------PNFSIAQNMAISRSLKDGGYkgamglfHEVDEQRtaenqRELLAlkcHSVNQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 143 EQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN-SALAPIADRVIHINDAKVRSVEL 221
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRLTQILT 492
|
250
....*....|.
gi 488224859 222 NDHPSSIDEIV 232
Cdd:PRK09700 493 NRDDMSEEEIM 503
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-197 |
8.28e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQ----F-----YNL 96
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQapvlFsgtvrFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 VPnLTAKENVELATEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGkq 176
Cdd:PLN03130 1334 DP-FNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD-- 1410
|
170 180
....*....|....*....|...
gi 488224859 177 vlKLLQNASRQH--GNTVLIITH 197
Cdd:PLN03130 1411 --ALIQKTIREEfkSCTMLIIAH 1431
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-216 |
9.50e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIiddtdiAQFSdkqlTAYrrtdvgfvfqfynlVP------ 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------AERS----IAY--------------VPqqawim 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 NLTAKENVELATEVSPDAL-DPVEV------LRQV--GLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLaDAVRVsqleadLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488224859 170 DFETGKQVLK--LLqnaSRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PTZ00243 814 DAHVGERVVEecFL---GALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-216 |
2.00e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSdkqLTAYRRtdvgfVFQFYNLVPNL---TA 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR-----VLSIIPQSPVLfsgTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELATEVSpDAlDPVEVLRQVGLAHRLNNFPSQL-----------SGGEQQRVSIARALAKNPKLLLCDEPTGALDF 171
Cdd:PLN03232 1327 RFNIDPFSEHN-DA-DLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488224859 172 ETGKQVLKLLQNASRQhgNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PLN03232 1405 RTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-223 |
2.11e-13 |
|
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: 68.70 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKS-TILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVFQFYNLVPNLTA 102
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 103 KENVELAT-------EVSPDALDPVEVLRQVGLAHRLNNFP----SQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDF 171
Cdd:TIGR02633 357 GKNITLSVlksfcfkMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488224859 172 ETGKQVLKLLqNASRQHGNTVLIIThnSALAP---IADRVIHINDAKVRSVELND 223
Cdd:TIGR02633 437 GAKYEIYKLI-NQLAQEGVAIIVVS--SELAEvlgLSDRVLVIGEGKLKGDFVNH 488
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-214 |
2.85e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 38 ILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIaQFSDKQLTAYRRtDVGFVFQ------FYNLVP--------NLTAK 103
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQ-QVATVFQdpeqqiFYTDIDsdiafslrNLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENvELATEVSpDALDPVEvlrqvglAHRLNNFPSQ-LSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQ 182
Cdd:PRK13638 110 EA-EITRRVD-EALTLVD-------AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR 180
|
170 180 190
....*....|....*....|....*....|..
