|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
3.67e-123 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 348.19 E-value: 3.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 ME-ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFRRRNIGLIYQFYNLIPVLNVKENILLPAELDN--RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSDEV 224
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-219 |
1.85e-107 |
|
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: 308.26 E-value: 1.85e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAEL--DNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLagVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-223 |
1.85e-82 |
|
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: 245.42 E-value: 1.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSI 162
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 163 ILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSDE 223
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-223 |
7.48e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 235.72 E-value: 7.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLP---AELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINR 159
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPlrvTGKSRKEIR-RRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLklsvKKYNQ---TLIMITHDKN-MALQADRIISIEDGIIKSDE 223
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELL----EEINRrgtTVLIATHDLElVDRMPKRVLELEDGRLVRDE 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-220 |
1.28e-71 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 217.22 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDID--GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKeaKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-218 |
8.66e-68 |
|
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: 207.49 E-value: 8.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLPAELDNRDID--GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEReiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGI 218
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLK-RLNKRGTTVIVATHDLSLVDRvAHRVIILDDGR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-217 |
2.35e-66 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 204.91 E-value: 2.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENIL----------------LPAEldnrDIDGEYfdDLMETLGLIDREKHLPNQLSGGQ 146
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNVLagrlgrtstwrsllglFPPE----DRERAL--EALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-224 |
1.51e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 203.39 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINR 159
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIagvPKAEIR-KRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG-IIKSDEV 224
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGrIVEQGPV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
1.99e-64 |
|
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: 198.90 E-value: 1.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlaifR 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLP---AELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGlklRGVPKAEIR-ARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
9.94e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 201.48 E-value: 9.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdla 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifRRRNIGLIYQFYNLIPVLNVKENILLPaeLDNRDIDGEY----FDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG3842 75 --EKRNVGMVFQDYALFPHLTVAENVAFG--LRMRGVPKAEirarVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN--MALqADRIISIEDGII 219
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLAL-ADRIAVMNDGRI 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
1.13e-63 |
|
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: 196.92 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNlktkdlaifR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELqgvPKAEAR-ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 161 SIILADEPTGNLDSKnSKEIL--ELLKLsVKKYNQTLIMITHDKNMALQ-ADRII 212
Cdd:cd03293 151 DVLLLDEPFSALDAL-TREQLqeELLDI-WRETGKTVLLVTHDIDEAVFlADRVV 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-212 |
3.21e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 197.23 E-value: 3.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLktkdlaif 82
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPVLNVKENILLPAELD--NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:COG1116 79 -GPDRGVVFQEPALLPWLTVLDNVALGLELRgvPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 161 SIILADEPTGNLDSKnSKEIL--ELLKLsVKKYNQTLIMITHDKNMALQ-ADRII 212
Cdd:COG1116 158 EVLLMDEPFGALDAL-TRERLqdELLRL-WQETGKTVLFVTHDVDEAVFlADRVV 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-217 |
1.07e-62 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 194.55 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPaeLDNRDIDG----EYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALIN 158
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALP--LKYRGVAKkeriERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLK-YINQKGTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
2.70e-62 |
|
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: 193.88 E-value: 2.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIf 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQ--FYNLIPVLNVKENILLPAE----LDNRDIDGEYFDDLMETLGL-IDREKHLPNQLSGGQQQRTSIGRA 155
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRihgkLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-224 |
3.46e-61 |
|
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: 191.26 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLPAELDN--RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG-IIKSDEV 224
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGeVVEEGTV 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-222 |
4.37e-61 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 201.88 E-value: 4.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPA-----ELDNRDidgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAvyaglERKQRL---LRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILH-QLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-219 |
2.62e-60 |
|
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: 189.32 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQFYNLIPVLNVKENILLPAeLDNR-----------DIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSI 152
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGR-LGRRstwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-219 |
3.63e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 192.21 E-value: 3.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDla 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrRNIGLIYQFYNLIPVLNVKENILLPaeLDNRDIDGEYFD----DLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG3839 75 ----RNIAMVFQSYALYPHMTVYENIAFP--LKLRKVPKAEIDrrvrEAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 157 INRPSIILADEPTGNLDSKnSKE--ILELLKLsVKKYNQTLIMITHDKN--MALqADRIISIEDGII 219
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAK-LRVemRAEIKRL-HRRLGTTTIYVTHDQVeaMTL-ADRIAVMNDGRI 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-219 |
2.63e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 186.74 E-value: 2.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIyNLKTKDLAIF 82
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLP---------AELDNRDIDgeyfddLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLApikvkkmskAEAEERAME------LLERVGLADKADAYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMR-DLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-217 |
3.43e-59 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 186.17 E-value: 3.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAELD--NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGkkKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-219 |
3.86e-59 |
|
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: 185.30 E-value: 3.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRRn 86
Cdd:cd03292 4 INVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 87 IGLIYQFYNLIPVLNVKENILLPAELDN---RDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGvppREIR-KRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 164 LADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNM-ALQADRIISIEDGII 219
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-219 |
1.59e-57 |
|
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: 182.31 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlaifR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFY--NLIPVLNVKENILLPAELDNRDIDGEYFDDLMETLGL----IDRekhLPNQLSGGQQQRTSIGRALI 157
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLppsfLDR---YPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDGII 219
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAvVAHLCDRVAVMQNGRI 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-217 |
2.90e-57 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 181.13 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAEL--DNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-220 |
3.89e-57 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 180.60 E-value: 3.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRrNIGLIYQFYNLIPVLNVKENILLPAELD---NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINR 159
Cdd:TIGR02982 81 RR-RIGYIFQAHNLLGFLTARQNVQMALELQpnlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-217 |
4.75e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 188.57 E-value: 4.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYG-KNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAI 81
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 FRRRnIGLIYQ--FYNLIPVLNVKENILLPAELdNRDIDGEYFDD----LMETLGL----IDRekhLPNQLSGGQQQRTS 151
Cdd:COG1123 340 LRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRL-HGLLSRAERRErvaeLLERVGLppdlADR---YPHELSGGQRQRVA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
4.60e-56 |
|
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: 176.22 E-value: 4.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifR 83
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPaeldnrdidgeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
7.58e-56 |
|
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: 176.89 E-value: 7.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrR 84
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQ-----FYNlipvLNVKENILLPAE---LDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:cd03225 75 RKVGLVFQnpddqFFG----PTVEEEVAFGLEnlgLPEEEIE-ERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-219 |
1.86e-55 |
|
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: 175.80 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIfr 83
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLP---------AELDNRDIDgeyfddLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLApikvkgmskAEAEERALE------LLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMK-DLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-219 |
3.23e-55 |
|
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: 176.32 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLP----AELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALIN 158
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFPlrehTDLSEAEIR-ELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-222 |
3.89e-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: 3.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYN--LI-PvlNVKENI--------LLPAELDNRdidgeyFDDLMETLGLIDREKHLPNQLSGGQQQRTSI 152
Cdd:COG1122 74 RRKVGLVFQNPDdqLFaP--TVEEDVafgpenlgLPREEIRER------VEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVAD 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
5.97e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 178.80 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIY-NLKTkdl 79
Cdd:COG1118 1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 aifRRRNIGLIYQFYNLIPVLNVKENI---LLPAELDNRDIDGEYfDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG1118 73 ---RERRVGFVFQHYALFPHMTVAENIafgLRVRPPSKAEIRARV-EELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRI 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-225 |
2.25e-54 |
|
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: 174.46 E-value: 2.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAif 82
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrRNIGLIYQFYNLIPVLNVKENILL-----------PAELDNRDIdgeyfDDLMETLGLID-REKHLpNQLSGGQQQRT 150
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryphlglfgrPSAEDREAV-----EEALERTGLEHlADRPV-DELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII----KSDEVM 225
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIvaqgPPEEVL 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-224 |
2.89e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 176.92 E-value: 2.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFrR 84
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQFYNLIPVLNVKENILLPAELDNR---DIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTpkaEIK-ARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknMALQ---ADRIISIEDG-IIKSDEV 224
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE--MDVVkriCDRVAVIDAGrLVEQGTV 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-214 |
4.29e-54 |
|
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: 172.41 E-value: 4.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRR 85
Cdd:TIGR03608 1 LKNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFYNLIPVLNVKENILLPAELDNRDIdGEYFDDLMETL---GLIDREKHLPNQLSGGQQQRTSIGRALINRPSI 162
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSK-KEKREKKKEALekvGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489524673 163 ILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHDKNMALQADRIISI 214
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLL-LELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-219 |
4.47e-54 |
|
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: 173.25 E-value: 4.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYF----DDLMETLGLIDR----EKHL--PNQLSGGQQQRTSI 152
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGrfseEDKERALSALERvglaDKAYqrADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEI 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
6.29e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 6.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLtkSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLktkDLAIFR 83
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQfynlIPVL---NVKENILLPAELDNRDIDGEYFDDLMETLGL----IDREkhlPNQLSGGQQQRTSIGRAL 156
Cdd:COG4619 74 RQ-VAYVPQ----EPALwggTVRDNLPFPFQLRERKFDRERALELLERLGLppdiLDKP---VERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-219 |
9.44e-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: 9.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlaifR 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRDID--GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTmSDRIAVMNKGKI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-219 |
1.89e-53 |
|
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: 171.53 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFR 83
Cdd:cd03261 1 IELRGLTKSFG--GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLMETL---GLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLeavGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-219 |
1.51e-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: 168.59 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlaifr 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rRNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03301 72 -RDIAMVFQNYALYPHMTVYDNIAFGLKLrkvPKDEID-ERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
3.42e-51 |
|
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: 163.71 E-value: 3.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFynliPVL---NVKENIllpaeldnrdidgeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRP 160
Cdd:cd03228 75 RKNIAYVPQD----PFLfsgTIRENI-----------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 161 SIILADEPTGNLDSKNSKEILE-LLKLSVKKynqTLIMITHDKNMALQADRIISIEDG 217
Cdd:cd03228 116 PILILDEATSALDPETEALILEaLRALAKGK---TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-219 |
3.97e-51 |
|
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: 169.06 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdla 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT----ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQFYNLIPVLNVKENI---LLPAELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:TIGR03265 75 ---KRDYGIVFQSYALFPNLTVADNIaygLKNRGMGRAEVA-ERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 158 NRPSIILADEPTGNLDSKnSKEIL--ELLKLSvKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDAR-VREHLrtEIRQLQ-RRLGVTTIMVTHDQEEALSmADRIVVMNHGVI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-219 |
5.95e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.24 E-value: 5.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLAIFR 83
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQFYNLIPVLNVKENILLPAEL--DNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:COG1131 73 RR-IGYVPQEPALYPDLTVRENLRFFARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHdkNMA---LQADRIISIEDGII 219
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTH--YLEeaeRLCDRVAIIDKGRI 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-212 |
4.52e-49 |
|
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: 162.92 E-value: 4.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRP---TSGKVYINDVDIYNLKTKDL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFRRRNIGLIYQ--FYNLIPVLNVKENILLPAELdNRDIDG----EYFDDLMETLGLIDREKHL---PNQLSGGQQQRT 150
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRI-HGGLSKaearERAIELLERVGLPDPERRLdryPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRII 212
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-219 |
7.52e-49 |
|
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: 160.89 E-value: 7.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETK--------------------VDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGK 63
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 64 VYINDVDIYNLKTKDLAIFRRRNIGLIYQFYNLIPVLNVKENILLPAELD--NRDIDGEYFDDLMETLGLIDREKHLPNQ 141
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQgvPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 142 LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEIL-ELLKLsVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQdELLRL-QAELQKTIVFITHDLDEALRlGDRIAIMKDGRL 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
8.02e-49 |
|
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: 157.98 E-value: 8.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifrr 84
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQfynlipvlnvkenillpaeldnrdidgeyfddLMETLGLID-REKHLpNQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03214 73 RKIAYVPQ--------------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-219 |
1.01e-48 |
|
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: 169.24 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYNlipvlNVKENILlpaeLDNRDIDgeyFDDLMETL---GLIDREKHLPN-----------QLSGG 145
Cdd:COG2274 548 RRQIGVVLQdvflFSG-----TIRENIT----LGDPDAT---DEEIIEAArlaGLHDFIEALPMgydtvvgeggsNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 146 QQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
1.19e-48 |
|
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: 158.88 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGG-----VDRPTSGKVYINDVDIYNLKTKD 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIfrRRNIGLIYQFYNLIPvLNVKENILLPAELdNRDIDGEYFDDLMETL----GLIDREK-HL-PNQLSGGQQQRTSI 152
Cdd:cd03260 77 LEL--RRRVGMVFQKPNPFP-GSIYDNVAYGLRL-HGIKLKEELDERVEEAlrkaALWDEVKdRLhALGLSGGQQQRLCL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYnqTLIMITHdkNMAlQADRI 211
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTH--NMQ-QAARV 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-219 |
3.26e-48 |
|
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: 166.09 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFynliPVL---NVKENILLPaeldNRDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQR 149
Cdd:COG4988 410 RRQIAWVPQN----PYLfagTIRENLRLG----RPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILE-LLKLSVkkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQaLRRLAK---GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-219 |
5.63e-48 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 157.65 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlaifRRR 85
Cdd:TIGR00968 3 IANISKRFGSFQ----ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA------RDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFYNLIPVLNVKENILLPAELDNRD--IDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:TIGR00968 73 KIGFVFQHYALFKHLTVRDNIAFGLEIRKHPkaKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
1.73e-47 |
|
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: 163.15 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 ME-ILRVENLTKSYGKNEtkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPT---SGKVYINDVDIYNLKT 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDlaifRRRNIGLIYQ--FYNLIPVlNVKENILLPAELDN--RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSI 152
Cdd:COG1123 79 AL----RGRRIGMVFQdpMTQLNPV-TVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
3.54e-47 |
|
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: 155.57 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdla 80
Cdd:cd03296 1 MSI-EVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifRRRNIGLIYQFYNLIPVLNVKENILL------PAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:cd03296 72 --QERNVGFVFQHYALFRHMTVFDNVAFglrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-219 |
4.51e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.91 E-value: 4.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGknetkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIFR 83
Cdd:COG3840 2 LRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQFYNLIPVLNVKENILL-------PAELDNRDIdgeyfDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG3840 71 RP-VSMLFQENNLFPHLTVAQNIGLglrpglkLTAEQRAQV-----EQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 157 I-NRPsIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG3840 145 VrKRP-ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRI 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
1.92e-46 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 154.92 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKN---ETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKK--ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRRnIGLIYQF--YNLIPvLNVKENI--------LLPAELDNRDIDgeyfddLMETLGLiDRE--KHLPNQLSGGQQQ 148
Cdd:TIGR04521 79 DLRKK-VGLVFQFpeHQLFE-ETVYKDIafgpknlgLSEEEAEERVKE------ALELVGL-DEEylERSPFELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD-KNMALQADRIISIEDGIIKSD 222
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
2.74e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.32 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNlktkdla 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifRRRNIGLIYQFYNL---IPVlNVKENILL-----------PAELDNRDIDgeyfdDLMETLGLIDREKHLPNQLSGGQ 146
Cdd:COG1121 73 --ARRRIGYVPQRAEVdwdFPI-TVRDVVLMgrygrrglfrrPSRADREAVD-----EALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII---KSD 222
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREGKTILVVTHDLGAVREyFDRVLLLNRGLVahgPPE 223
|
...
gi 489524673 223 EVM 225
Cdd:COG1121 224 EVL 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-219 |
1.77e-45 |
|
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: 158.78 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYNlipvlNVKENILLpAELDNRDidgeyfDDLMETL---GLIDREKHLPN-----------QLSGG 145
Cdd:COG4987 408 RRRIAVVPQrphlFDT-----TLRENLRL-ARPDATD------EELWAALervGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 146 QQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
2.26e-45 |
|
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: 151.81 E-value: 2.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGknETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKT-KDLaif 82
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIY-----QFYNLIpvlnVK-------ENILLPAELDNRDIdgeyfDDLMETLGLIDREKHLPNQLSGGQQQRT 150
Cdd:TIGR04520 76 -RKKVGMVFqnpdnQFVGAT----VEddvafglENLGVPREEMRKRV-----DEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-219 |
3.16e-45 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 152.55 E-value: 3.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrR 84
Cdd:COG1125 3 EFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDgEYFDDLMETLGLiDREKHL---PNQLSGGQQQRTSIGRALIN 158
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVPRLlgwDKERIR-ARVDELLELVGL-DPEEYRdryPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 159 RPSIILADEPTGNLDSKNSKEI-LELLKLSvKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLqDELLRLQ-RELGKTIVFVTHDIDEALKlGDRIAVMREGRI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-217 |
5.30e-45 |
|
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: 149.79 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifr 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENIL--LPAELDNRDIDGEYFDDLMETLG---LIDREkhlPNQLSGGQQQRTSIGRALIN 158
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIAEMLGidhLLNRK---PETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-219 |
3.36e-44 |
|
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: 146.00 E-value: 3.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifR 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENIllpaeldnrdidgeyfddlmetlglidrekhlpnQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 164 LADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-212 |
7.60e-44 |
|
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: 146.81 E-value: 7.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDG------------EYFDDLMETLGLIDREKHLPNQLSGGQQQRTS 151
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLlararreerearERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRII 212
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSlADRVT 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-222 |
8.42e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.87 E-value: 8.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaif 82
Cdd:PRK09452 14 LVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPVLNVKENI---LLPAELDNRDIDGEYFDDL-METL-GLIDREkhlPNQLSGGQQQRTSIGRALI 157
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVafgLRMQKTPAAEITPRVMEALrMVQLeEFAQRK---PHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMAL-QADRIISIEDGIIKSD 222
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALtMSDRIVVMRDGRIEQD 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-216 |
8.56e-44 |
|
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: 145.70 E-value: 8.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIFR 83
Cdd:COG4133 3 LEAENLSCRRG--ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKnMALQADRIISIED 216
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQP-LELAAARVLDLGD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-220 |
8.80e-44 |
|
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: 146.93 E-value: 8.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifR 83
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAEL--DNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELygLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHD-KNMALQADRIISIEDGIIK 220
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-217 |
3.59e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 145.02 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY--GKNetkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:PRK10908 1 MIRFEHVSKAYlgGRQ-----ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 iFRRRNIGLIYQFYNLIPVLNVKENILLPAEldnrdIDGEYFDDL-------METLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK10908 76 -FLRRQIGMIFQDHHLLMDRTVYDNVAIPLI-----IAGASGDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNM-ALQADRIISIEDG 217
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFE-EFNRVGVTVLMATHDIGLiSRRSYRMLTLSDG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-219 |
5.97e-43 |
|
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: 144.75 E-value: 5.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENI-LLPAEL--DNRDIDgEYFDDLMETLGLIDRE--KHLPNQLSGGQQQRTSIGRALIN 158
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIaLVPKLLkwPKEKIR-ERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEI 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
2.37e-42 |
|
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: 140.46 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLAIFRR 84
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----AKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQfynlipvlnvkenillpaeldnrdidgeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRPSIIL 164
Cdd:cd00267 73 RRIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 165 ADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKNMALQA-DRIISIEDG 217
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-222 |
3.34e-42 |
|
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: 142.05 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 32 KGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVdIYNLKTKDLAI-FRRRNIGLIYQFYNLIPVLNVKENILLPA 110
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINLpPQQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 111 ELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKK 190
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|...