gi 488224859 183 NASRQhGNTVLIITHNsalapiADRVIHINDA 214
Cdd:PRK13638 181 RIVAQ-GNHVIISSHD------IDLIYEISDA 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-196 |
5.02e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAY--------RRTDvgfvfqfyN 95
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgivyisedRKRD--------G 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 96 LVPNLTAKENVELA--TEVSPDA--LDPVEVLRQVGLAHRLNNF--PSQ------LSGGEQQRVSIARALAKNPKLLLCD 163
Cdd:PRK10762 341 LVLGMSVKENMSLTalRYFSRAGgsLKHADEQQAVSDFIRLFNIktPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 164 EPTGALDFETGKQVLKLLqNASRQHGNTVLIIT 196
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVS 452
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-197 |
8.52e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 3 YVEVKNEYKRYKMGETTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTpdeGQIIIDDTDIAQFSDKQLTAY 82
Cdd:PLN03140 876 FVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQETFA 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 83 RRTdvGFVFQFYNLVPNLTAKENV------ELATEVSPDA----LDPV-EVLRQVGLAHRLNNFP--SQLSGGEQQRVSI 149
Cdd:PLN03140 953 RIS--GYCEQNDIHSPQVTVRESLiysaflRLPKEVSKEEkmmfVDEVmELVELDNLKDAIVGLPgvTGLSTEQRKRLTI 1030
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488224859 150 ARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNaSRQHGNTVLIITH 197
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIH 1077
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-220 |
1.26e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 65.65 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMdTPDEGQIIIDDTDIAQFSdkqLTAYR 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLEN--ISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 84 RTdvgfvfqfYNLVPnltakENVELATEVSPDALDPVE---------VLRQVGLAHRLNNFPSQ-----------LSGGE 143
Cdd:cd03289 77 KA--------FGVIP-----QKVFIFSGTFRKNLDPYGkwsdeeiwkVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 144 QQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRqhGNTVLIITHNsaLAPIAD--RVIHINDAKVRSVE 220
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHR--IEAMLEcqRFLVIEENKVRQYD 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-211 |
2.13e-12 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 62.76 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSieKGELVIILGPSGAGKSTILNILGgmdtpdegqiiiddtdiaqfsdkqltayrrtdVGFVFQFYNLVPNLTAKE 104
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 105 NVELATevspdaldpVEVLRQVGLahrlnnfpSQLSGGEQQRVSIARALAKNPK----LLLCDEPTGALDFETGKQVLKL 180
Cdd:cd03227 61 GCIVAA---------VSAELIFTR--------LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 181 LqNASRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:cd03227 124 I-LEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-209 |
2.54e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 64.56 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILN-IL---------GGMDTPDEGQ-----------IIIDDTDIAQ---------- 73
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdTLypalarrlhLKKEQPGNHDrieglehidkvIVIDQSPIGRtprsnpatyt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 74 --FSD-KQL-------TAYRRTDVGFVFQFYNL--VPNLTAKENVELATEVsPDALDPVEVLRQVGLAH-RLNNFPSQLS 140
Cdd:cd03271 93 gvFDEiRELfcevckgKRYNRETLEVRYKGKSIadVLDMTVEEALEFFENI-PKIARKLQTLCDVGLGYiKLGQPATTLS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 141 GGEQQRVSIARALAK---NPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHNSALAPIADRVI 209
Cdd:cd03271 172 GGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHNLDVIKCADWII 242
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-209 |
2.58e-12 |
|
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: 62.97 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 30 IEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAqfsdkqltayrrtdvgfvfqfynlvpnltakenvela 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 110 teVSPDALDpvevlrqvglahrlnnfpsqLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHG 189
Cdd:cd03222 65 --YKPQYID--------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|.
gi 488224859 190 NTVLIITHNSALAP-IADRVI 209
Cdd:cd03222 123 KTALVVEHDLAVLDyLSDRIH 143
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-211 |
3.04e-12 |
|
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: 62.39 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 32 KGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDiaqfsdkqltayrrtdvgfvfqfynlvpnltakenvelate 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 112 vspdalDPVEVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKL-----LQNASR 186
Cdd:smart00382 40 ------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKS 113
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 187 QHGNTVLIITHNS------ALAPIADRVIHI 211
Cdd:smart00382 114 EKNLTVILTTNDEkdlgpaLLRRRFDRRIVL 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-197 |
9.17e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 33 GELVIILGPSGAGKSTILNILGGMDTpdeGQIIIDDTDIAQFSDKQLTAYRRTdvGFVFQFYNLVPNLTAKENVELAT-- 110
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPLDSSFQRSI--GYVQQQDLHLPTSTVRESLRFSAyl 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 111 ----EVSP----DALDPV-EVLRQVGLAHRLNNFPSQ-LSGGEQQRVSIARALAKNPKLLL-CDEPTGALDFETGKQVLK 179
Cdd:TIGR00956 864 rqpkSVSKsekmEYVEEViKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*...
gi 488224859 180 LLQNASrQHGNTVLIITH 197
Cdd:TIGR00956 944 LMRKLA-DHGQAILCTIH 960
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-209 |
2.00e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 63.11 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 121 EVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARALAK---NPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIIT 196
Cdd:TIGR00630 811 QTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIE 889
|
90
....*....|...
gi 488224859 197 HNSALAPIADRVI 209
Cdd:TIGR00630 890 HNLDVIKTADYII 902
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-197 |
3.00e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRykMGETTITANddISFSIEKGELVIILGPSGAGKSTILNILGGMdtPD----EGQIIIDDTDIAqfsdkQLT 80
Cdd:CHL00131 9 EIKNLHAS--VNENEILKG--LNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESIL-----DLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRTDVG--FVFQFYNLVPNLTAKENVELA-----TEVSPDALDPVEV-------LRQVGL-AHRLN-NFPSQLSGGEQ 144
Cdd:CHL00131 78 PEERAHLGifLAFQYPIEIPGVSNADFLRLAynskrKFQGLPELDPLEFleiinekLKLVGMdPSFLSrNVNEGFSGGEK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488224859 145 QRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITH 197
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-184 |
4.84e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 6 VKNEYKRYKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTpDEGQIIIDDTdiaQFSDKQLTAYRRT 85
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVL--QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGV---SWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 86 dvgfvfqfYNLVPnltakENVELATEVSPDALDPVE---------VLRQVGLAHRLNNFPSQ-----------LSGGEQQ 145
Cdd:TIGR01271 1294 --------FGVIP-----QKVFIFSGTFRKNLDPYEqwsdeeiwkVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190
....*....|....*....|....*....|....*....
gi 488224859 146 RVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNA 184
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS 1399
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-197 |
1.20e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 13 YKMGETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIII-DDTDIAQFsDKqltaYRRtdvgfvf 91
Cdd:PRK11147 327 YQIDGKQLV--KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVAYF-DQ----HRA------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 92 qfyNLVPNLTAKENV-ELATEV------------------SPD-ALDPVEVLrqvglahrlnnfpsqlSGGEQQRVSIAR 151
Cdd:PRK11147 393 ---ELDPEKTVMDNLaEGKQEVmvngrprhvlgylqdflfHPKrAMTPVKAL----------------SGGERNRLLLAR 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-224 |
1.42e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKS-TILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAY--------RRTDvgfvfqfy 94
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQgiamvpedRKRD-------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 95 NLVPNLTAKENVELAtevspdaldpveVLRQVGLAHRLNNFPSQ-----------------------LSGGEQQRVSIAR 151
Cdd:PRK13549 351 GIVPVMGVGKNITLA------------ALDRFTGGSRIDDAAELktilesiqrlkvktaspelaiarLSGGNQQKAVLAK 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488224859 152 ALAKNPKLLLCDEPTGALDFETGKQVLKLLqNASRQHGNTVLIIThnSALAP---IADRVIHINDAKVRSVELNDH 224
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAIIVIS--SELPEvlgLSDRVLVMHEGKLKGDLINHN 491
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-166 |
1.80e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 12 RYkmGETTitANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQfsdkqlTAYRRT---DVG 88
Cdd:NF033858 10 RY--GKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARHRRAvcpRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 89 FVFQFY--NLVPNLTAKENVEL--------ATE--VSPDALdpvevLRQVGLAhrlnNFPS----QLSGGEQQRVSIARA 152
Cdd:NF033858 80 YMPQGLgkNLYPTLSVFENLDFfgrlfgqdAAErrRRIDEL-----LRATGLA----PFADrpagKLSGGMKQKLGLCCA 150
|
170
....*....|....
gi 488224859 153 LAKNPKLLLCDEPT 166
Cdd:NF033858 151 LIHDPDLLILDEPT 164
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-198 |
2.98e-10 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 59.65 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 121 EVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARALAK---NPKLLLCDEPTGALDFETGKQVLKLLQnASRQHGNTVLIIT 196
Cdd:COG0178 808 QTLQDVGLGYiKLGQPATTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLH-RLVDKGNTVVVIE 886
|
..