gi 489524673 191 YNQTLIMITHD-KNMALQADRIISIEDGIIKSD 222
Cdd:cd03297 181 LNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
3.11e-41 |
|
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: 137.39 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLAIFRRRNIGLIYQFYNLIPVLNV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL----TDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 103 KENILLPAELD--NRDIDGEYFDDLMETLGLIDREKHL----PNQLSGGQQQRTSIGRALINRPSIILADEPT 169
Cdd:pfam00005 77 RENLRLGLLLKglSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-219 |
1.31e-40 |
|
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: 138.05 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiynlktKDLAIFRR 84
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RnIGLIYQFYNL-----IPVLNVKENILLPAELDNRDIDGEYFDDLMETL---GLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:cd03235 69 R-IGYVPQRRSIdrdfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALervGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-217 |
2.28e-40 |
|
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: 136.19 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDLAIFR 83
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI---SQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQfynlipvlnvkenillpaeldnrdiDGEYFDD-LMEtlglidrekhlpNQLSGGQQQRTSIGRALINRPSI 162
Cdd:cd03246 76 DH-VGYLPQ-------------------------DDELFSGsIAE------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 163 ILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-212 |
2.68e-40 |
|
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: 138.25 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:COG0411 2 DPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQFYNLIPVLNVKENILLPAEL-DNRDIDGEYF----------------DDLMETLGLIDREKHLPNQLS 143
Cdd:COG0411 78 ---RLGIARTFQNPRLFPELTVLENVLVAAHArLGRGLLAALLrlprarreereareraEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN--MALqADRII 212
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDlvMGL-ADRIV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-217 |
6.68e-40 |
|
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: 136.41 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRD-----IDG--EYFDDLMEtlglidREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAkrkarLERvyELFPRLKE------RRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIR-ELRDEGVTILLVEQNARFALEiADRAYVLERG 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-222 |
1.05e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 136.38 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKSYGKneTKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIfrRRNI 87
Cdd:PRK09493 6 NVSKHFGP--TQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI--RQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 88 GLIYQFYNLIPVLNVKENILL-PAEL------DNRDIDGEyfddLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVrgaskeEAEKQARE----LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQ-DLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
2.21e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI--NDVDIYNLKTKD 78
Cdd:COG4161 1 MSI-QLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFRRRNIGLIYQFYNLIPVLNVKENiLLPAELD----NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:COG4161 76 AIRLLRQKVGMVFQQYNLWPHLTVMEN-LIEAPCKvlglSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTGITQVIVTHEVEFARKvASQVVYMEKGRI 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-219 |
2.32e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.23 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYnlipvLNVKENILLPaeldNRDIDgeyFDDLMETL------GLIDRekhLPN-----------QL 142
Cdd:COG1132 413 RRQIGVVPQdtflFS-----GTIRENIRYG----RPDAT---DEEVEEAAkaaqahEFIEA---LPDgydtvvgergvNL 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 143 SGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILE-LLKLSVKKynqTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEaLERLMKGR---TTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
3.60e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.76 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRniGLIYQFYNLIPVLNVKENILLPAEL------DNRDIDgeyfDDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:COG4525 77 ---DR--GVVFQKDALLPWLNVLDNVAFGLRLrgvpkaERRARA----EELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLkLSV-KKYNQTLIMITHDKNMAL 206
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELL-LDVwQRTGKGVFLITHSVEEAL 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-222 |
3.82e-39 |
|
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: 134.25 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYgkNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRR 85
Cdd:cd03245 5 FRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQ----FYNlipvlNVKENIllpaELDNRDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQRT 150
Cdd:cd03245 79 NIGYVPQdvtlFYG-----TLRDNI----TLGAPLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-211 |
5.60e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.16 E-value: 5.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLH-------LLGGVDrpTSGKVYINDVDIYNlK 75
Cdd:COG1117 11 KIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYD-P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIFRRRnIGLIYQFYNLIPvLNVKENILLPAELdNRDIDGEYFDDLMET----LGLI----DREKHLPNQLSGGQQ 147
Cdd:COG1117 84 DVDVVELRRR-VGMVFQKPNPFP-KSIYDNVAYGLRL-HGIKSKSELDEIVEEslrkAALWdevkDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILEL---LKlsvKKYnqTLIMITHdkNMAlQADRI 211
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELileLK---KDY--TIVIVTH--NMQ-QAARV 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
1.24e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 134.03 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLktkdlaifr 83
Cdd:PRK11247 13 LLLNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEyfddLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:PRK11247 80 REDTRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKIGLD 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-216 |
1.71e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.61 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRP---TSGKVYINDVDIYNLKTkdla 80
Cdd:COG4136 2 LSLENLTITLGGRPL----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifRRRNIGLIYQFYNLIPVLNVKENIL--LPAELD--NRDidgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG4136 74 --EQRRIGILFQDDLLFPHLSVGENLAfaLPPTIGraQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIED 216
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-217 |
2.10e-38 |
|
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: 132.56 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKS---YGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIND----VDIYNL 74
Cdd:COG4778 3 TLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 75 KTKDLAIFRRRNIGLIYQFYNLIP---VLNVKENILLPAELDnRDIDGEYFDDLMETLGLIDREKHL-PNQLSGGQQQRT 150
Cdd:COG4778 83 SPREILALRRRTIGYVSQFLRVIPrvsALDVVAEPLLERGVD-REEARARARELLARLNLPERLWDLpPATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHDKN-MALQADRIISIEDG 217
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDEEvREAVADRVVDVTPF 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-219 |
2.17e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 136.31 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGknETKVDaiKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDla 80
Cdd:PRK11000 1 MASVTLRNVTKAYG--DVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrRNIGLIYQFYNLIPVLNVKENI---LLPAELDNRDIDG--EYFDDLMETLGLIDREkhlPNQLSGGQQQRTSIGRA 155
Cdd:PRK11000 75 ----RGVGMVFQSYALYPHLSVAENMsfgLKLAGAKKEEINQrvNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEI-LELLKLSvKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMrIEISRLH-KRLGRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-222 |
2.47e-38 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 140.39 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:TIGR03375 464 IEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYNlipvlNVKENILLpaelDNRDIDGEyfdDLMETL---GLIDREKHLPN-----------QLSGG 145
Cdd:TIGR03375 538 RRNIGYVPQdprlFYG-----TLRDNIAL----GAPYADDE---EILRAAelaGVTEFVRRHPDgldmqigergrSLSGG 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 146 QQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKynQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-219 |
3.02e-38 |
|
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: 132.11 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDlAIFRRR 85
Cdd:cd03265 3 VENLVKKYGDFE----AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VRE-PREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFYNLIPVLNVKENILLPAELDN--RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 164 LADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRI 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-222 |
3.27e-38 |
|
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: 134.93 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 38 ITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifrRRNIGLIYQFYNLIPVLNVKENILLPAE---LDN 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKmrkVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 115 RDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQT 194
Cdd:TIGR01187 75 AEIK-PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*....
gi 489524673 195 LIMITHDKNMAL-QADRIISIEDGIIKSD 222
Cdd:TIGR01187 154 FVFVTHDQEEAMtMSDRIAIMRKGKIAQI 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
3.72e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.95 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKT---- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIFRRRNIGLIYQFYNLIPVLNVKENIL---LPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIR-QLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-220 |
4.18e-38 |
|
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: 131.86 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiYNLKTKDLAIfr 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELD--NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 162 IILADEPTGNLDSKNSKEILELLkLSVKKyNQTLIMITHDKNMA-LQADRIISIEDGIIK 220
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLI-LEVRK-GRSIILTTHSMDEAeALCDRIAIMSDGKLR 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-222 |
4.72e-38 |
|
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: 131.46 E-value: 4.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 27 SLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlaifrrRNIGLIYQFYNLIPVLNVKENI 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 107 LL---PAeLDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILEL 183
Cdd:cd03298 92 GLglsPG-LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489524673 184 LKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-211 |
5.13e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 135.73 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY-GKNetkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlai 81
Cdd:PRK11607 19 LLEIRNLTKSFdGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 fRRRNIGLIYQFYNLIPVLNVKENILLPAELDnRDIDGEYFDDLMETLGLIDRE---KHLPNQLSGGQQQRTSIGRALIN 158
Cdd:PRK11607 89 -YQRPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQefaKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 159 RPSIILADEPTGNLDSK-NSKEILELLKLsVKKYNQTLIMITHDKNMAL-QADRI 211
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKlRDRMQLEVVDI-LERVGVTCVMVTHDQEEAMtMAGRI 220
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-211 |
5.81e-38 |
|
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: 132.03 E-value: 5.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLH-------LLGGVDrpTSGKVYINDVDIYNLK 75
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIfrRRNIGLIYQFYNLIPvLNVKENILLPAELDNRDiDGEYFDDLMETL--------GLIDREKHLPNQLSGGQQ 147
Cdd:TIGR00972 75 IDVVEL--RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIK-DKKELDEIVEESlkkaalwdEVKDRLHDSALGLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYnqTLIMITHdkNMAlQADRI 211
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTH--NMQ-QAARI 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-212 |
7.17e-38 |
|
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: 137.80 E-value: 7.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY-GKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaif 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRP----ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW--- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQfynlIPVL---NVKENILL------PAELDnRDIDGEYFDDLMETLGL-IDRE--KHlPNQLSGGQQQRT 150
Cdd:TIGR02857 395 -RDQIAWVPQ----HPFLfagTIAENIRLarpdasDAEIR-EALERAGLDEFVAALPQgLDTPigEG-GAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILE-LLKLSvkkYNQTLIMITHDKNMALQADRII 212
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEaLRALA---QGRTVLLVTHRLALAALADRIV 527
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-220 |
1.77e-37 |
|
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: 129.68 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNEtkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDlaifRR 84
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLI-----YQFYNLipvlNVKENILLpaELDNRDIDGEYFDDLMETLGLID-REKHlPNQLSGGQQQRTSIGRALIN 158
Cdd:cd03226 71 KSIGYVmqdvdYQLFTD----SVREELLL--GLKELDAGNEQAETVLKDLDLYAlKERH-PLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKN-MALQADRIISIEDGIIK 220
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-219 |
4.91e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 132.51 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKneTKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDla 80
Cdd:PRK10851 1 MSI-EIANIKKSFGR--TQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrRNIGLIYQFYNLIPVLNVKENI-----LLPA-ELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:PRK10851 74 ----RKVGFVFQHYALFRHMTVFDNIafgltVLPRrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
5.53e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 132.27 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYgknETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDla 80
Cdd:PRK11650 1 MAGLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrRNIGLIYQFYNLIPVLNVKENilLPAELDNRDIDGEYFD-------DLMETLGLIDREkhlPNQLSGGQQQRTSIG 153
Cdd:PRK11650 76 ----RDIAMVFQNYALYPHMSVREN--MAYGLKIRGMPKAEIEervaeaaRILELEPLLDRK---PRELSGGQRQRVAMG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEI-LELLKLSvKKYNQTLIMITHDK--NMALqADRIISIEDGII 219
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKLRVQMrLEIQRLH-RRLKTTSLYVTHDQveAMTL-ADRVVVMNGGVA 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
6.98e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 129.54 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA--- 80
Cdd:COG4598 9 LEVRDLHKSFGDLEV----LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGElvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 -----IFR-RRNIGLIYQFYNLIPVLNVKENILL-PAELDNRDIDG--EYFDDLMETLGLIDREKHLPNQLSGGQQQRTS 151
Cdd:COG4598 85 adrrqLQRiRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEaiERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMR-DLAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRI 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-222 |
7.43e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 129.82 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGK---NETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdl 79
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEKR--ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 aiFRR-RNIGLIYQ--FYNLIPVLNVKENILLpAE-----------LDNRDIdgEYFDDLMETLGLiDREKHLPNQ---L 142
Cdd:COG1101 76 --YKRaKYIGRVFQdpMMGTAPSMTIEENLAL-AYrrgkrrglrrgLTKKRR--ELFRELLATLGL-GLENRLDTKvglL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 143 SGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKS 221
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDyGNRLIMMHEGRIIL 229
|
.
gi 489524673 222 D 222
Cdd:COG1101 230 D 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
9.06e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 9.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI--NDVDIYNlKTKD 78
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSK-TPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFR-RRNIGLIYQFYNLIPVLNVKENiLLPAELD----NRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK11124 75 KAIRElRRNVGMVFQQYNLWPHLTVQQN-LIEAPCRvlglSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLK-LSVKKYNQtlIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIReLAETGITQ--VIVTHEVEVARKtASRVVYMENGHI 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-222 |
1.04e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.82 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNETKVD--AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLK-TKD 78
Cdd:PRK13633 3 EMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LaifrRRNIGLIYQFY-NLIPVLNVKENI--------LLPAELDNRdidgeyFDDLMETLGLIDREKHLPNQLSGGQQQR 149
Cdd:PRK13633 83 I----RNKAGMVFQNPdNQIVATIVEEDVafgpenlgIPPEEIRER------VDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-220 |
1.13e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 128.06 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 27 SLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifrRRNIGLIYQFYNLIPVLNVKENI 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 107 LL---PAeLDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILEL 183
Cdd:TIGR01277 92 GLglhPG-LKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 489524673 184 LKLSVKKYNQTLIMITHD-KNMALQADRIISIEDGIIK 220
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKIK 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-217 |
1.77e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.40 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYGKN---ETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIY--NLK 75
Cdd:PRK13637 1 MSI-KIENLTHIYMEGtpfEKK--ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLaifrRRNIGLIYQF--YNLIpvlnvKENI------------LLPAELDNRDIDGeyfddlMETLGLiDREKHL--- 138
Cdd:PRK13637 78 LSDI----RKKVGLVFQYpeYQLF-----EETIekdiafgpinlgLSEEEIENRVKRA------MNIVGL-DYEDYKdks 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 139 PNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD-KNMALQADRIISIEDG 217
Cdd:PRK13637 142 PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKG 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
2.65e-36 |
|
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: 127.58 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFrrrnigliyQFYNLIPVLNV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---------QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELDNRDIDG----EYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSK 178
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKserrAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489524673 179 EILELLKLSVKKYNQTLIMITHDKNMAL-QADRIISIEDG 217
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-219 |
2.79e-36 |
|
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: 133.27 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKS----TLLHLLGGVDRPTSGKVYINDVDIYNLKT 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIFRRRNIGLIYQ--FYNLIPVLNV----KENILL-----PAELDNRDIDgeyfddLMETLGLIDREKHL---PNQL 142
Cdd:COG4172 84 RELRRIRGNRIAMIFQepMTSLNPLHTIgkqiAEVLRLhrglsGAAARARALE------LLERVGIPDPERRLdayPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 143 SGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-217 |
7.54e-36 |
|
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: 126.25 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:COG0410 1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQFYNLIPVLNVKENILLPAEL--DNRDIDG------EYFDDLMEtlglidREKHLPNQLSGGQQQRTSI 152
Cdd:COG0410 77 ---RLGIGYVPEGRRIFPSLTVEENLLLGAYArrDRAEVRAdlervyELFPRLKE------RRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIR-RLNREGVTILLVEQNARFALEiADRAYVLERG 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
1.13e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNETkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRR 85
Cdd:PRK13632 10 VENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI----RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFY-NLIPVLNVKENILLpaELDNRDID----GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVEDDIAF--GLENKKVPpkkmKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG-IIKS 221
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGkLIAQ 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
1.41e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.67 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLai 81
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLIYQ-----FYNLIPVLNVK---ENILLPaeldnRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK13635 80 --RRQVGMVFQnpdnqFVGATVQDDVAfglENIGVP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKS 221
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-219 |
1.69e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.30 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIfR 83
Cdd:PRK11432 7 VVLKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----THRSI-Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDNRDiDGEYFDDLMETLGLIDR---EKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVP-KEERKQRVKEALELVDLagfEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKI 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-217 |
7.28e-35 |
|
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: 126.75 E-value: 7.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaIFR---RRNIGLIYQFYNLIPVLN 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARG---IFLpphRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 VKENILL---PAELDNRDIDgeyFDDLMETLG---LIDRekhLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSK 175
Cdd:COG4148 94 VRGNLLYgrkRAPRAERRIS---FDEVVELLGighLLDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489524673 176 NSKEILELLKLSVKKYNQTLIMITHD-KNMALQADRIISIEDG 217
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSlDEVARLADHVVLLEQG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-225 |
1.67e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.27 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifrr 84
Cdd:COG4604 3 EIKNVSKRYG--GKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQFYNLIPVLNVKEniL------------LPAEldnrdiDGEYFDDLMETLGLID-REKHLpNQLSGGQQQRTS 151
Cdd:COG4604 75 KRLAILRQENHINSRLTVRE--LvafgrfpyskgrLTAE------DREIIDEAIAYLDLEDlADRYL-DELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII----KSDEVM 225
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVvaqgTPEEII 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-225 |
2.07e-34 |
|
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: 125.61 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTK-DLAIFRRRnIGLIYQFYNLIPVLNVKE 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRR-IGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 105 NIllpaELDNRDIDGEY----FDDLMETLG---LIDRekhLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNS 177
Cdd:TIGR02142 95 NL----RYGMKRARPSErrisFERVIELLGighLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 178 KEILELLKLSVKKYNQTLIMITHD-KNMALQADRIISIEDGIIKS----DEVM 225
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVAAagpiAEVW 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-212 |
4.42e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.07 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY-------GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLK 75
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIFRRRnIGLIYQ--FYNLIPVLNVKENILLPAELdNRDIDG----EYFDDLMETLGLidREKHL---PNQLSGGQ 146
Cdd:COG4608 87 GRELRPLRRR-MQMVFQdpYASLNPRMTVGDIIAEPLRI-HGLASKaerrERVAELLELVGL--RPEHAdryPHEFSGGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRII 212
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHiSDRVA 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-220 |
1.80e-33 |
|
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: 118.57 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlaifr 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rrnigliyQFYNLIPVLNVKENIllpaeldnrdidgeyFDD-LMETLGLidrekhlpnQLSGGQQQRTSIGRALINRPSI 162
Cdd:cd03247 72 --------ALSSLISVLNQRPYL---------------FDTtLRNNLGR---------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 163 ILADEPTGNLDSKNSKEILELLkLSVKKyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLI-FEVLK-DKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-200 |
2.68e-33 |
|
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: 120.19 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGkvyiNDVDIYNLKTKDLA 80
Cdd:COG1119 1 DPLLELRNVTVRRG--GKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFR-RRNIGLI-----YQFYNLIPVLNVkenIL--------LPAELDNRDIdgEYFDDLMETLGLIDREKHLPNQLSGGQ 146
Cdd:COG1119 73 VWElRKRIGLVspalqLRFPRDETVLDV---VLsgffdsigLYREPTDEQR--ERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITH 200
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-225 |
3.40e-33 |
|
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: 125.25 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTksYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rRNIGLIYQFYNLIPVlNVKENIllpAeldnRdidgeyFDDlmetlglIDREK---------------HLPN-------- 140
Cdd:COG4618 406 -RHIGYLPQDVELFDG-TIAENI---A----R------FGD-------ADPEKvvaaaklagvhemilRLPDgydtrige 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 141 ---QLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:COG4618 464 ggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIR-ALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
250
....*....|..