gi 488224859 197 HN 198
Cdd:COG0178 887 HN 888
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-216 |
5.93e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiiddtdiaQFSDKQLTAYRRTDVGFVFQfynlvPNLTAK 103
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENANIGYYAQDHAYDFE-----NDLTLF 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 104 ENVELATEVSPDALdpveVLRqvGLAHRL-------NNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETgkq 176
Cdd:PRK15064 403 DWMSQWRQEGDDEQ----AVR--GTLGRLlfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES--- 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 177 vLKLLQNASRQHGNTVLIITHN----SALapiADRVIHINDAKV 216
Cdd:PRK15064 474 -IESLNMALEKYEGTLIFVSHDrefvSSL---ATRIIEITPDGV 513
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-201 |
1.24e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.84 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDI-----SFSIEKGELVIILGPSGAGKSTILNILGGM--------DTPDEG------------------QII--- 65
Cdd:TIGR00954 460 VTPNGDVlieslSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGklfyvpqrpymtlgtlrdQIIypd 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 66 -IDDTDIAQFSDKQLTAYRrtdvgfvfqfynlvpnltakENVELATEVSpdaldpvevlRQVGLAhRLNNFPSQLSGGEQ 144
Cdd:TIGR00954 540 sSEDMKRRGLSDKDLEQIL--------------------DNVQLTHILE----------REGGWS-AVQDWMDVLSGGEK 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 145 QRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNAsrqhGNTVLIITHNSAL 201
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSHRKSL 641
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-211 |
1.29e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.92 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 114 PDALDPVEVLRQVGLAHRLNNFP-SQLSGGEQQRVSIARAL---AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhG 189
Cdd:PRK00635 784 PSIHEKIHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-G 862
|
90 100
....*....|....*....|..
gi 488224859 190 NTVLIITHNSALAPIADRVIHI 211
Cdd:PRK00635 863 HTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
23-218 |
1.35e-09 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 56.12 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 23 NDDISFS-IEKGELVIILGPSGAGKSTILN----ILGGmDTPDEGQIIIDDTDIAqfsdkqlTAYRRTDVGFVFQFYNL- 96
Cdd:cd03279 17 EQVIDFTgLDNNGLFLICGPTGAGKSTILDaityALYG-KTPRYGRQENLRSVFA-------PGEDTAEVSFTFQLGGKk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 97 -----VPNLTAKENVELAtevspdaldpveVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALA----------KNPKLLL 161
Cdd:cd03279 89 yrverSRGLDYDQFTRIV------------LLPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlqnrggARLEALF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 162 CDEPTGALDfETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKVRS 218
Cdd:cd03279 157 IDEGFGTLD-PEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPGGS 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-198 |
2.19e-09 |
|
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: 57.33 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 18 TTITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGqiiidDTDIAQFSDKQLTAYRRTDVGFVFQFYNLV 97
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAGKSILTNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 PNLTAKENVELATEVSPDALDPVE-----VLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:TIGR01257 2025 DLLTGREHLYLYARLRGVPAEEIEkvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180
....*....|....*....|....*.
gi 488224859 173 TGKQVLKLLQNASRQhGNTVLIITHN 198
Cdd:TIGR01257 2105 ARRMLWNTIVSIIRE-GRAVVLTSHS 2129
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
121-198 |
2.32e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 57.00 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 121 EVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARALAKNPK---LLLCDEPTGALDFETGKQVLKLLQnASRQHGNTVLIIT 196
Cdd:PRK00349 812 QTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLH-RLVDKGNTVVVIE 890
|
..