gi 489524673 218 IIKS----DEVM 225
Cdd:COG4618 543 RVQAfgprDEVL 554
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-222 |
3.48e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 27 SLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDiYNLKTKDlaifrRRNIGLIYQFYNLIPVLNVKENI 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS-----RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 107 LL---PAELDNRDiDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILEL 183
Cdd:PRK10771 93 GLglnPGLKLNAA-QREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489524673 184 LKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-219 |
3.78e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 125.32 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQfynLIPVLN--VKENILLPAEldnrDIDGEYFDDLMETLGLidrEKHLPN-------------QLSGGQQQ 148
Cdd:PRK11160 413 RQAISVVSQ---RVHLFSatLRDNLLLAAP----NASDEALIEVLQQVGL---EKLLEDdkglnawlgeggrQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHD-KNMAlQADRIISIEDGII 219
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRlTGLE-QFDRICVMDNGQI 551
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-219 |
9.82e-33 |
|
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: 118.10 E-value: 9.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYgknETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYNLIpvlnvKENILLpAELDNRDIDGEyfdDLMETLGLIDREKHLPNQ-----------LSGGQQQ 148
Cdd:cd03253 74 RRAIGVVPQdtvlFNDTI-----GYNIRY-GRPDATDEEVI---EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-219 |
1.53e-32 |
|
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: 117.72 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQ----FYNlipvlNVKENILLpaelDNRDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQ 148
Cdd:cd03251 75 RRQIGLVSQdvflFND-----TVAENIAY----GRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELL-KLSVkkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALeRLMK---NRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-219 |
1.69e-32 |
|
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: 122.87 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSY-------GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTL-LHLLGGVdrPTSGKVYINDVDIYN 73
Cdd:COG4172 274 PLLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 74 LKTKDLAIFRRRnIGLIYQ--FYNLIPVLNVKENI-----LLPAELDNRDIDgEYFDDLMETLGL--IDREKHlPNQLSG 144
Cdd:COG4172 352 LSRRALRPLRRR-MQVVFQdpFGSLSPRMTVGQIIaeglrVHGPGLSAAERR-ARVAEALEEVGLdpAARHRY-PHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 145 GQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknmaLQ-----ADRIISIEDGII 219
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD----LAvvralAHRVMVMKDGKV 504
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-185 |
3.20e-32 |
|
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: 116.87 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKneTKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKdLAIFR 83
Cdd:cd03218 1 LRAENLSKRYGK--RKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TK-LPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIY--QFYNLIPVLNVKENILLPAEL--DNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINR 159
Cdd:cd03218 72 RARLGIGYlpQEASIFRKLTVEENILAVLEIrgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180
....*....|....*....|....*.
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLK 185
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIK 177
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-221 |
4.48e-32 |
|
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: 116.56 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKnetKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrR 84
Cdd:cd03254 4 EFENVNFSYDE---KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQFYNLIPVlNVKENILlpaeLDNRDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQRTSIG 153
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIR----LGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILE-LLKLSVKKynqTLIMITHDKNMALQADRIISIEDGIIKS 221
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEaLEKLMKGR---TSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-211 |
4.80e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGV-----DRPTSGKVYINDVDIYNLk 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 tkDLAIFRRRnIGLIYQFYNLIPVLNVKENILLPAELdNRDIDG--EYFDDLMETLG-------LIDREKHLPNQLSGGQ 146
Cdd:PRK14247 76 --DVIELRRR-VQMVFQIPNPIPNLSIFENVALGLKL-NRLVKSkkELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEIlELLKLSVKKyNQTLIMITHdknMALQADRI 211
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKK-DMTIVLVTH---FPQQAARI 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-173 |
5.14e-32 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 115.75 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNetkvDAIKNVSLSVEKGTFiAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaiFR 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQ---FYNLIPVLNVKENILLPAELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03264 72 RR-IGYLPQefgVYPNFTVREFLDYIAWLKGIPSKEVK-ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170
....*....|...
gi 489524673 161 SIILADEPTGNLD 173
Cdd:cd03264 150 SILIVDEPTAGLD 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.45e-31 |
|
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: 120.29 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVD--RPTSGKV-----------YIN--- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 68 ----------------DVDIYNLKTKDLAIFRRRNIGLIYQFYNLIPVLNVKENILLPAEldnrDIDGEYFD------DL 125
Cdd:TIGR03269 77 kvgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALE----EIGYEGKEavgravDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 126 METLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITH-DKNM 204
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVI 232
|
250 260
....*....|....*....|....
gi 489524673 205 ALQADRIISIEDGIIK----SDEV 224
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKeegtPDEV 256
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
4.02e-31 |
|
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: 113.47 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifr 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELdnRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARL--LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 164 LADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHD-KNMALQADRIISIEDGII 219
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLlSEIQKVADRIGIINKGKL 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-200 |
5.70e-31 |
|
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: 112.64 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVDA--IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGG--VDRPTSGKVYINDVDIYnlktkdL 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFRRRnIGLIYQFYNLIPVLNVKENILLPAELdnrdidgeyfddlmetlglidrekhlpNQLSGGQQQRTSIGRALINR 159
Cdd:cd03213 78 RSFRKI-IGYVPQDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALELVSN 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITH 200
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLR-RLADTGRTIICSIH 169
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-219 |
6.68e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNlKTKDLAIFR-RRNIGLIYQF-YNLIPV 99
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKYIRPvRKRIGMVFQFpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 100 LNVKENILLPAELDNRDID--GEYFDDLMETLGLI-DREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKN 176
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDevKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489524673 177 SKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDGII 219
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSI 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-168 |
8.54e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.20 E-value: 8.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKneTKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTkDLA 80
Cdd:COG1137 1 MMTLEAENLVKSYGK--RTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----T-HLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRRNIGLIY--Q----FYNLipvlNVKENILLPAELDNRDIDG--EYFDDLMETLGLIDREKHLPNQLSGGQQQRTSI 152
Cdd:COG1137 72 MHKRARLGIGYlpQeasiFRKL----TVEDNILAVLELRKLSKKEreERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170
....*....|....*.
gi 489524673 153 GRALINRPSIILADEP 168
Cdd:COG1137 148 ARALATNPKFILLDEP 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
1.08e-30 |
|
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: 112.46 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynLKTKDLAif 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPAEA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPVLNVKENILLPAELD--NRDIDGEYFDDLMETLG---LIDREKhlpNQLSGGQQQRTSIGRALI 157
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYglKGDELTARLEELADRLGmeeLLDRRV---GGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHdkNM---ALQADRIISIEDGII 219
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTH--IMqevERLCDRVVVLHRGRV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-222 |
1.22e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 113.53 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKD----- 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 -----LAIFRRRnIGLIYQFYNLIPVLNVKENI---------LLPAELDNRDIdgEYFDdlmeTLGLIDREK-HLPNQLS 143
Cdd:PRK10619 82 adknqLRLLRTR-LTMVFQHFNLWSHMTVLENVmeapiqvlgLSKQEARERAV--KYLA----KVGIDERAQgKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ-QLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-219 |
2.28e-30 |
|
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: 112.25 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 20 VDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlIPV 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQ----EPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 100 L---NVKENILL-----PAELDNRDIDGEYFDDLMETlglidrekhLPN-----------QLSGGQQQRTSIGRALINRP 160
Cdd:cd03249 88 LfdgTIAENIRYgkpdaTDEEVEEAAKKANIHDFIMS---------LPDgydtlvgergsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-225 |
2.53e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.56 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifR 83
Cdd:PRK13548 3 LEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRniGLIYQFYNLIPVLNVKENI---LLPAELDNRDiDGEYFDDLMETLGLID-REKHLPnQLSGGQQQRTSIGRALI-- 157
Cdd:PRK13548 77 RR--AVLPQHSSLSFPFTVEEVVamgRAPHGLSRAE-DDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 158 ----NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD----EVM 225
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADgtpaEVL 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-219 |
3.23e-30 |
|
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: 112.59 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY------GKNETKVdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKT 76
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfGAKQRAP-VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIFrRRNIGLIYQ--FYNLIPVLNVKENILLPAELDNRDIDGEYFDDLMETLGLID-REKH---LPNQLSGGQQQRT 150
Cdd:TIGR02769 81 KQRRAF-RRDVQLVFQdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGlRSEDadkLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
2.34e-29 |
|
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: 107.51 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlAifR 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-A--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYqfynlipvlnvkenillpaeldnrdidgeyfddlmetlglidrekhlpnQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03216 74 RAGIAMVY-------------------------------------------------QLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 164 LADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIR-RLRAQGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-211 |
4.25e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIND--VDIYNlkTKDlA 80
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS--PRD-A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IfrRRNIGLIYQFYNLIPVLNVKENILLPAE------LDNRDIDGEyFDDLMETLGL-IDrekhlPN----QLSGGQQQR 149
Cdd:COG3845 78 I--ALGIGMVHQHFMLVPNLTVAENIVLGLEptkggrLDRKAARAR-IRELSERYGLdVD-----PDakveDLSVGEQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKN--MALqADRI 211
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHKLRevMAI-ADRV 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-220 |
4.40e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 113.60 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTksYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:TIGR01842 317 LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rRNIGLIYQFYNLIPVlNVKENIllpaeldnrdidgEYFDDLMETLGLIDREK----H-----LPN-----------QLS 143
Cdd:TIGR01842 392 -KHIGYLPQDVELFPG-TVAENI-------------ARFGENADPEKIIEAAKlagvHelilrLPDgydtvigpggaTLS 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-217 |
4.61e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQ-----FYNL 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQnpdnqFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 97 IPVLNVK---ENILLPAELDNRDIDgeyfdDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLD 173
Cdd:PRK13648 100 IVKYDVAfglENHAVPYDEMHRRVS-----EALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489524673 174 SKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-201 |
6.62e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.01 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSY------GKNETKVdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNL 74
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsGKHQHQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 75 KTKDLAIFRRrNIGLIYQ--FYNLIPVLNVKENILLP----AELDNRDiDGEYFDDLMETLGL----IDRekhLPNQLSG 144
Cdd:PRK10419 80 NRAQRKAFRR-DIQMVFQdsISAVNPRKTVREIIREPlrhlLSLDKAE-RLARASEMLRAVDLddsvLDK---RPPQLSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 145 GQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-217 |
7.56e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlAif 82
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-A-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAE------LDNRDIDGEYfDDLMETLGL-IDrekhlPNQ----LSGGQQQRTS 151
Cdd:COG1129 77 QAAGIAIIHQELNLVPNLSVAENIFLGREprrgglIDWRAMRRRA-RELLARLGLdID-----PDTpvgdLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKN--MALqADRIISIEDG 217
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIR-RLKAQGVAIIYISHRLDevFEI-ADRVTVLRDG 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-222 |
8.70e-29 |
|
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: 108.19 E-value: 8.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY----------------GKNETK-VDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI 66
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslFKRKYReVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 67 NDVDIYNLKTKDLaifrrRNIGLIY-QFYNLIPVLNVKENILLPAELDNRDiDGEYFDDLMETLGLIDREKHLPN---QL 142
Cdd:cd03267 81 AGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLP-PARFKKRLDELSELLDLEELLDTpvrQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 143 SGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD-KNMALQADRIISIEDGIIKS 221
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRLLY 234
|
.
gi 489524673 222 D 222
Cdd:cd03267 235 D 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-212 |
8.88e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.93 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 21 DAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVyindvdiynlktkdlAIFRRRNIGLIYQFYNLIPVL 100
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 101 --NVKENILL-----------PAELDNRDIDgeyfdDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADE 167
Cdd:NF040873 71 plTVRDLVAMgrwarrglwrrLTRDDRAAVD-----DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489524673 168 PTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKNMALQADRII 212
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-211 |
9.14e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGV-----DRPTSGKVYINDVDIYNLKTKD 78
Cdd:PRK14267 5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIfrRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLME------TL--GLIDREKHLPNQLSGGQQQRT 150
Cdd:PRK14267 81 IEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaALwdEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLkLSVKKyNQTLIMITHDknmALQADRI 211
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELL-FELKK-EYTIVLVTHS---PAQAARV 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
1.70e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifR 83
Cdd:COG4559 2 LEAENLSVRLGGRTL----LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRniGLIYQFYNLIPVLNVKENILL-------PAELDNRDIDgeyfdDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:COG4559 76 RR--AVLPQHSSLAFPFTVEEVVALgraphgsSAAQDRQIVR-----EALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 157 I-------NRPSIILADEPTGNLDSKNSKEILELLK-LSVKKYnqTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARqLARRGG--GVVAVLHDLNLAAQyADRILLLHQG 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-220 |
2.56e-28 |
|
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: 106.42 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQfynlIPVL---NVKENIllpaeldnrDIDGEYFD-DLMETL--------------GLIDREKHLPNQLSGG 145
Cdd:cd03244 77 RSRISIIPQ----DPVLfsgTIRSNL---------DPFGEYSDeELWQALervglkefveslpgGLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 146 QQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-217 |
2.57e-28 |
|
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: 107.22 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKV-YIN----DVDIYNLKTK 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK----GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMrsgaELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIFRRRNIGLIYQFynliPVLNVKENILLPAELDNR--DIDGEYFDDLMETLGL------IDREK--HLPNQLSGGQQ 147
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQN----PRDGLRMRVSAGANIGERlmAIGARHYGNIRATAQDwleeveIDPTRidDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMA-LQADRIISIEDG 217
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVArLLAQRLLVMQQG 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-211 |
3.57e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.18 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLH-------LLGGVDrpTSGKVYINDVDIYNLK 75
Cdd:PRK14243 10 VLRTENLNVYYGSFL----AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIfrRRNIGLIYQFYNLIPVlNVKENILLPAELDNRDIDgeyFDDLMET----LGLIDREKHLPNQ----LSGGQQ 147
Cdd:PRK14243 84 VDPVEV--RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGD---MDELVERslrqAALWDEVKDKLKQsglsLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYnqTLIMITHdkNMAlQADRI 211
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTH--NMQ-QAARV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-201 |
5.55e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.57 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY----GKNETKVD---AIKNVSLSVEKGTFIAITGPSGSGKST----LLHLLggvdrPTSGKVYINDVDI 71
Cdd:PRK15134 275 LLDVEQLQVAFpirkGILKRTVDhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 72 YNLKTKDLAIFRRRnIGLIYQFYN--LIPVLNVKENI----------LLPAELDNRDIDgeyfddLMETLGLIDREKH-L 138
Cdd:PRK15134 350 HNLNRRQLLPVRHR-IQVVFQDPNssLNPRLNVLQIIeeglrvhqptLSAAQREQQVIA------VMEEVGLDPETRHrY 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 139 PNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
6.82e-28 |
|
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: 105.06 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiynlktKDLAIFR 83
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAELDN---RDIDGEyFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGlkkEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHdkNMAL---QADRIISIEDG 217
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVI-RELARAGKTVILSTH--QMELveeLCDRVLLLNKG 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-217 |
8.19e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.25 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGV---DRPTSGKVYI--NDVDIYNLKTK 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELlgRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIfRRRNIGLIYQFYNLIPVLNVKENILLPA-----------ELDNRDIDGEYFDDLMEtLGLIDREKHLPNQLSGGQ 146
Cdd:PRK09984 80 DIRK-SRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-219 |
9.54e-28 |
|
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: 105.26 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGKNETkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYindVDIYNLKTKDLAIFRRRn 86
Cdd:cd03252 4 EHVRFRYKPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL---VDGHDLALADPAWLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 87 IGLIYQfYNLIPVLNVKENILL--PAELDNRDIDG-------EYFDDLMETLGLIDREKHLpnQLSGGQQQRTSIGRALI 157
Cdd:cd03252 78 VGVVLQ-ENVLFNRSIRDNIALadPGMSMERVIEAaklagahDFISELPEGYDTIVGEQGA--GLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
1.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiyNLKTKDLA 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRRNIGLIYQFY-NLIPVLNVKENILLpaELDNRDID----GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRA 155
Cdd:PRK13650 77 WDIRHKIGMVFQNPdNQFVGATVEDDVAF--GLENKGIPheemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKS 221
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVES 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-219 |
1.41e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.45 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKvdaiKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA----ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rRNIGLIYQFYNLIPVLNVKENIL------LPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:PRK10253 81 -RRIGLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKI 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-201 |
2.37e-27 |
|
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: 108.60 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVlNVKENILLPAEldnrDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQRTSI 152
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDT-TVRENLRLARP----DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLkLSVKKyNQTLIMITHD 201
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDL-LAALS-GRTVVLITHH 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-217 |
3.14e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRRNIGLIYQFYNLIPVLN 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 VKENILLPAELDNRDID--GEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKE 179
Cdd:PRK10070 123 VLDNTAFGMELAGINAEerREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489524673 180 IL-ELLKLSVkKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK10070 203 MQdELVKLQA-KHQRTIVFISHDLDEAMRiGDRIAIMQNG 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-220 |
1.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 21 DAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYN-LKTKDLAIFRRRnIGLIYQFynlipv 99
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKK-VGIVFQF------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 100 lnvKENILLpAELDNRDI----------DGEYFDDLMETLGLIDREKHL----PNQLSGGQQQRTSIGRALINRPSIILA 165
Cdd:PRK13634 94 ---PEHQLF-EETVEKDIcfgpmnfgvsEEDAKQKAREMIELVGLPEELlarsPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 166 DEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHdkNM---ALQADRIISIEDGIIK 220
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTH--SMedaARYADQIVVMHKGTVF 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-223 |
1.26e-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: 102.22 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDGE---YFDDLMETLGlidREKHLpnqLSGGQQQRTSIGRALI 157
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAAlprRSRKIPDEiyeLFPVLKEMLG---RRGGD---LSGGQQQQLAIARALV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSDE 223
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASG 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-212 |
1.35e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.44 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKS-TLLHLLGGVDRP---TSGKVYINDVDIYNLKT 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDlaifRRRNIG----LIYQ--FYNLIPVLNVKENILLPAELD---NRDIDGEYFDDLMETLGLIDREKHL---PNQLSG 144
Cdd:PRK11022 81 KE----RRNLVGaevaMIFQdpMTSLNPCYTVGFQIMEAIKVHqggNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 145 GQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNM-ALQADRII 212
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKII 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-219 |
1.67e-26 |
|
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: 100.58 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSygknetkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDLAI 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV---TRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 FRRRNIGLI---YQFYNLIPVLNVKENILLPAeldnrdidgeyfddlmetlglidrekhlpnQLSGGQQQRTSIGRALIN 158
Cdd:cd03215 72 AIRAGIAYVpedRKREGLVLDLSVAENIALSS------------------------------LLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLI-RELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-217 |
2.31e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.31 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKV-YIN----DVDIYNLKTK 77
Cdd:PRK11701 6 LLSVRGLTKLYGP----RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMrdgqLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIFRRRNIGLIYQfyNLIPVL--------NVKE-----------NILLPAE--LDNRDIDGEYFDDLmetlglidrek 136
Cdd:PRK11701 82 ERRRLLRTEWGFVHQ--HPRDGLrmqvsaggNIGErlmavgarhygDIRATAGdwLERVEIDAARIDDL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 137 hlPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMA-LQADRIISIE 215
Cdd:PRK11701 149 --PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVArLLAHRLLVMK 226
|
..
gi 489524673 216 DG 217
Cdd:PRK11701 227 QG 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
2.58e-26 |
|
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: 105.65 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNETKV-DAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFR---RRNIGLIYQFYNLIPVLNVKENIL------LPAELDNRD----IDGEYFDDlMETLGLIDRekhLPNQLSGGQQ 147
Cdd:TIGR03269 358 DGRgraKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARMKavitLKMVGFDE-EKAEEILDK---YPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG-IIK 220
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGkIVK 508
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
3.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.86 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEIlRVENLTKSYG-KNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDL 79
Cdd:PRK13651 1 MQI-KVKNIVKIFNkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 A------------IFR--------RRNIGLIYQF--YNLIPVLNVKENILLPAEL-----DNRDIDGEYfddlMETLGL- 131
Cdd:PRK13651 80 KekvleklviqktRFKkikkikeiRRRVGVVFQFaeYQLFEQTIEKDIIFGPVSMgvskeEAKKRAAKY----IELVGLd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 132 IDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADR 210
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD-NLNKQGKTIILVTHDLDNVLEwTKR 234
|
250
....*....|.
gi 489524673 211 IISIEDG-IIK 220
Cdd:PRK13651 235 TIFFKDGkIIK 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.66e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.01 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYG-KNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDI--------- 71
Cdd:PRK13631 20 IILRVKNLYCVFDeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 72 -YNLKTKDLAIFR--RRNIGLIYQF--YNLIPVLNVKENILLPAELDNRDIDG-EYFDDLMETLGL----IDREkhlPNQ 141
Cdd:PRK13631 100 iTNPYSKKIKNFKelRRRVSMVFQFpeYQLFKDTIEKDIMFGPVALGVKKSEAkKLAKFYLNKMGLddsyLERS---PFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 142 LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSvKKYNQTLIMITHDKNMALQ-ADRIISIEDG-II 219
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEvADEVIVMDKGkIL 255
|
..
gi 489524673 220 KS 221
Cdd:PRK13631 256 KT 257
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-217 |
4.40e-26 |
|
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: 100.24 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVD-AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINdvdiynlktkdlaif 82
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrRNIGLIYQFynliP-VLN--VKENILLPAELDNrdidgEYFDDLMETLGLIDREKHLPNQ-----------LSGGQQQ 148
Cdd:cd03250 66 --GSIAYVSQE----PwIQNgtIRENILFGKPFDE-----ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
5.88e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYgKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaif 82
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYN-LIPVLNVKENI--------LLPAELDNRdidgeyFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK13647 78 -RSKVGLVFQDPDdQVFSSTVWDDVafgpvnmgLDKDEVERR------VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILD-RLHNQGKTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-224 |
1.18e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 13 YGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQ 92
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 93 fynlIPVL---NVKENILLPAELDNRDIDGEYFDDLMETLGLIDR--EKHLpNQLSGGQQQRTSIGRALINRPSIILADE 167
Cdd:PRK10247 89 ----TPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTilTKNI-AELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 168 PTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSDEV 224
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEA 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-201 |
1.29e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIF 82
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RrrniGLIYQFYNLIPVLNVKENILLPAELDN--RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:PRK11248 72 R----GVVFQNEGLLPWRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
1.51e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGV-----DRPTSGKVYINDVDIYNLKT 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIfrRRNIGLIYQFYNLIPvLNVKENILLPAELdNRDIDGEYFDDLMETlGLI---------DREKHLPNQLSGGQQ 147
Cdd:PRK14239 80 DTVDL--RKEIGMVFQQPNPFP-MSIYENVVYGLRL-KGIKDKQVLDEAVEK-SLKgasiwdevkDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYnqTLIMITHdkNMAlQADRI 211
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTR--SMQ-QASRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.79e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIyNLKTKDLAIF 82
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFY-NLIPVLNVKENIL---LPAELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALIN 158
Cdd:PRK13639 77 RKT-VGIVFQNPdDQLFAPTVEEDVAfgpLNLGLSKEEVE-KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMA-LQADRIISIEDG-IIKS 221
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLY-DLNKEGITIIISTHDVDLVpVYADKVYVMSDGkIIKE 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-201 |
2.17e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKS----TLLHLLGGVDRpTSGKVYINDVDIYNLKT 76
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIFRRRNIGLIYQ--FYNLIPVLNVKENILLPAELDNRDIDGEYFDdlmETLGLID---------REKHLPNQLSGG 145
Cdd:PRK09473 89 KELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFE---ESVRMLDavkmpearkRMKMYPHEFSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 146 QQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-221 |
2.36e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.49 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 37 AITGPSGSGKSTLLHLLGGVDRPTSGKVYIND---VDIYNlktkdlAIF---RRRNIGLIYQFYNLIPVLNVKENILLPA 110
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEK------GIClppEKRRIGYVFQDARLFPHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 111 eldnRDIDGEYFDDLMETLG---LIDRekhLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELL-KL 186
Cdd:PRK11144 102 ----AKSMVAQFDKIVALLGiepLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLeRL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 489524673 187 SvKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKS 221
Cdd:PRK11144 175 A-REINIPILYVSHSLDEILRlADRVVVLEQGKVKA 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
3.16e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYgknETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLa 80
Cdd:PRK13652 1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQfynlipvlNVKENILLPA-ELD------NRDIDGEYF----DDLMETLGLIDREKHLPNQLSGGQQQR 149
Cdd:PRK13652 77 ---RKFVGLVFQ--------NPDDQIFSPTvEQDiafgpiNLGLDEETVahrvSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNM-ALQADRIISIEDGII 219
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-219 |
4.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYgkNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIF 82
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFY-NLIPVLNVKENILLpaELDNRDIDGEYF----DDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:PRK13640 83 REK-VGIVFQNPdNQFVGATVGDDVAF--GLENRAVPRPEMikivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
5.33e-25 |
|
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: 95.59 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVyindvdiynlktkdlaifr 83
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rrnigliyqfyNLIPVLNVKenillpaeldnrdidgeYFDdlmetlglidrekhlpnQLSGGQQQRTSIGRALINRPSII 163
Cdd:cd03221 58 -----------TWGSTVKIG-----------------YFE-----------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 164 LADEPTGNLDSKnSKEILELLklsVKKYNQTLIMITHDKNMaLQ--ADRIISIEDG 217
Cdd:cd03221 93 LLDEPTNHLDLE-SIEALEEA---LKEYPGTVILVSHDRYF-LDqvATKIIELEDG 143
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-222 |
6.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIY-NLKTKDLAIFRRRnIGLIYQFynliPVLNVK 103
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRKK-VSLVFQF----PEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 104 ENILL------PAELDNRDIDG-EYFDDLMETLGLI-DREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSK 175
Cdd:PRK13641 100 ENTVLkdvefgPKNFGFSEDEAkEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489524673 176 NSKEILELLKlSVKKYNQTLIMITHD-KNMALQADRIISIEDG-IIKSD 222
Cdd:PRK13641 180 GRKEMMQLFK-DYQKAGHTVILVTHNmDDVAEYADDVLVLEHGkLIKHA 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-201 |
6.77e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.65 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY------GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKT 76
Cdd:PRK11308 5 LLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIfRRRNIGLIYQfyNLIPVLNVKENI--LLPAELD-NRDIDG----EYFDDLMETLGLidREKH---LPNQLSGGQ 146
Cdd:PRK11308 85 EAQKL-LRQKIQIVFQ--NPYGSLNPRKKVgqILEEPLLiNTSLSAaerrEKALAMMAKVGL--RPEHydrYPHMFSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-221 |
1.22e-24 |
|
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: 96.33 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifr 83
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQfynlipvlnvkENILLPAEL-DNRDIDGEYFD-DLMETLglidREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:cd03369 81 RSSLTIIPQ-----------DPTLFSGTIrSNLDPFDEYSDeEIYGAL----RVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIKS 221
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
1.45e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNEtkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINdvdiynlktKDLaifrrr 85
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGL------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFYNLIPVLNVKENIL---------------LPAELDNRDIDGEYFDDLMET-------------------LGL 131
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLdgdaelraleaeleeLEAKLAEPDEDLERLAELQEEfealggweaearaeeilsgLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 132 IDREKHLP-NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSkNSKEILE-LLklsvKKYNQTLIMITHDK----NMa 205
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLEeFL----KNYPGTVLVVSHDRyfldRV- 215
|
250
....*....|....*.
gi 489524673 206 lqADRIISIEDGIIKS 221
Cdd:COG0488 216 --ATRILELDRGKLTL 229
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-219 |
1.68e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 96.67 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKST----LLHLLGGVDRPTSGKVYINDVDIYNLKtkdlaiFRRRNIGLIYQ----F 93
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQnprtA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 94 YNliPVLNVKEN------ILLPAELDNRDIDGEyfddLMETLGLIDREKHL---PNQLSGGQQQRTSIGRALINRPSIIL 164
Cdd:TIGR02770 75 FN--PLFTMGNHaietlrSLGKLSKQARALILE----ALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 165 ADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDGII 219
Cdd:TIGR02770 149 ADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGvVARIADEVAVMDDGRI 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-200 |
1.83e-24 |
|
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: 96.57 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRP---TSGKVYINDVDIYNLKTKDl 79
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 aifrrrNIGLIYQFYNLIPVLNVKE------NILLPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:cd03234 82 ------CVAYVRQDDILLPGLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITH 200
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-219 |
1.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKnETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLai 81
Cdd:PRK13642 3 KILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLIYQFY-NLIPVLNVKENILLPAEldNRDIDGEYF----DDLMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:PRK13642 80 --RRKIGMVFQNPdNQFVGATVEDDVAFGME--NQGIPREEMikrvDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-221 |
2.73e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.12 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNL-KTKDLAIFRRRnIGLIYQFynliPVL 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQIRKK-VGLVFQF----PES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 101 NVKENILL------PAELDNRDIDGEYFddLMETLGLIDREKHL----PNQLSGGQQQRTSIGRALINRPSIILADEPTG 170
Cdd:PRK13649 97 QLFEETVLkdvafgPQNFGVSQEEAEAL--AREKLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 171 NLDSKNSKEILELLKlSVKKYNQTLIMITH-DKNMALQADRIISIEDG-IIKS 221
Cdd:PRK13649 175 GLDPKGRKELMTLFK-KLHQSGMTIVLVTHlMDDVANYADFVYVLEKGkLVLS 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
2.86e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.85 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNE-----------------TKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVY 65
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 66 INDVDIYNLKtKDLAifrrRNIGLIY-QFYNLIPVLNVKENILLpaeldNRDI----DGEY---FDDLMETLGLidreKH 137
Cdd:COG4586 81 VLGYVPFKRR-KEFA----RRIGVVFgQRSQLWWDLPAIDSFRL-----LKAIyripDAEYkkrLDELVELLDL----GE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 138 LPN----QLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknM----ALqAD 209
Cdd:COG4586 147 LLDtpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD--MddieAL-CD 223
|
....*...
gi 489524673 210 RIISIEDG 217
Cdd:COG4586 224 RVIVIDHG 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-221 |
3.55e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVD-AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNL-KTKDLA 80
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRRnIGLIYQF--YNLIPVLNVKENILLPAELDNRDIDGEYF-DDLMETLGLIDR--EKHlPNQLSGGQQQRTSIGRA 155
Cdd:PRK13643 81 PVRKK-VGVVFQFpeSQLFEETVLKDVAFGPQNFGIPKEKAEKIaAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITH-DKNMALQADRIISIEDGIIKS 221
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-217 |
5.12e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.41 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 16 NETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfyn 95
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQ--- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 96 lIPVL---NVKENILL------PAELDNRDIDGEYFDDLMETLGLIDRE-KHLPNQLSGGQQQRTSIGRALINRPSIILA 165
Cdd:TIGR00958 563 -EPVLfsgSVRENIAYgltdtpDEEIMAAAKAANAHDFIMEFPNGYDTEvGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489524673 166 DEPTGNLDSknskEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:TIGR00958 642 DEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKG 689
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-219 |
6.24e-24 |
|
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: 99.12 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlIPVL-N- 101
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQ----DTVLfNd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 -VKENILL------PAELdNRDIDGEYFDDLMETL-----------GLidrekhlpnQLSGGQQQRTSIGRALINRPSII 163
Cdd:COG5265 447 tIAYNIAYgrpdasEEEV-EAAARAAQIHDFIESLpdgydtrvgerGL---------KLSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 164 LADEPTGNLDSKNSKEILELLKlSVKKyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALR-EVAR-GRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-217 |
8.13e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGkNETKVDaikNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIF 82
Cdd:PRK13537 7 PIDFRNVEKRYG-DKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILlpaeldnrdIDGEYFD-----------DLMETLGLIDREKHLPNQLSGGQQQRTS 151
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLL---------VFGRYFGlsaaaaralvpPLLEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLR-SLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-225 |
8.21e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKneTKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAif 82
Cdd:PRK11231 2 TLRTENLTVGYGT--KRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrRNIGLIYQFYnLIPV-LNVKENIL--------LPAELDNRdiDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIG 153
Cdd:PRK11231 76 --RRLALLPQHH-LTPEgITVRELVAygrspwlsLWGRLSAE--DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKS----DEVM 225
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAqgtpEEVM 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-219 |
9.25e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPTSGKVYINDVDIYNLktkDLAIFRRrNIGLIYQfyN-LIPVLNV 102
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRK-HLSWVGQ--NpQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLpaelDNRDIDGEYFDDLMETLGLIDREKHLPN-----------QLSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:PRK11174 440 RDNVLL----GNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489524673 172 LDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-217 |
9.68e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.77 E-value: 9.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKS-TLLHLLGGVDRpTSGKVYIND----------VD 70
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrqvIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 71 IYNLKTKDLAIFRRRNIGLIYQ--FYNLIPVLNVKENILLPAELdNRDIDGEyfDDLMETLGLIDREK---------HLP 139
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRL-HQGASRE--EAMVEAKRMLDQVRipeaqtilsRYP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 140 NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDG 217
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-212 |
1.09e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.24 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGK-----NETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiYNLKTK 77
Cdd:PRK15112 4 LLEVRNLSKTFRYrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAiFRRRNIGLIYQ--FYNLIPVLNVKENILLPAELdNRDIDGE----YFDDLMETLGLI-DREKHLPNQLSGGQQQRT 150
Cdd:PRK15112 81 DYS-YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRL-NTDLEPEqrekQIIETLRQVGLLpDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 151 SIGRALINRPSIILADEPTGNLD-SKNSKEILELLKLSVKK------YNQTLIMITH--DKNMALQADRII 212
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQgisyiyVTQHLGMMKHisDQVLVMHQGEVV 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-217 |
1.37e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKSYGkNETKVDAiknVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIFRRRNI 87
Cdd:PRK13536 46 GVSKSYG-DKAVVNG---LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-----PARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 88 GLIYQFYNLIPVLNVKENILLPAE---LDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIIL 164
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRyfgMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 165 ADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-182 |
1.79e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 93.19 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTksYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktKDLAIFR 83
Cdd:TIGR01189 1 LAARNLA--CSRGERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIdgeyfDDLMETLGLIDREkHLP-NQLSGGQQQRTSIGRALINR 159
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHFWAAIhggAQRTI-----EDALAAVGLTGFE-DLPaAQLSAGQQRRLALARLWLSR 145
|
170 180
....*....|....*....|...