gi 488224859 197 HN 198
Cdd:PRK00349 891 HN 892
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-198 |
8.01e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 5 EVKNEYKRYKMGETTITANDdISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDT----DIAQFSDKQLT 80
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNN-ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 81 AYRRtdvgfvFQFYNLVPNLTaKENVElatEVSPDALDPVEVlrqvglAHRLNNFPSQLSGGEQQRVSIARALAKNPKLL 160
Cdd:PRK13545 102 GIEN------IELKGLMMGLT-KEKIK---EIIPEIIEFADI------GKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 488224859 161 LCDEPTGALDFETGKQVLKLLqNASRQHGNTVLIITHN 198
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKM-NEFKEQGKTIFFISHS 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-216 |
2.54e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQ--------LTAYRRTDVGFVF---QF 93
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTGIYAYldiGF 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 94 YNLVPNLTA-KENVEL--ATEVSPDALDPVEVLRQVGLAHRLNnfPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PRK10982 346 NSLISNIRNyKNKVGLldNSRMKSDTQWVIDSMRVKTPGHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488224859 171 FETGKQVLKLLQNASRQHGNTVLIITHNSALAPIADRVIHINDAKV 216
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-211 |
2.93e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYRRTDVGFVF----QFYNLVPN 99
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdrEYRQLEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTA--KENVELATEVSPDALDPVEVL----RQVGLAHRLNNFPSQL-------SGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK10636 98 LHDanERNDGHAIATIHGKLDAIDAWtirsRAASLLHGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488224859 167 GALDFETGKQVLKLLQNasrqHGNTVLIITHN-SALAPIADRVIHI 211
Cdd:PRK10636 178 NHLDLDAVIWLEKWLKS----YQGTLILISHDrDFLDPIVDKIIHI 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-232 |
8.32e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 20 ITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTayrRTDVGFVFQFYNLVPN 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL---ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELA-----------------TEVSPDALDpVEVLRQVGLAhrlnnfpsQLSGGEQQRVSIARALAKNPKLLLC 162
Cdd:PRK10982 88 RSVMDNMWLGryptkgmfvdqdkmyrdTKAIFDELD-IDIDPRAKVA--------TLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488224859 163 DEPTGALdfeTGKQVLKLLQ--NASRQHGNTVLIITHN-SALAPIADRVIHINDAK-VRSVELNDhpSSIDEIV 232
Cdd:PRK10982 159 DEPTSSL---TEKEVNHLFTiiRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQwIATQPLAG--LTMDKII 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-213 |
1.40e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 24 DDISFSIEKGELVIILGPSGAGKSTILNILGGmDTPD--------------EGQIIID-DTDIAQFSDKQLTAYR-RTDV 87
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGETIWDiKKHIGYVSSSLHLDYRvSTSV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 88 ------GFvFQ---FYNLVPNLTAKenveLATEVspdaldpvevLRQVGLAHRLNNFPSQ-LSGGEQQRVSIARALAKNP 157
Cdd:PRK10938 356 rnvilsGF-FDsigIYQAVSDRQQK----LAQQW----------LDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488224859 158 KLLLCDEPTGALDfETGKQVLKLLQNASRQHGNT-VLIITHNSALAP--IADRVIHIND 213
Cdd:PRK10938 421 TLLILDEPLQGLD-PLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPacITHRLEFVPD 478
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-197 |
6.30e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayRRtdvgfvfQFyNLVP------N 99
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RR-------QF-SMIPqdpvlfD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 LTAKENVELATEVSPD----ALDPVEVLRQV-----GLAHRLNNFPSQLSGGEQQRVSIARALAK-NPKLLLCDEPTGAL 169
Cdd:PTZ00243 1398 GTVRQNVDPFLEASSAevwaALELVGLRERVaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANI 1477
|
170 180
....*....|....*....|....*...