gi 489524673 160 PSIILADEPTGNLDsKNSKEILE 182
Cdd:TIGR01189 146 RPLWILDEPTTALD-KAGVALLA 167
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-219 |
2.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDiynlkTKDLAIF 82
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-----TGDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 R--RRNIGLIYQFYNLIPV-LNVKENI--------LLPAELDNRdidgeyFDDLMETLGLIDREKHLPNQLSGGQQQRTS 151
Cdd:PRK13644 73 QgiRKLVGIVFQNPETQFVgRTVEEDLafgpenlcLPPIEIRKR------VDRALAEIGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIK-KLHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-217 |
3.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNET-KVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDI-YNLK----TKDL 79
Cdd:PRK13645 9 LDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKkikeVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 aifrRRNIGLIYQF--YNLIPVLNVKENILLPAEL-DNRDidgEYFDDLMETLGLI----DREKHLPNQLSGGQQQRTSI 152
Cdd:PRK13645 89 ----RKEIGLVFQFpeYQLFQETIEKDIAFGPVNLgENKQ---EAYKKVPELLKLVqlpeDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEG 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-217 |
1.09e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAi 81
Cdd:PRK11300 4 PLLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frrrNIGLIYQFYN--LIPVLNVKENiLLPAEldNRDIDGEYFDDLMETLGL-------IDREKH---------LPNQ-- 141
Cdd:PRK11300 79 ----RMGVVRTFQHvrLFREMTVIEN-LLVAQ--HQQLKTGLFSGLLKTPAFrraeseaLDRAATwlervglleHANRqa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 142 --LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknMALQ---ADRIISIED 216
Cdd:PRK11300 152 gnLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD--MKLVmgiSDRIYVVNQ 229
|
.
gi 489524673 217 G 217
Cdd:PRK11300 230 G 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-221 |
2.16e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGkneTKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRN 86
Cdd:PRK13657 338 DDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 87 IGLIYQFYNLipvLN--VKENILLPAElDNRDIDGEYFDDLMETLGLIDREKH--------LPNQLSGGQQQRTSIGRAL 156
Cdd:PRK13657 411 IAVVFQDAGL---FNrsIEDNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDgydtvvgeRGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKlSVKKyNQTLIMITHDKNMALQADRIISIEDG-IIKS 221
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALD-ELMK-GRTTFIIAHRLSTVRNADRILVFDNGrVVES 550
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-217 |
2.26e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDiynlktkDLAIFRRRniglIYqfynlIPVLNV 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-------RVLFLPQR----PY-----LPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAelDNRDIDGEYFDDLMETLGL------IDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKN 176
Cdd:COG4178 443 REALLYPA--TAEAFSDAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489524673 177 SKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:COG4178 521 EAALYQLLREELP--GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-219 |
5.24e-22 |
|
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: 89.84 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYgKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaif 82
Cdd:cd03248 11 IVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFynliPVL---NVKENIL-----LPAELDNRDIDGEYFDDLMETLGL-IDRE-KHLPNQLSGGQQQRTSI 152
Cdd:cd03248 87 -HSKVSLVGQE----PVLfarSLQDNIAyglqsCSFECVKEAAQKAHAHSFISELASgYDTEvGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-217 |
6.50e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktkDLAIf 82
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL------DPED- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGliyqfY-----NLIPVLNVKENILLPAEL---DNRDIDGEyFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:COG4152 70 -RRRIG-----YlpeerGLYPKMKVGEQLVYLARLkglSKAEAKRR-ADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 155 ALINRPSIILADEPTGNLDSKN----SKEILELlklsvKKYNQTLIMITHdkNMALQ---ADRIISIEDG 217
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNvellKDVIREL-----AAKGTTVIFSSH--QMELVeelCDRIVIINKG 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
1.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIyNLKTKDLAIF 82
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRrNIGLIYQFY-NLIPVLNVKENI---LLPAELDNRDIDgEYFDDLMETLGlIDREKHLPNQ-LSGGQQQRTSIGRALI 157
Cdd:PRK13636 81 RE-SVGMVFQDPdNQLFSASVYQDVsfgAVNLKLPEDEVR-KRVDNALKRTG-IEHLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 158 NRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDG 217
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDiVPLYCDNVFVMKEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-220 |
1.05e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiyNLKtkdLAIF 82
Cdd:COG0488 315 VLELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----TVK---IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIgliyqfyNLIPVLNVKENIllpaeldnrdidGEYFDDLMET-----LG--LIDREKHL-P-NQLSGGQQQRTSIG 153
Cdd:COG0488 384 DQHQE-------ELDPDKTVLDEL------------RDGAPGGTEQevrgyLGrfLFSGDDAFkPvGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 154 RALINRPSIILADEPTGNLDSkNSKEILELLklsVKKYNQTLIMITHDKnMALQ--ADRIISIEDGIIK 220
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDI-ETLEALEEA---LDDFPGTVLLVSHDR-YFLDrvATRILEFEDGGVR 508
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-217 |
1.47e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.47 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNEtkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRR 85
Cdd:PRK10790 343 IDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQfynlIPVL---NVKENILLpaeldNRDIDGEYFDDLMETLGLIDREKHLP-----------NQLSGGQQQRTS 151
Cdd:PRK10790 416 GVAMVQQ----DPVVladTFLANVTL-----GRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKNSKEILELLKLsVKKyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAA-VRE-HTTLVVIAHRLSTIVEADTILVLHRG 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-219 |
2.95e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 91.72 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNEtkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLktkdlaifr 83
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--------- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rrNIGLIYQFYNLIP------VLNVKENILLPAeldNRDIDGEYFDDLMETLGLIDREKHLP-----------NQLSGGQ 146
Cdd:TIGR01193 542 --DRHTLRQFINYLPqepyifSGSILENLLLGA---KENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILE-LLKLSVKkynqTLIMITHDKNMALQADRIISIEDGII 219
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNnLLNLQDK----TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-225 |
3.56e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKsygknETKVDAIKNVSLSVEKGTFIAITGPSGSGKS-TLLHLLG----GVDRpTSGKVYINDVDIYnlktkd 78
Cdd:PRK10418 5 IELRNIAL-----QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGilpaGVRQ-TAGRVLLDGKPVA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFRRRNIGLIYQ----FYNliPVLN----VKENILLPAELDNRDIdgeyFDDLMETLGLIDREKHL---PNQLSGGQQ 147
Cdd:PRK10418 73 PCALRGRKIATIMQnprsAFN--PLHTmhthARETCLALGKPADDAT----LTAALEAVGLENAARVLklyPFEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIEDG-IIKSDEVM 225
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGrIVEQGDVE 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
3.61e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTkdlA 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLMETLG-LIDREKHLPNQLSGGQQQRTSIGRALINR 159
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 160 PSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIE-QLREQGMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-217 |
4.02e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDR------PTSGKVYINDVDIYNLKtkdlAIFRRRNIGLIYQFYNL 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID----AIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 97 IPVLNVKENILLPAEL----DNRDIDgEYFDDLMETLGL----IDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEP 168
Cdd:PRK14246 102 FPHLSIYDNIAYPLKShgikEKREIK-KIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489524673 169 TGNLDSKNSKEILELlkLSVKKYNQTLIMITHD-KNMALQADRIISIEDG 217
Cdd:PRK14246 181 TSMIDIVNSQAIEKL--ITELKNEIAIVIVSHNpQQVARVADYVAFLYNG 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-217 |
4.92e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY-GknetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlAIf 82
Cdd:PRK11288 5 LSFDGIGKTFpG-----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-AL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPVLNVKENILL---PAE---LDNRDIDGEYFDDLmETLGL-IDREKHLpNQLSGGQQQRTSIGRA 155
Cdd:PRK11288 78 -AAGVAIIYQELHLVPEMTVAENLYLgqlPHKggiVNRRLLNYEAREQL-EHLGVdIDPDTPL-KYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 156 LINRPSIILADEPTGNLdskNSKEILELLKL--SVKKYNQTLIMITH--DKNMALqADRIISIEDG 217
Cdd:PRK11288 155 LARNARVIAFDEPTSSL---SAREIEQLFRVirELRAEGRVILYVSHrmEEIFAL-CDAITVFKDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
9.78e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKS-TLLHLLGGVDRP----TSGKVYINDVDIYNLK 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIFRRRNIGLIYQ--FYNLIPVLNVK----ENILLPAELDNRDIDGEYFDDLmETLGLIDREKHL---PNQLSGGQ 146
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQepMVSLNPLHTLEkqlyEVLSLHRGMRREAARGEILNCL-DRVGIRQAAKRLtdyPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-173 |
1.06e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTksyGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlai 81
Cdd:COG3845 256 VVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 FRRRNIGLI---YQFYNLIPVLNVKENILLpaeldnrdidGEYFDDLMETLGLIDREK-------------------HLP 139
Cdd:COG3845 330 RRRLGVAYIpedRLGRGLVPDMSVAENLIL----------GRYRRPPFSRGGFLDRKAirafaeelieefdvrtpgpDTP 399
|
170 180 190
....*....|....*....|....*....|....*
gi 489524673 140 -NQLSGGQQQRTSIGRALINRPSIILADEPTGNLD 173
Cdd:COG3845 400 aRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-185 |
2.76e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQFYNLIPVLNVKENILLPAELdNRDIDGEYFDD----LMETLGLIDREKHLPNQLSGGQQQRTSIGRAL 156
Cdd:PRK10895 77 ---RRGIGYLPQEASIFRRLSVYDNLMAVLQI-RDDLSAEQREDraneLMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190
....*....|....*....|....*....|..
gi 489524673 157 INRPSIILADEPTGNLDS---KNSKEILELLK 185
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPisvIDIKRIIEHLR 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
3.11e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPT---SGKVYINDVDiynLKTKDL 79
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEE---LQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFRRRNIGLIYQFYNLIPVLNVKENILLPAELDNR---DIDGEYF--DDLMETLGlIDREKHLP-NQLSGGQQQRTSIG 153
Cdd:PRK13549 77 RDTERAGIAIIHQELALVKELSVLENIFLGNEITPGgimDYDAMYLraQKLLAQLK-LDINPATPvGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKN--MALqADRIISIEDG 217
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIR-DLKAHGIACIYISHKLNevKAI-SDTICVIRDG 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-200 |
6.31e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLL-----GGVDRptSGKVYINDVDIynlktkDLAIFRRRNiGLIYQFYNLI 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspKGVKG--SGSVLLNGMPI------DAKEMRAIS-AYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 98 PVLNVKENILLPAEL-----DNRDIDGEYFDDLMETLGLIDREKHL---PNQ---LSGGQQQRTSIGRALINRPSIILAD 166
Cdd:TIGR00955 112 PTLTVREHLMFQAHLrmprrVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|....*
gi 489524673 167 EPTGNLDSKNSKEILELLK-LSVKkyNQTLIMITH 200
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKgLAQK--GKTIICTIH 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
6.52e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGknETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFG--DTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IFRRrnigliyqfynlipVLNVKENILLPAELDNRDI------------------DGEYFDDLMETLG---LIDREKhlp 139
Cdd:PRK09536 75 ASRR--------------VASVPQDTSLSFEFDVRQVvemgrtphrsrfdtwtetDRAAVERAMERTGvaqFADRPV--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 140 NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKNMALQ-ADRIISIEDGI 218
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARyCDELVLLADGR 216
|
.
gi 489524673 219 I 219
Cdd:PRK09536 217 V 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-212 |
8.17e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRV-ENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGG--VDRPTSGKVYINDVDIYNlktk 77
Cdd:COG2401 25 ERVAIVlEAFGVELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIfrrrnigliyqfynlipvlnvkenillpaeLDNRDIDGEyFDDLMETL---GLID----REKhlPNQLSGGQQQRT 150
Cdd:COG2401 99 EASL------------------------------IDAIGRKGD-FKDAVELLnavGLSDavlwLRR--FKELSTGQKFRF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 151 SIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNM--ALQADRII 212
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVidDLQPDLLI 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-168 |
1.10e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.82 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRRnIGLIYQFYNLIPVLNVKE 104
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 105 NIL--------LPAELDNRDIdgeyfddLM--ETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEP 168
Cdd:PRK11831 104 NVAyplrehtqLPAPLLHSTV-------MMklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-221 |
2.42e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVD--RPTSGKVYINDVDIYNLKTKDLAi 81
Cdd:COG0396 1 LEIKNLHVSVEGKEI----LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLIYQFYNLIPVLNVKE------NILLPAELDNRDIDGEYfDDLMETLGL----IDREkhLPNQLSGGQQQRTS 151
Cdd:COG0396 76 --RAGIFLAFQYPVEIPGVSVSNflrtalNARRGEELSAREFLKLL-KEKMKELGLdedfLDRY--VNEGFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 152 IGRALINRPSIILADEPTGNLDsknskeI--LELLKLSVKKY---NQTLIMITHDKNM--ALQADRIISIEDG-IIKS 221
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD------IdaLRIVAEGVNKLrspDRGILIITHYQRIldYIKPDFVHVLVDGrIVKS 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-169 |
3.05e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSygknetkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlAI 81
Cdd:COG1129 255 VVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-AI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLI---YQFYNLIPVLNVKENILLPA--------ELDNRDIDgEYFDDLMETLGL-IDREKHLPNQLSGGQQQR 149
Cdd:COG1129 326 --RAGIAYVpedRKGEGLVLDLSIRENITLASldrlsrggLLDRRRER-ALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK 402
|
170 180
....*....|....*....|
gi 489524673 150 TSIGRALINRPSIILADEPT 169
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPT 422
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-201 |
3.21e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIfRRRNIGLIYQ--FYNLIPV 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 100 LNVKENILLP-----AELDNRDIDgEYFDDLMETLGL----IDRekhLPNQLSGGQQQRTSIGRALINRPSIILADEPTG 170
Cdd:PRK15079 115 MTIGEIIAEPlrtyhPKLSRQEVK-DRVKAMMLKVGLlpnlINR---YPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|.
gi 489524673 171 NLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-211 |
3.22e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.47 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVD----RPTSGKVYINDVDIYNLKT 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDlaifRRRNIGliyqfYNLIPVLNVKENILLPAELDNRDI---------DGEYFD----------DLMETLGLIDRE-- 135
Cdd:PRK15093 81 RE----RRKLVG-----HNVSMIFQEPQSCLDPSERVGRQLmqnipgwtyKGRWWQrfgwrkrraiELLHRVGIKDHKda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 136 -KHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRI 211
Cdd:PRK15093 152 mRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKI 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-220 |
5.22e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.07 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY-GKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaif 82
Cdd:PRK11176 342 IEFRNVTFTYpGKEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLipvLN--VKENILLPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQ--------LSGGQQQRTSI 152
Cdd:PRK11176 416 -RNQVALVSQNVHL---FNdtIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAI 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALD-ELQK-NRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-201 |
6.58e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTS-----GKVYINDVDIYNlktKD 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE---RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFR-RRNIGLIYQFYNLIPvLNVKENILLPAEL----DNRDIDGeYFDDLMETLGLIDREKHLPNQ----LSGGQQQR 149
Cdd:PRK14258 81 VNLNRlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDD-IVESALKDADLWDEIKHKIHKsaldLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-217 |
9.56e-19 |
|
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: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPT---SGKVYINDVDiynLKTKDL 79
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSP---LKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFRRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEY------FDDLMETLGLIDREKHLP-NQLSGGQQQRTSI 152
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKN-MALQADRIISIEDG 217
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIR-DLKAHGVACVYISHKLNeVKAVCDTICVIRDG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
1.19e-18 |
|
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: 80.26 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVD--RPTSGKVYINDVDIYNLKTKDLAi 81
Cdd:cd03217 1 LEIKDLHVSVGGKEI----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLIYQFYNLIPVLNVKENIllpaeldnRDIDgEYFddlmetlglidrekhlpnqlSGGQQQRTSIGRALINRPS 161
Cdd:cd03217 76 --RLGIFLAFQYPPEIPGVKNADFL--------RYVN-EGF--------------------SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMA--LQADRIISIEDG-IIKS 221
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVIN-KLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGrIVKS 186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-217 |
1.42e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifr 83
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQFYNLIPVLNVKENILLpAELDNRDIDGEYFDD----------LMETLGL-IDREKHLPNqLSGGQQQRTSI 152
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYI-GRHLTKKVCGVNIIDwremrvraamMLLRVGLkVDLDEKVAN-LSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSkEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEV-DYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-217 |
1.51e-18 |
|
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: 83.91 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTK---SYGKnetkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDLAIf 82
Cdd:TIGR01257 931 VKNLVKifePSGR-----PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAV- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFD--DLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRP 160
Cdd:TIGR01257 1002 -RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 161 SIILADEPTGNLDSKNSKEILELLklsvKKY--NQTLIMITHDKNMA-LQADRIISIEDG 217
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLL----LKYrsGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-200 |
1.77e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLK-TKDLAIFRRRNigliyqfyNLIPVLNV 102
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYLGHRN--------AMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAEL---DNRDIdgeyfDDLMETLGLIDREkHLP-NQLSGGQQQRTSIGRALI-NRPSIILaDEPTGNLDSKNS 177
Cdd:PRK13539 91 AENLEFWAAFlggEELDI-----AAALEAVGLAPLA-HLPfGYLSAGQKRRVALARLLVsNRPIWIL-DEPTAALDAAAV 163
|
170 180
....*....|....*....|...
gi 489524673 178 KEILELLKLSVKKyNQTLIMITH 200
Cdd:PRK13539 164 ALFAELIRAHLAQ-GGIVIAATH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-223 |
1.82e-18 |
|
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: 80.27 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY------------------GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVY 65
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 66 IndvdiynlktkdlaifRRRNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIDgEYFDDLMETLGLIDReKHLP-NQ 141
Cdd:cd03220 81 V----------------RGRVSSLLGLGGGFNPELTGRENIYLNGRLlglSRKEID-EKIDEIIEFSELGDF-IDLPvKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 142 LSGGQQQRTSIGRALINRPSIILADEPTGNLDS----KNSKEILELLKLSVkkynqTLIMITHDKNMALQ-ADRIISIED 216
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAafqeKCQRRLRELLKQGK-----TVILVSHDPSSIKRlCDRALVLEK 217
|
....*..
gi 489524673 217 GIIKSDE 223
Cdd:cd03220 218 GKIRFDG 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
5.44e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDV-----DIYNLKtkDLAIFRRRnIGLIYQFYNLI 97
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrSIFNYR--DVLEFRRR-VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 98 PvLNVKENIL-------LPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTG 170
Cdd:PRK14271 114 P-MSIMDNVLagvrahkLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489524673 171 NLDSKNSKEILELLKLSVKKYnqTLIMITHdkNMAlQADRI 211
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTH--NLA-QAARI 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-217 |
1.18e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.99 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPT---SGKVYINDvdiynlktkDL 79
Cdd:NF040905 1 ILEMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDG---------EV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFR------RRNIGLIYQFYNLIPVLNVKENILLPAELDNRD-ID-GEYF---DDLMETLGLIDREKHLPNQLSGGQQQ 148
Cdd:NF040905 67 CRFKdirdseALGIVIIHQELALIPYLSIAENIFLGNERAKRGvIDwNETNrraRELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-219 |
1.77e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.32 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVyindvdiynlKTKDLAifr 83
Cdd:PRK15064 320 LEVENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENA--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 rrNIGLIYQFYNlipvlnvkenillpAELDNrDID---------GEYFDDLM--ETLGLI----DREKHLPNQLSGGQQQ 148
Cdd:PRK15064 383 --NIGYYAQDHA--------------YDFEN-DLTlfdwmsqwrQEGDDEQAvrGTLGRLlfsqDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDsknsKEILELLKLSVKKYNQTLIMITHDKNM--ALqADRIISI-EDGII 219
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD----MESIESLNMALEKYEGTLIFVSHDREFvsSL-ATRIIEItPDGVV 514
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-67 |
2.39e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYGKNETKVD------------------AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGK 63
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
....
gi 489524673 64 VYIN 67
Cdd:COG1134 83 VEVN 86
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-200 |
2.75e-17 |
|
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: 76.76 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKdlaifRRRNIGLIYQFYNLIPVLNVKEN 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-----IARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 106 ILLPAeldnRDIDGEYFDDLMETLGLIDREkHLP-NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDsKNSKEILELL 184
Cdd:cd03231 94 LRFWH----ADHSDEQVEEALARVGLNGFE-DRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVARFAEA 167
|
170
....*....|....*.
gi 489524673 185 KLSVKKYNQTLIMITH 200
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-211 |
3.11e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.79 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRP----TSGKVYINDVDIYNLKT 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KDLAIFRRRNIGLIYQ--FYNLIPVLNV----KENIllpaelDNRDIDGEYFD----------DLMETLGLIDREKHL-- 138
Cdd:COG4170 81 RERRKIIGREIAMIFQepSSCLDPSAKIgdqlIEAI------PSWTFKGKWWQrfkwrkkraiELLHRVGIKDHKDIMns 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 139 -PNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLklsvKKYNQ----TLIMITHDKNMALQ-ADRI 211
Cdd:COG4170 155 yPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLL----ARLNQlqgtSILLISHDLESISQwADTI 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-210 |
7.16e-17 |
|
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: 78.82 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiynlktkdlaifrRRNI 87
Cdd:TIGR03719 9 RVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP---------------GIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 88 GLIYQFYNLIPVLNVKENILLPAElDNRDIDGEY-------------FDDLMETLG----LIDREK-------------- 136
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVA-EIKDALDRFneisakyaepdadFDKLAAEQAelqeIIDAADawdldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 137 -HLP------NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSknskEILELLKLSVKKYNQTLIMITHDK----NMA 205
Cdd:TIGR03719 150 lRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDRyfldNVA 225
|
....*...
gi 489524673 206 ---LQADR 210
Cdd:TIGR03719 226 gwiLELDR 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-225 |
7.34e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.42 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPTSGKVYINDVDIYNLKTKDLAifRRRniGLIYQFYNLIPVLNVKEN 105
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELA--RHR--AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 106 ILL--PAELDNRDIDGEyFDDLMETLGLIDR-EKHLpNQLSGGQQQRTSIGRAL------IN-RPSIILADEPTGNLDsk 175
Cdd:COG4138 90 LALhqPAGASSEAVEQL-LAQLAEALGLEDKlSRPL-TQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLD-- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 176 nskeI---LELLKLsVKKYNQ---TLIMITHDKNMALQ-ADRIISIEDGII----KSDEVM 225
Cdd:COG4138 166 ----VaqqAALDRL-LRELCQqgiTVVMSSHDLNHTLRhADRVWLLKQGKLvasgETAEVM 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-217 |
1.20e-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: 78.41 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKT--------KDLAIFrrrniGLIYQFY 94
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTswimpgtiKDNIIF-----GLSYDEY 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 95 NLIPVLN---VKENILLPAELDNrdidgeyfDDLMEtlGLIdrekhlpnQLSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:TIGR01271 517 RYTSVIKacqLEEDIALFPEKDK--------TVLGE--GGI--------TLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489524673 172 LDSKNSKEILE--LLKLSVkkyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:TIGR01271 579 LDVVTEKEIFEscLCKLMS---NKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-184 |
1.73e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLAIFRRrnigliyqfyNLI------- 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQ----------DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 98 --PVLNVKENILLPAELdNRDIDGEYFDDLMETLGLIDREkHLP-NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDS 174
Cdd:PRK13538 85 ikTELTALENLRFYQRL-HGPGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170
....*....|
gi 489524673 175 KNSKEILELL 184
Cdd:PRK13538 163 QGVARLEALL 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-172 |
2.20e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYgkneTKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI--NDVDIYNLKTKDLA 80
Cdd:PRK10762 4 LLQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrrNIGLIYQFYNLIPVLNVKENILLPAELDNR--DIDGEYF----DDLMETLGLIDREKHLPNQLSGGQQQRTSIGR 154
Cdd:PRK10762 80 -----GIGIIHQELNLIPQLTIAENIFLGREFVNRfgRIDWKKMyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170
....*....|....*...
gi 489524673 155 ALINRPSIILADEPTGNL 172
Cdd:PRK10762 155 VLSFESKVIIMDEPTDAL 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-185 |
2.34e-16 |
|
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: 74.20 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvdRPTSGKVyinDVDIYnLKTKDLAIFRRRNIGLIYQFYNLIPVLNV 102
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI---TGEIL-INGRPLDKNFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELdnRDidgeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILE 182
Cdd:cd03232 97 REALRFSALL--RG-------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
...
gi 489524673 183 LLK 185
Cdd:cd03232 150 FLK 152
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-211 |
4.76e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSY-------GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLK 75
Cdd:PRK10261 313 ILQVRNLVTRFplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 76 TKDLAIFRRrNIGLIYQ--FYNLIPVLNVKENILLPAELDNRdIDGEYFDD----LMETLGLidREKH---LPNQLSGGQ 146
Cdd:PRK10261 393 PGKLQALRR-DIQFIFQdpYASLDPRQTVGDSIMEPLRVHGL-LPGKAAAArvawLLERVGL--LPEHawrYPHEFSGGQ 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknMALqADRI 211
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD--MAV-VERI 530
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-215 |
1.74e-15 |
|
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: 72.83 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 27 SLSVEKGTF-----IAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYnlktkdlaifrrrnigliYQFYNLIPVLN 101
Cdd:cd03237 14 TLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------------YKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 VKENILLPAELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEIL 181
Cdd:cd03237 76 GTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*
gi 489524673 182 ELLKLSVKKYNQTLIMITHDKNMA-LQADRIISIE 215
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIdYLADRLIVFE 190
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-217 |
5.87e-15 |
|
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: 70.82 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRRNIGLIYQFYNLIPVlNV 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELDNR-------------DIDGEYFDDLMEtLGlidrEKHLpnQLSGGQQQRTSIGRALINRPSIILADEPT 169
Cdd:cd03290 96 EENITFGSPFNKQrykavtdacslqpDIDLLPFGDQTE-IG----ERGI--NLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489524673 170 GNLDSKNSKEILE--LLKLsVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:cd03290 169 SALDIHLSDHLMQegILKF-LQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-219 |
8.35e-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: 73.06 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNETKvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLH-LLGGVDRpTSGKVYIndvdiynlktkdlaifrR 84
Cdd:TIGR00957 639 VHNATFTWARDLPP--TLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHM-----------------K 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQfYNLIPVLNVKENILLPAELDNRdidgeYFDDLMETLGLIDREKHLPN-----------QLSGGQQQRTSIG 153
Cdd:TIGR00957 699 GSVAYVPQ-QAWIQNDSLRENILFGKALNEK-----YYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 154 RALINRPSIILADEPTGNLDSKNSKEILE-------LLKlsvkkyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLK------NKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-210 |
1.63e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKSYGKNetKVdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiyNLKtkdlaifrrrnI 87
Cdd:PRK11819 11 RVSKVVPPK--KQ-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP----GIK-----------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 88 GLIYQFYNLIPVLNVKENIL--------LPAELDnrDI------DGEYFDDLMETLG----LIDREK------------- 136
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEegvaevkaALDRFN--EIyaayaePDADFDALAAEQGelqeIIDAADawdldsqleiamd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 137 --HLP------NQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSknskEILELLKLSVKKYNQTLIMITHDK----NM 204
Cdd:PRK11819 151 alRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHDRyfldNV 226
|
....*....
gi 489524673 205 A---LQADR 210
Cdd:PRK11819 227 AgwiLELDR 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-224 |
2.15e-14 |
|
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: 71.39 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTkSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLH-LLGGVDRPTSGKVYINDVDIyNLKTKDLA 80
Cdd:TIGR02633 256 VILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPV-DIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 IfrRRNIGLI---YQFYNLIPVLNVKENILLpAELDNRDIDGEyFDDLMEtLGLIDRE----------KHLP-NQLSGGQ 146
Cdd:TIGR02633 334 I--RAGIAMVpedRKRHGIVPILGVGKNITL-SVLKSFCFKMR-IDAAAE-LQIIGSAiqrlkvktasPFLPiGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKNMALQ-ADRIISIEDGIIKSDEV 224
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFV 486
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-216 |
2.74e-14 |
|
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: 67.95 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaiKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINdvdiynlktkdlaifR 83
Cdd:cd03223 1 IELENLSLATPDGRVLL---KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQF-YnlIPVLNVKENILLPaeldnrdidgeyFDDlmetlglidrekhlpnQLSGGQQQRTSIGRALINRPSI 162
Cdd:cd03223 63 GEDLLFLPQRpY--LPLGTLREQLIYP------------WDD----------------VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 163 ILADEPTGNLDSKNSKEILELLklsvKKYNQTLIMITHDKNMALQADRIISIED 216
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-201 |
6.03e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiynlktkdlaif 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQFYNLIPV--LNVKENILLPAELDNRDIdgeyfddlmetLGLIDREK--HLPNQ----LSGGQQQRTSIGR 154
Cdd:PRK09544 66 -KLRIGYVPQKLYLDTTlpLTVNRFLRLRPGTKKEDI-----------LPALKRVQagHLIDApmqkLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHD 201
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-169 |
6.70e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNlktkdlAIF 82
Cdd:NF033858 1 VARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYqfY-------NLIPVLNVKENI--------LLPAELDNRdIdgeyfDDLMETLGL---IDRekhlP-NQLS 143
Cdd:NF033858 71 RRAVCPRIA--YmpqglgkNLYPTLSVFENLdffgrlfgQDAAERRRR-I-----DELLRATGLapfADR----PaGKLS 138
|
170 180
....*....|....*....|....*.
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPT 169
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
6.76e-14 |
|
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: 69.12 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKV-------YINDVD-IYNLKTKDLAIFrrrniGLIYQFY 94
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisFSSQFSwIMPGTIKENIIF-----GVSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 95 ---NLIPVLNVKENILLPAELDNrdidgeyfdDLMETLGLIdrekhlpnqLSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:cd03291 128 rykSVVKACQLEEDITKFPEKDN---------TVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489524673 172 LDSKNSKEILE--LLKLSVkkyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:cd03291 190 LDVFTEKEIFEscVCKLMA---NKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-169 |
9.15e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGkNETKVDaikNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI--NDVDiynlkTKDLAIfrR 84
Cdd:NF033858 270 RGLTMRFG-DFTAVD---HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgQPVD-----AGDIAT--R 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQFYNLIPVLNVKENILLPAEL---DNRDIdGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPS 161
Cdd:NF033858 339 RRVGYMSQAFSLYGELTVRQNLELHARLfhlPAAEI-AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
....*...
gi 489524673 162 IILADEPT 169
Cdd:NF033858 418 LLILDEPT 425
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-217 |
1.10e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAifrrRNIGLIYQFYNLIPVLNVKEN 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 106 ILL---P---AELDNRDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKE 179
Cdd:PRK10575 106 VAIgryPwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 489524673 180 ILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGG 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-217 |
1.26e-13 |
|
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: 66.90 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdrpTSGKVYIN-DVDIYNLKTKDLAIF 82
Cdd:cd03233 6 WRNISFTTGKGRSKIPI--LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEgDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGLIYQFYNLIPVLNVKENILLPAELD-NRDIDGeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRPS 161
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRETLDFALRCKgNEFVRG----------------------ISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 162 IILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMIThdknmaLQA--------DRIISIEDG 217
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL------YQAsdeiydlfDKVLVLYEG 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-201 |
1.30e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIFRRR 85
Cdd:PRK15056 9 VNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 NIGLIYQFynliPVLnvKENILLPAELDN-------RDIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALIN 158
Cdd:PRK15056 86 SEEVDWSF----PVL--VEDVVMMGRYGHmgwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHD 201
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLR-ELRDEGKTMLVSTHN 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-184 |
1.40e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 33 GTFIAITGPSGSGKSTLLHLLGGVDRPTS--GKVYINDVDIynlkTKDlaIFRRrnIGLIYQFYNLIPVLNVKENIL--- 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQ--ILKR--TGFVTQDDILYPHLTVRETLVfcs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 108 ---LPAELdNRDIDGEYFDDLMETLGLIDREKHLPNQ-----LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKE 179
Cdd:PLN03211 166 llrLPKSL-TKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
....*
gi 489524673 180 ILELL 184
Cdd:PLN03211 245 LVLTL 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-222 |
1.57e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTkSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDR-PTSGKVYIN--DVDIYNLKTkd 78
Cdd:PRK13549 258 VILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDgkPVKIRNPQQ-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 lAIfrRRNIGLI---YQFYNLIPVLNVKENILLPAeLDnRDIDGEYFDDLMEtLGLIDRE-KHLP----------NQLSG 144
Cdd:PRK13549 335 -AI--AQGIAMVpedRKRDGIVPVMGVGKNITLAA-LD-RFTGGSRIDDAAE-LKTILESiQRLKvktaspelaiARLSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 145 GQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKyNQTLIMITHDKNMAL-QADRIISIEDGIIKSD 222
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLgLSDRVLVMHEGKLKGD 486
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-217 |
2.41e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.46 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaiKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDLAIFR 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRnIGLIYQFYNLIpvlnvkENILLPaelDNRDIDGEYFDDLMETLGLIDREKHLPN-----QLSGGQQQRTSIGRALIN 158
Cdd:PRK10522 397 KL-FSAVFTDFHLF------DQLLGP---EGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 159 RPSIILADEPTGNLDSKNSKEI-LELLKLsVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPL-LQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-221 |
4.19e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 1 MEILRVENLTKSYGknetkvDA--IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIndvdiynlkTKD 78
Cdd:PRK11147 1 MSLISIHGAWLSFS------DAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---------EQD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFR-----RRNI-GLIYQF--------------YNLIPVL--------NVKENILLPAELDNRDidGEYFD----DLM 126
Cdd:PRK11147 66 LIVARlqqdpPRNVeGTVYDFvaegieeqaeylkrYHDISHLvetdpsekNLNELAKLQEQLDHHN--LWQLEnrinEVL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 127 ETLGLiDREKHLpNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSknskEILELLKLSVKKYNQTLIMITHD----K 202
Cdd:PRK11147 144 AQLGL-DPDAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDrsfiR 217
|
250
....*....|....*....