gi 488224859 170 DFETGKQVLKLLQNASRQHgnTVLIITH 197
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFSAY--TVITIAH 1503
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-208 |
8.24e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 27 SFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLTAYrrtdVGFVFQFYN---LVPN---- 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL----VSDEWQRNNtdmLSPGeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 100 -LTAKENVELATEvspdalDPV---EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGK 175
Cdd:PRK10938 99 gRTTAEIIQDEVK------DPArceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190
....*....|....*....|....*....|...
gi 488224859 176 QVLKLLQNASRQHGNTVLIITHNSALAPIADRV 208
Cdd:PRK10938 173 QLAELLASLHQSGITLVLVLNRFDEIPDFVQFA 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-211 |
1.57e-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: 47.22 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 23 NDDISFsieKGELVIILGPSGAGKSTILN----ILGGmDTPDEGQIIIDDTDIAQfsdkqlTAYRRTDVGFVFQfynlvp 98
Cdd:cd03240 15 RSEIEF---FSPLTLIVGQNGAGKTTIIEalkyALTG-ELPPNSKGGAHDPKLIR------EGEVRAQVKLAFE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 99 nLTAKENVELatEVSPDALDPVEVLRQVGLAHRLNNFPSQLSGGEQQ------RVSIARALAKNPKLLLCDEPTGALDFE 172
Cdd:cd03240 79 -NANGKKYTI--TRSLAILENVIFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488224859 173 TGKQVL-KLLQNASRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:cd03240 156 NIEESLaEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-197 |
2.19e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 40 GPSGAGKSTILNILGGMDTPDEGQIIIDDTD-IAQFSDKQltayrrtdvgFVFQFYNLV--------------------- 97
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDPNErLGKLRQDQ----------FAFEEFTVLdtvimghtelwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 98 --PNLTAKENVELAT-EVSPDALDPV-------EVLRQVGLAHRLNNFP-SQLSGGEQQRVSIARALAKNPKLLLCDEPT 166
Cdd:PRK15064 104 alPEMSEEDGMKVADlEVKFAEMDGYtaearagELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190
....*....|....*....|....*....|.
gi 488224859 167 GALDFETgkqvLKLLQNASRQHGNTVLIITH 197
Cdd:PRK15064 184 NNLDINT----IRWLEDVLNERNSTMIIISH 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-211 |
2.82e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488224859 139 LSGGEQQRVSIARALAKNPK--LLLCDEPTGAL---DFETGKQVLKLLqnasRQHGNTVLIITHNSALAPIADRVIHI 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLhpqDTHKLINVIKKL----RDQGNTVLLVEHDEQMISLADRIIDI 550
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-209 |
3.92e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 26 ISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQltAYRRtdvGFVF-----QFYNLVPNL 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAKENVELATE--VSPDA--LDPVevlRQVGLAHR----LN-NFPS------QLSGGEQQRVSIARALAKNPKLLLCDEP 165
Cdd:PRK11288 347 SVADNINISARrhHLRAGclINNR---WEAENADRfirsLNiKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488224859 166 TGALDFETGKQVLKLLQNASRQhGNTVLIIThnSALAP---IADRVI 209
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFVS--SDLPEvlgVADRIV 467
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
4-198 |
9.09e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 4 VEVKNEYKRYKMGET----------------TITANDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIiid 67
Cdd:PRK13546 5 VNIKNVTKEYRIYRTnkermkdalipkhknkTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 68 dtdiaqfsdkqltaYRRTDVGFVFQFYNLVPNLTAKENVELA------TEVSPDALDPvEVLRQVGLAHRLNNFPSQLSG 141
Cdd:PRK13546 82 --------------DRNGEVSVIAISAGLSGQLTGIENIEFKmlcmgfKRKEIKAMTP-KIIEFSELGEFIYQPVKKYSS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 142 GEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITHN 198
Cdd:PRK13546 147 GMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHN 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-201 |
2.50e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 25 DISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIID-DTDIAQFSDKQLTAY--RRTDVGFVFQFYNLVPNLT 101
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSaKVRMAVFSQHHVDGLdlSSNPLLYMMRCFPGVPEQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 102 AKENVELATEVSPDALDPVEVLrqvglahrlnnfpsqlSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETgkqVLKLL 181
Cdd:PLN03073 607 LRAHLGSFGVTGNLALQPMYTL----------------SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALI 667
|
170 180
....*....|....*....|
gi 488224859 182 QNASRQHGNtVLIITHNSAL 201
Cdd:PLN03073 668 QGLVLFQGG-VLMVSHDEHL 686
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
139-219 |
3.39e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 139 LSGGEQQ------RVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGN--TVLIITHNSALAPIADRVIH 210
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDipQVIMISHHRELLSVADVAYE 881
|
....*....