gi 489524673 203 NMalqADRIISIEDGIIKS 221
Cdd:PRK11147 218 NM---ATRIVDLDRGKLVS 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-200 |
5.70e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 20 VDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVdiYNLKTKDLAIFRRRnIGLIYQ----FYN 95
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRSK-IGVVSQdpllFSN 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 96 LIPVlNVKENILLPAELD------NRDIDGEY----------------FDDLMETL---GLIDREKH------------- 137
Cdd:PTZ00265 475 SIKN-NIKYSLYSLKDLEalsnyyNEDGNDSQenknkrnscrakcagdLNDMSNTTdsnELIEMRKNyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 138 -----------LPNQ-----------LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTL 195
Cdd:PTZ00265 554 kkvlihdfvsaLPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
....*
gi 489524673 196 IMITH 200
Cdd:PTZ00265 634 IIIAH 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-219 |
8.71e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNL---KTKDL 79
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 80 AIFrrrnigLIYQFYNLIPVLNVKENILLpaELDNRDIDGEYFDDLMETLGLidrekHLPNQLSGG-----QQQRTSIGR 154
Cdd:PRK15439 87 GIY------LVPQEPLLFPNLSVKENILF--GLPKRQASMQKMKQLLAALGC-----QLDLDSSAGslevaDRQIVEILR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 155 ALINRPSIILADEPTGNLDSKNS----KEILELLKLSVKkynqtLIMITHDKNMALQ-ADRIISIEDGII 219
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETerlfSRIRELLAQGVG-----IVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-225 |
1.07e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPTSGKVYINDVDIYNLKTKDLAIFRrrniGLIYQFYNLIPVLNVKEN 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 106 ILL--PAELDNRDIDGEyFDDLMETLGLIDR-EKHLpNQLSGGQQQRTSIGRALIN-RPSI------ILADEPTGNLDSK 175
Cdd:PRK03695 90 LTLhqPDKTRTEAVASA-LNEVAEALGLDDKlGRSV-NQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 176 NSKEILELLK------LSVkkynqtlIMITHDKNMAL-QADRIISIEDGII----KSDEVM 225
Cdd:PRK03695 168 QQAALDRLLSelcqqgIAV-------VMSSHDLNHTLrHADRVWLLKQGKLlasgRRDEVL 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-218 |
1.21e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLAIfrRRNIGLIYQ------FYNL 96
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQdpeqqiFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 97 IP--VLNVKENILLPAELDNRDIDgeyfddlmETLGLIDRE--KHLPNQ-LSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:PRK13638 95 IDsdIAFSLRNLGVPEAEITRRVD--------EALTLVDAQhfRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489524673 172 LDSKNSKEILELLKLSVKKYNQTLIMiTHDknmalqADRIISIEDGI 218
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIIS-SHD------IDLIYEISDAV 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-219 |
1.27e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSygknetkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKD-LAif 82
Cdd:PRK10762 258 LKVDNLSGP---------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLA-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrrnIGLIY-----QFYNLIPVLNVKENILLPA--ELDNRDIDGEYFDDLMETLGLID--------REKHLPNqLSGGQQ 147
Cdd:PRK10762 327 ----NGIVYisedrKRDGLVLGMSVKENMSLTAlrYFSRAGGSLKHADEQQAVSDFIRlfniktpsMEQAIGL-LSGGNQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMAL-QADRIISIEDGII 219
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLgMSDRILVMHEGRI 473
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-212 |
1.42e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHllggvdrPTSGKVYINDVDIYNLKTKDLaif 82
Cdd:PTZ00265 1225 HIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDL--- 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrRNIGLIYQFYNLIPVLNVKENILLPAELDNRD-----IDGEYFDDLMETLglidrekhlPNQ-----------LSGGQ 146
Cdd:PTZ00265 1295 --RNLFSIVSQEPMLFNMSIYENIKFGKEDATREdvkraCKFAAIDEFIESL---------PNKydtnvgpygksLSGGQ 1363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSkNSKEILELLKLSVK-KYNQTLIMITHDKNMALQADRII 212
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKTIVDIKdKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
1.51e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTksyGKNETKVdaiKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDI-----YNLKTK 77
Cdd:PRK09700 265 VFEVRNVT---SRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspLDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIF--RRRNIGLIYQFynlipvlNVKENILLPAELDNRDIDGEY--FDDLMETLGLIDREKHLP----------NQLS 143
Cdd:PRK09700 339 GMAYIteSRRDNGFFPNF-------SIAQNMAISRSLKDGGYKGAMglFHEVDEQRTAENQRELLAlkchsvnqniTELS 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQA-DRIISIEDGIIKS 221
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-173 |
1.78e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 12 SYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVyinDVDIYNLKTKDlaifRRRNIGLIY 91
Cdd:PRK13543 18 AFSRNEEPV--FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---QIDGKTATRGD----RSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 92 QFYNLIPVLNVKENILLPAELDNRDIDgEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAK-QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
..
gi 489524673 172 LD 173
Cdd:PRK13543 168 LD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-221 |
1.88e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvdRP----TSGKVYINDVDIYNLKTKD 78
Cdd:CHL00131 7 ILEIKNLHASVNENEI----LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAifrRRNIGLIYQFYNLIP----------VLNVKENILLPAELDNRdidgEYFDDLMETLGLIDREKHLPNQ-----LS 143
Cdd:CHL00131 81 RA---HLGIFLAFQYPIEIPgvsnadflrlAYNSKRKFQGLPELDPL----EFLEIINEKLKLVGMDPSFLSRnvnegFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 144 GGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMA--LQADRIISIEDG-IIK 220
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLdyIKPDYVHVMQNGkIIK 232
|
.
gi 489524673 221 S 221
Cdd:CHL00131 233 T 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-219 |
5.03e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKsygknetkvDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDlaif 82
Cdd:PRK15439 268 VLTVEDLTG---------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ---- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYqfynlipvlnvkenilLPaelDNRDIDGEYFDD---------LMETLGLIDREKHL--------------- 138
Cdd:PRK15439 335 -RLARGLVY----------------LP---EDRQSSGLYLDAplawnvcalTHNRRGFWIKPAREnavleryrralnikf 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 139 --PNQ----LSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRI 211
Cdd:PRK15439 395 nhAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIR-SIAAQNVAVLFISSDLEEIEQmADRV 473
|
....*...
gi 489524673 212 ISIEDGII 219
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-200 |
1.05e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 2 EILRVENLTKSYgkNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNlKTKDLai 81
Cdd:TIGR01257 1936 DILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 82 frRRNIGLIYQFYNLIPVLNVKENILLPAELdnRDIDGEYFDDL----METLGLIDREKHLPNQLSGGQQQRTSIGRALI 157
Cdd:TIGR01257 2011 --HQNMGYCPQFDAIDDLLTGREHLYLYARL--RGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489524673 158 NRPSIILADEPTGNLDSKnSKEILELLKLSVKKYNQTLIMITH 200
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQ-ARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
1.06e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvDRPTS---------GKVYINDVDIYNLKTKDLAifRRRNIgLIYQF 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLA--RLRAV-LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 94 YNLIPvLNVKENILL--------PAELDNRDidGEYFDDLMETLG---LIDREKhlpNQLSGGQQQRTSIGRAL------ 156
Cdd:PRK13547 93 QPAFA-FSAREIVLLgrypharrAGALTHRD--GEIAWQALALAGataLVGRDV---TTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 157 ---INRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDGIIKSD 222
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-214 |
1.27e-11 |
|
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: 61.89 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLL---------------------HLLGGVDRPtsgkvyinDVD-IYNL------ 74
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKP--------DVDsIEGLspaiai 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 75 KTKDLAIFRRRNIGLIYQFYNLIPVLNVKENILlpaeldNRDidgeyfdDLMETLGL----IDREKhlpNQLSGGQQQR- 149
Cdd:cd03270 83 DQKTTSRNPRSTVGTVTEIYDYLRLLFARVGIR------ERL-------GFLVDVGLgyltLSRSA---PTLSGGEAQRi 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 150 ---TSIGRALINrpSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISI 214
Cdd:cd03270 147 rlaTQIGSGLTG--VLYVLDEPSIGLHPRDNDRLIETLK-RLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-185 |
1.50e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvdRPTSGkvYINDVD-IYNLKTKDlAIFRRRnIGLIYQFYNLIPVLN 101
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG--VITGGDrLVNGRPLD-SSFQRS-IGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 VKENIL------LPAELDNRDIDgEYFDDLMETLGL---IDREKHLPNQ-LSGGQQQRTSIGRALINRP-SIILADEPTG 170
Cdd:TIGR00956 853 VRESLRfsaylrQPKSVSKSEKM-EYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPkLLLFLDEPTS 931
|
170
....*....|....*
gi 489524673 171 NLDSKNSKEILELLK 185
Cdd:TIGR00956 932 GLDSQTAWSICKLMR 946
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-219 |
2.83e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 17 ETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynl 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQ---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 97 IPVL---NVKENILL------PAELDNRDIDGEYFDDLMEtlglidrekhLPN-----------QLSGGQQQRTSIGRAL 156
Cdd:PRK10789 397 TPFLfsdTVANNIALgrpdatQQEIEHVARLASVHDDILR----------LPQgydtevgergvMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524673 157 INRPSIILADEPTGNLDSKNSKEILELLKLSVKKynQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
3.51e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKnetKVdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIND-VDI-YNLKTKDla 80
Cdd:TIGR03719 322 VIEAENLTKAFGD---KL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtVKLaYVDQSRD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrrrnigliyqfyNLIPVLNVKENI---LLPAELDNRDIDGEYFDDLMETLGlIDREKHLpNQLSGGQQQRTSIGRALI 157
Cdd:TIGR03719 396 --------------ALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNFKG-SDQQKKV-GQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489524673 158 NRPSIILADEPTGNLDSknskEILELLKLSVKKYNQTLIMITHDK 202
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDR 500
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-217 |
6.74e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlIPVL---NV 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQ----SPVLfsgTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELDNRDI----DGEYFDDLME--TLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKN 176
Cdd:PLN03232 1327 RFNIDPFSEHNDADLwealERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489524673 177 SKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PLN03232 1407 DSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-202 |
6.81e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSY-GKNetkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINdvdiynlkTK-DLAIF- 82
Cdd:PRK11147 322 MENVNYQIdGKQ-----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------TKlEVAYFd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIgliyqfynLIPVLNVKENIllpaeldnrdIDGEyfddlmETLGLIDREKHL----------PNQ-------LSGG 145
Cdd:PRK11147 389 QHRAE--------LDPEKTVMDNL----------AEGK------QEVMVNGRPRHVlgylqdflfhPKRamtpvkaLSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 146 QQQRTSIGRALInRPS--IILaDEPTGNLDSknskEILELLKLSVKKYNQTLIMITHDK 202
Cdd:PRK11147 445 ERNRLLLARLFL-KPSnlLIL-DEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDR 497
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-219 |
6.89e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIyNLKTKDLAIfrRRNIGLI---YQFYNLIPVLNV 102
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAI--RAGIMLCpedRKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAE--------LDNRDIDGEYFDDLMETLGLIDREKHLP-NQLSGGQQQRTSIGRALINRPSIILADEPTGNLD 173
Cdd:PRK11288 349 ADNINISARrhhlragcLINNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 174 SKNSKEILELLklsvkkYN-----QTLIMITHD--KNMALqADRIISIEDGII 219
Cdd:PRK11288 429 VGAKHEIYNVI------YElaaqgVAVLFVSSDlpEVLGV-ADRIVVMREGRI 474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-175 |
9.22e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 11 KSYGKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvdRPTSGkvYIN-DVDIYNLkTKDLAIFRRRNiGL 89
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEgDIRISGF-PKKQETFARIS-GY 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 90 IYQFYNLIPVLNVKENIL------LPAELDNRDiDGEYFDDLMETL---GLIDREKHLP--NQLSGGQQQRTSIGRALIN 158
Cdd:PLN03140 958 CEQNDIHSPQVTVRESLIysaflrLPKEVSKEE-KMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*..
gi 489524673 159 RPSIILADEPTGNLDSK 175
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDAR 1053
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-217 |
1.49e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 26 VSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlIPVL---NV 102
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQ----APVLfsgTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENIllpaeldnrDIDGEYFD-DLMETLglidREKHLPN------------------QLSGGQQQRTSIGRALINRPSII 163
Cdd:PLN03130 1330 RFNL---------DPFNEHNDaDLWESL----ERAHLKDvirrnslgldaevseageNFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 164 LADEPTGNLDSKN----SKEILELLKlsvkkyNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PLN03130 1397 VLDEATAAVDVRTdaliQKTIREEFK------SCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-204 |
1.81e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYindvdiYNLKTKdLAIFRRRNIG--------LIYQFYN 95
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVR-MAVFSQHHVDgldlssnpLLYMMRC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 96 LIPVLNVKenilLPAELDNRDIDGEYFDDLMETLglidrekhlpnqlSGGQQQRTSIGRALINRPSIILADEPTGNLDSK 175
Cdd:PLN03073 599 FPGVPEQK----LRAHLGSFGVTGNLALQPMYTL-------------SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180
....*....|....*....|....*....
gi 489524673 176 NSKEILELLKLsvkkYNQTLIMITHDKNM 204
Cdd:PLN03073 662 AVEALIQGLVL----FQGGVLMVSHDEHL 686
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-223 |
2.14e-10 |
|
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: 59.81 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSY-GKNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlKTKDLAIF 82
Cdd:COG4615 328 LELRGVTYRYpGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRnIGLIYQFYNLIPVLNVKENILLPAELdnrdidgeyfDDLMETLGL-----IDREKHLPNQLSGGQQQRTsigrALI 157
Cdd:COG4615 405 RQL-FSAVFSDFHLFDRLLGLDGEADPARA----------RELLERLELdhkvsVEDGRFSTTDLSQGQRKRL----ALL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 158 -----NRPsIILADE------P-------TgnldsknskEILELLKLSVKkynqTLIMITHDKNMALQADRIISIEDGII 219
Cdd:COG4615 470 valleDRP-ILVFDEwaadqdPefrrvfyT---------ELLPELKARGK----TVIAISHDDRYFDLADRVLKMDYGKL 535
|
....
gi 489524673 220 KSDE 223
Cdd:COG4615 536 VELT 539
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-222 |
2.81e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTS-------GKV-YINDVD-IYNLKTKDLAIFrrrniGLIYQ--- 92
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirGTVaYVPQVSwIFNATVRDNILF-----GSPFDper 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 93 FYNLIPVLNVKENI-LLPAeldnrdidgeyfDDLMEtLGlidrEKHLpnQLSGGQQQRTSIGRALINRPSIILADEPTGN 171
Cdd:PLN03130 710 YERAIDVTALQHDLdLLPG------------GDLTE-IG----ERGV--NISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489524673 172 LDSKNSKEILE-LLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:PLN03130 771 LDAHVGRQVFDkCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-217 |
3.80e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTksyGKNETkvdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKD---- 78
Cdd:PRK10982 250 ILEVRNLT---SLRQP---SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 ---LAIFRRRNIGlIY-----QFYNLIPvlNVKENILLPAELDNRDI--DGEYFDDLM--ETLGlidrEKHLPNQLSGGQ 146
Cdd:PRK10982 324 gfaLVTEERRSTG-IYayldiGFNSLIS--NIRNYKNKVGLLDNSRMksDTQWVIDSMrvKTPG----HRTQIGSLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 147 QQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGiTDRILVMSNG 467
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-197 |
6.54e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 15 KNETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLhllggvdRPTSGKVYINDVDI-----YNLKTKDlAIFRRRNIGL 89
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLL-------KTIASNTDGFHIGVegvitYDGITPE-EIKKHYRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 90 IY--QFYNLIPVLNVKENILLPAEL---DNR--DIDGEYF-----DDLMETLGL-IDREKHLPNQL----SGGQQQRTSI 152
Cdd:TIGR00956 141 VYnaETDVHFPHLTVGETLDFAARCktpQNRpdGVSREEYakhiaDVYMATYGLsHTRNTKVGNDFvrgvSGGERKRVSI 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489524673 153 GRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIM 197
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-214 |
7.35e-10 |
|
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: 55.83 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 32 KGTFIAITGPSGSGKSTLLhllggvdrptsgkvyindvdiynlktkdlaifrrRNIGLI--YQFYNLIPVLNVKENILLP 109
Cdd:cd03227 20 EGSLTIITGPNGSGKSTIL----------------------------------DAIGLAlgGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 110 AELdnrdidgeyfddlMETLGLIDrekhlpnQLSGGQQQRTSI----GRALINRPSIILADEPTGNLDSKNSKEILELLK 185
Cdd:cd03227 66 AVS-------------AELIFTRL-------QLSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170 180
....*....|....*....|....*....
gi 489524673 186 LSVKKYNQtLIMITHDKNMALQADRIISI 214
Cdd:cd03227 126 EHLVKGAQ-VIVITHLPELAELADKLIHI 153
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-222 |
1.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLH-LLGGVDRPTSGKVYIndvdiynlktkdlaifrRRNIGLIYQFyNLIPVLN 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-----------------RGSVAYVPQV-SWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 102 VKENILLPAELDN----RDIDGEYFDDLMETLGLIDR----EKHLpnQLSGGQQQRTSIGRALINRPSIILADEPTGNLD 173
Cdd:PLN03232 695 VRENILFGSDFESerywRAIDVTALQHDLDLLPGRDLteigERGV--NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489524673 174 SKNSKEILE-LLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:PLN03232 773 AHVAHQVFDsCMKDELK--GKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-220 |
1.85e-09 |
|
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: 56.40 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLH-LLGGVDrpTSGKVYINDVDIYNLKTKDLaifrR 84
Cdd:cd03289 5 VKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 85 RNIGLIYQfynlipvlnvKENILLPAELDNRDIDGEYFDD----LMETLGLIDREKHLPNQ-----------LSGGQQQR 149
Cdd:cd03289 77 KAFGVIPQ----------KVFIFSGTFRKNLDPYGKWSDEeiwkVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 150 TSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-206 |
2.02e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlkTKDLAIFRRRnIGLIYQFYNLIPVLNV 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ-LCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELDNRDIDGEYFDDLMETLGLIDREKHLpnqLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILE 182
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|....
gi 489524673 183 llKLSVKKYNQTLIMITHDKNMAL 206
Cdd:PRK13540 169 --KIQEHRAKGGAVLLTSHQDLPL 190
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-214 |
8.04e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 19 KVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGgvdrPTSGKVYINdvdiynlktKDLAIFRRRNIGLIYQFYNLIp 98
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLI---------SFLPKFSRNKLIFIDQLQFLI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 99 vlnvkenillpaeldnrDIDGEYFddlmeTLGLIdrekhlPNQLSGGQQQRTSIGRALINRP--SIILADEPTGNLDSKN 176
Cdd:cd03238 73 -----------------DVGLGYL-----TLGQK------LSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 489524673 177 SKEILELLKLSVKKYNqTLIMITHDKNMALQADRIISI 214
Cdd:cd03238 125 INQLLEVIKGLIDLGN-TVILIEHNLDVLSSADWIIDF 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-220 |
1.01e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIndvdiynlktkdlaifrRRNIGLIYQfYNLIPVLNV 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------------ERSIAYVPQ-QAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 KENILLPAELDNRDI-----------DGEYFDDLMET-LGlidrEKHLpnQLSGGQQQRTSIGRALINRPSIILADEPTG 170
Cdd:PTZ00243 738 RGNILFFDEEDAARLadavrvsqleaDLAQLGGGLETeIG----EKGV--NLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 171 NLDSKNSKEILE---LLKLSVKkynqTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:PTZ00243 812 ALDAHVGERVVEecfLGALAGK----TRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-217 |
1.04e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 20 VDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIyNLKTKDLAIfrRRNIGLIYQFYNLIPV 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEAL--ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 100 LNVKENILL---PAELDNRDIDGEYFD--DLMETLGL-IDREKHLPNqLSGGQQQRTSIGRALINRPSIILADEPTGNLD 173
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDtkAIFDELDIdIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489524673 174 SKNSKEILELLKlSVKKYNQTLIMITHDKNMALQ-ADRIISIEDG 217
Cdd:PRK10982 167 EKEVNHLFTIIR-KLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-220 |
1.40e-08 |
|
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: 54.53 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 6 VENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVdRPTSGKVYINDV--DIYNLKTkdlaifR 83
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVswNSVTLQT------W 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 84 RRNIGLIYQfynlipvlnvKENILLPAELDNRDIDGEYFDD----LMETLGLIDREKHLPNQ-----------LSGGQQQ 148
Cdd:TIGR01271 1291 RKAFGVIPQ----------KVFIFSGTFRKNLDPYEQWSDEeiwkVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524673 149 RTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLECQQFLVIEGSSVK 1430
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
1.47e-08 |
|
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: 54.57 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlipvlnv 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQ---------- 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 103 kENILLPAELD-NRDIDGEYFDD----LMETLGLIDREKHLPNQ-----------LSGGQQQRTSIGRALINRPSIILAD 166
Cdd:TIGR00957 1368 -DPVLFSGSLRmNLDPFSQYSDEevwwALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 167 EPTGNLDSKNSKEILELLKLSVKkyNQTLIMITHDKNMALQADRIISIEDGIIK 220
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-200 |
2.23e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGvDRPTSgkvYINDVDIYNlktkdlaifRRR-----------NIGLIY 91
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG---YSNDLTLFG---------RRRgsgetiwdikkHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 92 QFYNL-----IPVLNVkenillpaeldnrdIDGEYFDdlmeTLGLI----DREKHLPNQ------------------LSG 144
Cdd:PRK10938 343 SSLHLdyrvsTSVRNV--------------ILSGFFD----SIGIYqavsDRQQKLAQQwldilgidkrtadapfhsLSW 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524673 145 GQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITH 200
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-215 |
2.38e-08 |
|
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: 52.22 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 37 AITGPSGSGKSTLLH-----LLGgvDRPTSGKVYINDVDIYNLKTKDLAI---FRRRNIGLiyqfYNLIPVLNVKENILL 108
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyaLTG--ELPPNSKGGAHDPKLIREGEVRAQVklaFENANGKK----YTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 109 PAEldnrdidGEYFDDLMETLGlidrekhlpnQLSGGQQQ------RTSIGRALINRPSIILADEPTGNLDSKNSKE-IL 181
Cdd:cd03240 100 CHQ-------GESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLA 162
|
170 180 190
....*....|....*....|....*....|....
gi 489524673 182 ELLKLSVKKYNQTLIMITHDKNMALQADRIISIE 215
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-219 |
2.71e-08 |
|
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: 52.60 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKNETKVdaIKNVSLSVEKGTFIAITGPSGSGKSTL-LHLLGGVDRpTSGKVYINDVDIYNLKTKDLaif 82
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rRRNIGLIYQfynlIPVLnVKENILLPAELDNRDIDGEYFDDLmETLGLIDREKHLPNQL-----------SGGQQQRTS 151
Cdd:cd03288 94 -RSRLSIILQ----DPIL-FSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 152 IGRALINRPSIILADEPTGNLDSKnSKEILELLKLSVKKyNQTLIMITHDKNMALQADRIISIEDGII 219
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFA-DRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-212 |
3.30e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGknetkvdaikNVSLSVEKGTF-----IAITGPSGSGKSTLLHLLGGVDRPTSGKVYInDVDI-----YnLKT 76
Cdd:PRK13409 344 PDLTKKLG----------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKIsykpqY-IKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 77 KdlaifrrrnigliyqfYNlIPVLNVKENIllpaeldNRDIDGEYFD-DLMETLGLIDREKHLPNQLSGGQQQRTSIGRA 155
Cdd:PRK13409 412 D----------------YD-GTVEDLLRSI-------TDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAAC 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNM-ALQADRII 212
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMiDYISDRLM 525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-212 |
3.58e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKSYGknetkvdaikNVSLSVEKGTF-----IAITGPSGSGKSTLLHLLGGVDRPTSGKVyINDVDI-----Ynlktk 77
Cdd:COG1245 346 DLTKSYG----------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKIsykpqY----- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 dlaifrrrniglIYQFYNLipvlNVKENIllpAELDNRDIDGEYF-DDLMETLGLiDR--EKHLPNqLSGGQQQRTSIGR 154
Cdd:COG1245 410 ------------ISPDYDG----TVEEFL---RSANTDDFGSSYYkTEIIKPLGL-EKllDKNVKD-LSGGELQRVAIAA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 155 ALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDknMALQ---ADRII 212
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD--IYLIdyiSDRLM 527
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
7.06e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 32 KGTFIAITGPSGSGKSTLLHLLGGvdrptsgkvyindvdiynlktkdlaIFRRRNIGLIYqfynlipvlnvkenillpae 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-------------------------ELGPPGGGVIY-------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 112 ldnrdIDGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSV--- 188
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180 190
....*....|....*....|....*....|...
gi 489524673 189 --KKYNQTLIMITHDKnMALQADRIISIEDGII 219
Cdd:smart00382 111 lkSEKNLTVILTTNDE-KDLGPALLRRRFDRRI 142
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-222 |
9.32e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLTKSYGKnetkVDAIKNVSLSVEKGTFIAITGPSGSG--KSTLLHLLGGVD---RPTSGKVYINDVDIYNlktKD 78
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRALR---RT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 79 LAIFRRRNIGLIYQFYNlipvlnvKENILL---PAELDNRDIDGEYfDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRA 155
Cdd:NF000106 87 IG*HRPVR*GRRESFSG-------RENLYMigr*LDLSRKDARARA-DELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 156 LINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMALQADRIISIEDGIIKSD 222
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-175 |
1.43e-07 |
|
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: 50.44 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 10 TKSYGKNETKVDAIKnvslSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIND-----VDIY----------NL 74
Cdd:cd03236 7 VHRYGPNSFKLHRLP----VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeiLDEFrgselqnyftKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 75 KTKDLAIFRRRnigliyQFYNLIPVlNVKENILlpaELDNRDIDGEYFDDLMETLGL---IDREKhlpNQLSGGQQQRTS 151
Cdd:cd03236 83 LEGDVKVIVKP------QYVDLIPK-AVKGKVG---ELLKKKDERGKLDELVDQLELrhvLDRNI---DQLSGGELQRVA 149
|
170 180
....*....|....*....|....
gi 489524673 152 IGRALINRPSIILADEPTGNLDSK 175
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIK 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-68 |
1.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 1.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524673 2 EILRVENLTKSYGKnetKVdAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYIND 68
Cdd:PRK11819 323 KVIEAENLSKSFGD---RL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-215 |
2.92e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKV------------------------YINDVDI-YNLKTK 77
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalpqpaleYVIDGDReYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 78 DLAIFRRRNIGliyqfyNLIPVLNVKENILLPAELDNRDidgeyfDDLMETLGLIDREKHLP-NQLSGGQQQRTSIGRAL 156
Cdd:PRK10636 97 QLHDANERNDG------HAIATIHGKLDAIDAWTIRSRA------ASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 157 INRPSIILADEPTGNLDsknsKEILELLKLSVKKYNQTLIMITHDKN-MALQADRIISIE 215
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDfLDPIVDKIIHIE 220
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-178 |
7.02e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 38 ITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKtKDLAIFRRRNIGLIYQfynlipvLNVKENILLPAELDNrdi 117
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIGHNLGLKLE-------MTVFENLKFWSEIYN--- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 118 DGEYFDDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSK 178
Cdd:PRK13541 100 SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-204 |
7.30e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNeTKVDAIKnvsLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVyindvdiynlktkDLAif 82
Cdd:PRK10636 312 LLKMEKVSAGYGDR-IILDSIK---LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLA-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 rrRNIGLIYQFYNLIPVLNVKENillPAELDNRDIDGEYFDDLMETLGLI----DREKHLPNQLSGGQQQRTSIGRALIN 158
Cdd:PRK10636 373 --KGIKLGYFAQHQLEFLRADES---PLQHLARLAPQELEQKLRDYLGGFgfqgDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489524673 159 RPSIILADEPTGNLDSKNSKEILELLklsvKKYNQTLIMITHDKNM 204
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEAL----IDFEGALVVVSHDRHL 489
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-197 |
1.21e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 8 NLTKsygknETKVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGG----------------------VDRPTSGKVY 65
Cdd:PLN03140 171 NLAK-----KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkldpslkvsgeityngyrlnefVPRKTSAYIS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 66 INDVDIYNLKTKDLAIFRRRNIGLIYQfYNLIPVLNVKEN---ILLPAELD-------NRDIDGEYFDDL-METLGL-ID 133
Cdd:PLN03140 246 QNDVHVGVMTVKETLDFSARCQGVGTR-YDLLSELARREKdagIFPEAEVDlfmkataMEGVKSSLITDYtLKILGLdIC 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524673 134 REKHLPNQL----SGGQQQRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKLSVKKYNQTLIM 197
Cdd:PLN03140 325 KDTIVGDEMirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-51 |
1.37e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 1.37e-06
10 20
....*....|....*....|....*...
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTLLH 51
Cdd:COG0178 622 KNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-219 |
1.43e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIYNLKTKDLaifrRRNIGLIYQfynlIPVL-- 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQ----DPVLfd 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 101 -NVKENI--LLPAEldnrdiDGEYFDDLmETLGL----------ID-REKHLPNQLSGGQQQRTSIGRALINRPS-IILA 165
Cdd:PTZ00243 1398 gTVRQNVdpFLEAS------SAEVWAAL-ELVGLrervasesegIDsRVLEGGSNYSVGQRQLMCMARALLKKGSgFILM 1470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 166 DEPTGNLDSKNSKEILELLKLSVKKYnqTLIMITHDKNMALQADRIISIEDGII 219
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
1.83e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 1.83e-06
10 20
....*....|....*....|....*....
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLH 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-51 |
1.84e-06 |
|
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: 48.09 E-value: 1.84e-06
10 20
....*....|....*....|....*....
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLH 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-215 |
2.98e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 7 ENLTKSYGknetkvDAIKNVSLS-VEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDVDIynlktkdlaifrrr 85
Cdd:cd03222 4 PDCVKRYG------VFFLLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 86 niglIYQfynlipvlnvkenillPAELDnrdidgeyfddlmetlglidrekhlpnqLSGGQQQRTSIGRALINRPSIILA 165
Cdd:cd03222 64 ----VYK----------------PQYID----------------------------LSGGELQRVAIAAALLRNATFYLF 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489524673 166 DEPTGNLDSKNSKEILELLKLSVKKYNQTLIMITHDKNMA-LQADRIISIE 215
Cdd:cd03222 96 DEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLdYLSDRIHVFE 146
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-200 |
5.59e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 3 ILRVENLTKSYGKNETkvdaIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVD--RPTSGKVYINDVDIYNLKTKDLA 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 81 ifrRRNIGLIYQFYNLIPvlNVKENILLPAEL-------DNRDIDGEYFDDLME-TLGLIDREKHLPNQ-----LSGGQQ 147
Cdd:PRK09580 77 ---GEGIFMAFQYPVEIP--GVSNQFFLQTALnavrsyrGQEPLDRFDFQDLMEeKIALLKMPEDLLTRsvnvgFSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489524673 148 QRTSIGRALINRPSIILADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITH 200
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVN-SLRDGKRSFIIVTH 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-210 |
5.67e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.67 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGV--------DRPTSGKVY------------INDVDIYNLKTKDlaiF 82
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFyvpqrpymtlgtLRDQIIYPDSSED---M 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 83 RRRNIGliyqfynlipvlnvkeNILLPAELDNRDIDgeyfdDLMETLGLIDREKHLPNQLSGGQQQRTSIGRALINRPSI 162
Cdd:TIGR00954 545 KRRGLS----------------DKDLEQILDNVQLT-----HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489524673 163 ILADEPTGNLDSKNSKEILELLklsvKKYNQTLIMITHDK------NMALQADR 210
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKslwkyhEYLLYMDG 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-49 |
6.49e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 6.49e-06
10 20
....*....|....*....|....*.
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTL 49
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-51 |
7.83e-06 |
|
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: 45.68 E-value: 7.83e-06
10 20
....*....|....*....|....*....
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTLLH 51
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-66 |
1.00e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 1.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489524673 22 AIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYI 66
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-217 |
3.67e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 140 NQLSGGQQQRTSIGRALINRPSII--LADEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISIEDG 217
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIK-KLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-64 |
5.76e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 5.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 5 RVENLTKSYGKNETkVDAIKNVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKV 64
Cdd:PRK13546 23 RMKDALIPKHKNKT-FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-214 |
1.35e-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: 42.31 E-value: 1.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489524673 140 NQLSGGQQQR----TSIGRALINRPSIIlaDEPTGNLDSKNSKEILELLKlSVKKYNQTLIMITHDKNMALQADRIISI 214
Cdd:TIGR00630 487 GTLSGGEAQRirlaTQIGSGLTGVLYVL--DEPSIGLHQRDNRRLINTLK-RLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-202 |
1.49e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 25 NVSLSVEKGTFIAITGPSGSGKSTLLHLLGGVDRPTSGKVYINDvdiyNLKtkdLAIFRRRNIGliYQFYNLIPVL---- 100
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP----NER---LGKLRQDQFA--FEEFTVLDTVimgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 101 ----NVKEN---ILLPAELDNRD------IDGEY--FD---------DLMETLGlIDREKH--LPNQLSGGQQQRTSIGR 154
Cdd:PRK15064 90 telwEVKQErdrIYALPEMSEEDgmkvadLEVKFaeMDgytaearagELLLGVG-IPEEQHygLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489524673 155 ALINRPSIILADEPTGNLDSkNSKEILELLklsVKKYNQTLIMITHDK 202
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDI-NTIRWLEDV---LNERNSTMIIISHDR 212
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-49 |
1.66e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 1.66e-04
10 20
....*....|....*....|....*.
gi 489524673 24 KNVSLSVEKGTFIAITGPSGSGKSTL 49
Cdd:PRK00349 17 KNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-214 |
3.87e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 128 TLGLidreKHLP-----NQLSGGQQQRTSIGRALIN---RPSIILADEPTGNLDSKNSKEILELLkLSVKKYNQTLIMIT 199
Cdd:PRK00635 795 SLGL----DYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVL-QSLTHQGHTVVIIE 869
|
90
....*....|....*
gi 489524673 200 HDKNMALQADRIISI 214
Cdd:PRK00635 870 HNMHVVKVADYVLEL 884
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-49 |
4.16e-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: 40.77 E-value: 4.16e-04
10 20
....*....|....*....|....*..
gi 489524673 23 IKNVSLSVEKGTFIAITGPSGSGKSTL 49
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-203 |
4.42e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524673 133 DREKHLPNQLSGGQQQRTSIGRALINRPSIILADEPTGNLDsknsKEILELLKLSVKKYNQTLIMITHDKN 203
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSHARE 402
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-212 |
5.36e-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: 40.77 E-value: 5.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524673 142 LSGGQQQRTSIGRALINR---PSIILADEPTGNLDSKNSKEILELLKLSVKKYNqTLIMITHDKNMALQADRII 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYII 902
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
30-139 |
1.44e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 38.52 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 30 VEKGTFIAITGPSGSGKSTLL-----------HLLGGVDRPTSGKVYINDVDIynlktkDLAIFRRRnigliyqfynlip 98
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLAldlaaavatgkPWLGGPRVPEQGKVLYVSAEG------PADELRRR------------- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489524673 99 vlnvkeniLLPAELDNRDIDGEYFDDLMETLGLIDREKHLP 139
Cdd:pfam13481 91 --------LRAAGADLDLPARLLFLSLVESLPLFFLDRGGP 123
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
31-53 |
1.61e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 1.61e-03
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
32-53 |
2.61e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 37.36 E-value: 2.61e-03
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
35-53 |
2.72e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 37.49 E-value: 2.72e-03
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
35-53 |
3.19e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 3.19e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
37-50 |
5.23e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.23e-03
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
34-60 |
7.34e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 36.36 E-value: 7.34e-03
10 20 30
....*....|....*....|....*....|
gi 489524673 34 TFIAITGPSGSGKSTLLHLLG---GVDRPT 60
Cdd:COG0572 8 RIIGIAGPSGSGKTTFARRLAeqlGADKVV 37
|
|
| Tmk |
COG0125 |
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ... |
32-53 |
8.06e-03 |
|
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis
Pssm-ID: 439895 [Multi-domain] Cd Length: 206 Bit Score: 36.29 E-value: 8.06e-03
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-201 |
8.07e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 4 LRVENLtKSYgKNETKVDaiknvslsVEKGTFIaITGPSGSGKSTLLH----LLGGvdRPTSGKVYINDV---------- 69
Cdd:COG0419 5 LRLENF-RSY-RDTETID--------FDDGLNL-IVGPNGAGKSTILEairyALYG--KARSRSKLRSDLinvgseeasv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524673 70 ---------------------DIYNLKTKDL--AIFRRRNIGLIYQFYNLIPVLNVKENILLPAELDNRDIDGEYFDDLM 126
Cdd:COG0419 72 elefehggkryrierrqgefaEFLEAKPSERkeALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524673 127 ETLGlidrekhlPNQLSGGQQQRTSIGRALinrpSIILaDepTGNLDSKNSKEILELLKlsvkkynqTLIMITHD 201
Cdd:COG0419 152 GLDP--------IETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDALE--------ELAIITHV 203
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-60 |
8.26e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 8.26e-03
10 20 30
....*....|....*....|....*....|
gi 489524673 32 KGTFIAITGPSGSGKSTLL-HLLGGVDRPT 60
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLnALLPELVLAT 113
|
|
| |