gi 488224859 211 INDAKVRSV 219
Cdd:PRK01156 882 VKKSSGSSK 890
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-221 |
3.95e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 139 LSGGEQQ------RVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQHGNtVLIITHNSALAPIADRVIHIN 212
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQ-VIIVSHDEELKDAADYVIRVS 867
|
90
....*....|...
gi 488224859 213 ----DAKVRSVEL 221
Cdd:PRK03918 868 leggVSKVEVVSL 880
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-172 |
4.31e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 16 GETTITanDDISFSIEKGELVIILGPSGAGKSTILNILGGMDTPDEGQI-IIDDTDIAQFSDKQLTaYRRTDVGFVFQFY 94
Cdd:PRK10636 323 GDRIIL--DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE-FLRADESPLQHLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 95 NLVPNLTAKEnvelatevspdaldpvevLRQV--GLAHR---LNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGAL 169
Cdd:PRK10636 400 RLAPQELEQK------------------LRDYlgGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
...
gi 488224859 170 DFE 172
Cdd:PRK10636 462 DLD 464
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-211 |
4.42e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 119 PVEVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARAL---AKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLI 194
Cdd:PRK00635 1679 PLQALIDNGLGYlPLGQNLSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSL-GHSVIY 1757
|
90
....*....|....*..
gi 488224859 195 ITHNSALAPIADRVIHI 211
Cdd:PRK00635 1758 IDHDPALLKQADYLIEM 1774
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-214 |
5.02e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.36 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 30 IEKGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDDTDIAQFSDKQLtayrRTDVGFVFQ---------FYNLVPNL 100
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQdpilfsgsiRFNLDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 101 TAK-----ENVELA-----TEVSPDALDPVevlrqvgLAHRLNNFpsqlSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:cd03288 120 KCTddrlwEALEIAqlknmVKSLPGGLDAV-------VTEGGENF----SVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488224859 171 FETGKQVLKLLQNASRQHgnTVLIITHnsalapiadRVIHINDA 214
Cdd:cd03288 189 MATENILQKVVMTAFADR--TVVTIAH---------RVSTILDA 221
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-198 |
6.60e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 35 LVIILGPSGAGKSTILN----ILGG---MDTPDEGQIIIDDTDIA------QFSDKQLTAYRR----------------- 84
Cdd:COG0419 25 LNLIVGPNGAGKSTILEairyALYGkarSRSKLRSDLINVGSEEAsvelefEHGGKRYRIERRqgefaefleakpserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 85 -----TDVGFVFQFYNLVPNLTAKENVELAtevspdALDPVEVLRQVGLAhRLNNF--PSQLSGGEQQRVSIARALAknp 157
Cdd:COG0419 105 alkrlLGLEIYEELKERLKELEEALESALE------ELAELQKLKQEILA-QLSGLdpIETLSGGERLRLALADLLS--- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488224859 158 klLLCDepTGALDFETGKQVLKLLQNASrqhgntvlIITHN 198
Cdd:COG0419 175 --LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
66-211 |
3.23e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 66 IDDTDIAQFSDKQLTayrrtDVGFVFQFYNLVPnltakENVELATEVSPDALDPVEVLRQVGLAH-RLNNFPSQLSGGEQ 144
Cdd:TIGR00630 425 VGGKSIADVSELSIR-----EAHEFFNQLTLTP-----EEKKIAEEVLKEIRERLGFLIDVGLDYlSLSRAAGTLSGGEA 494
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488224859 145 QRVSIARALAKNPK--LLLCDEPTGAL---DFETGKQVLKLLQNAsrqhGNTVLIITHNSALAPIADRVIHI 211
Cdd:TIGR00630 495 QRIRLATQIGSGLTgvLYVLDEPSIGLhqrDNRRLINTLKRLRDL----GNTLIVVEHDEDTIRAADYVIDI 562
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-197 |
3.95e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 3.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 121 EVLRQVGLAHRLNNFPSQLSGGEQQRVSIARALAKNPKLLLCDEPTGALDFETGKQVLKLLQNASRQhGNTVLIITH 197
Cdd:NF000106 127 ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQ 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-170 |
4.22e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.22e-04
10 20 30
....*....|....*....|....*....|...
gi 488224859 138 QLSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-63 |
7.04e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 7.04e-04
10 20 30
....*....|....*....|....*....|..
gi 488224859 32 KGELVIILGPSGAGKSTILNILggmdTPDEGQ 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNAL----LPELVL 111
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
32-53 |
9.55e-04 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 38.90 E-value: 9.55e-04
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
32-53 |
2.06e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 38.15 E-value: 2.06e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-211 |
2.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 136 PSQLSGGEQQ------RVSIARALAKN-------PKLLLcDEPTGALDFETGKQVLKLLQNAsRQHG-NTVLIITHNSAL 201
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESM-RRLGvEQIVVVSHDDEL 856
|
90
....*....|
gi 488224859 202 APIADRVIHI 211
Cdd:PRK02224 857 VGAADDLVRV 866
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
24-84 |
2.48e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488224859 24 DDISFSIEKGeLVIILGPSGAGKSTILN----ILGGM--DTPDEGQIIIDDTDIAQFSDKQLTAYRR 84
Cdd:pfam13476 10 RDQTIDFSKG-LTLITGPNGSGKTTILDaiklALYGKtsRLKRKSGGGFVKGDIRIGLEGKGKAYVE 75
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
32-68 |
2.78e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|....*..
gi 488224859 32 KGELVIILGPSGAGKSTILNILGGMDTPDEGQIIIDD 68
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDD 230
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
35-53 |
3.67e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.36 E-value: 3.67e-03
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-57 |
4.01e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 4.01e-03
10 20
....*....|....*....|....*..
gi 488224859 32 KGELVIILGPSGAGKSTILN-ILGGMD 57
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELD 131
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-170 |
4.32e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 4.32e-03
10 20 30
....*....|....*....|....*....|..
gi 488224859 139 LSGGEQQRVSIARALAKNPKLLLCDEPTGALD 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK05416 |
PRK05416 |
RNase adapter RapZ; |
34-53 |
4.94e-03 |
|
RNase adapter RapZ;
Pssm-ID: 235450 Cd Length: 288 Bit Score: 37.39 E-value: 4.94e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-211 |
7.41e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488224859 115 DALDPVEVLRQVGLAH-RLNNFPSQLSGGEQQRVSIARALAKNPK--LLLCDEPTGALDFETGKQVLKLLQNASRQHgNT 191
Cdd:PRK00635 1363 DLLNRLTFIDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNN-NT 1441
|
90 100
....*....|....*....|
gi 488224859 192 VLIITHNSALAPIADRVIHI 211
Cdd:PRK00635 1442 VIATDRSGSLAEHADHLIHL 1461
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
35-76 |
7.63e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 37.33 E-value: 7.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488224859 35 LVIILGPSGAGKSTILNIL-----GGMDTPDEGQIIIDDTDIAQFSD 76
Cdd:TIGR00606 30 LTILVGPNGAGKTTIIECLkyictGDFPPGTKGNTFVHDPKVAQETD 76
|
|
| |
