|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-256 |
5.26e-140 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 393.30 E-value: 5.26e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFS--LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL 83
Cdd:COG1116 1 MSAAapALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGKIKEIIQVPLTHPRH---KESEL 240
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDrelRTSPE 240
|
250
....*....|....*.
gi 375134789 241 LFGFRNQALNMLDHTA 256
Cdd:COG1116 241 FAALRAEILDLLREEA 256
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-230 |
3.27e-121 |
|
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: 344.46 E-value: 3.27e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQ 90
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFG 170
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 171 ALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGKIKEIIQVPL 230
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-222 |
5.15e-88 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 265.04 E-value: 5.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL-- 83
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 -KR--GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG3842 75 eKRnvGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRI 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-229 |
4.85e-85 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 254.02 E-value: 4.85e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLI 88
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGKIKEIIQVP 229
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELD 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-252 |
2.33e-84 |
|
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: 251.23 E-value: 2.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQEHRLLPWLTVFENIHLALE 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 110 ET--PLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRI 187
Cdd:TIGR01184 81 RVlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 188 WQHEKITMILVTHDIEEAVYLGDRVIVMSARPG-KIKEIIQVPLTHPRHKESEL----LFGFRNQALNML 252
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDRLEVVedpsYYDLRNEALYFL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-222 |
1.16e-82 |
|
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: 246.28 E-value: 1.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---GL 87
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 168 PFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-225 |
7.46e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 236.20 E-value: 7.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSfslLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDL-- 83
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN-----GRDLft 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 -----KR--GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:COG1118 69 nlpprERrvGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRIEQV 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-227 |
3.59e-75 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 227.62 E-value: 3.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSfSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG----- 80
Cdd:COG1136 1 MS-PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 -TDLKR---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:COG1136 80 lARLRRrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDiEEAVYLGDRVIVMsaRPGKIKEIIQ 227
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRL--RDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-222 |
5.60e-73 |
|
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: 221.98 E-value: 5.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMsaRPGKI 222
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIEL--RDGKI 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-225 |
1.76e-72 |
|
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: 221.34 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL-KR--GL 87
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhKRpvNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 168 PFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKIQQI 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-222 |
3.28e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 216.86 E-value: 3.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KRGL 87
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLppkDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 --IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG3839 78 amVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-225 |
4.96e-69 |
|
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: 216.44 E-value: 4.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KR-- 85
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI--TRLppqKRdy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH--GVIEQV 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-233 |
9.89e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 209.18 E-value: 9.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD---LKR--GL 87
Cdd:COG1125 4 FENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDpveLRRriGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGL--KGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 166 DEPFGALDAITRSHLQAELQRIwQHE-KITMILVTHDIEEAVYLGDRVIVMsaRPGKikeIIQV--P---LTHP 233
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRL-QRElGKTIVFVTHDIDEALKLGDRIAVM--REGR---IVQYdtPeeiLANP 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-250 |
4.20e-65 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 203.37 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSF-QRdqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIF 89
Cdd:PRK11247 13 LLLNAVSKRYgER-----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENIHLALEETPLTREERNLrvnehiEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLKGQWRDAALQAL------AAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 170 GALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEIIQVPLTHPRHKESELLFGFRNQAL 249
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI--EEGKIGLDLTVDLPRPRRRGSARLAELEAEVL 239
|
.
gi 375134789 250 N 250
Cdd:PRK11247 240 Q 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-229 |
2.57e-63 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 198.77 E-value: 2.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQEHRLLPWLTVFENIHLAL 108
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 109 EETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIW 188
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 375134789 189 QHEKITMILVTHDIEEAVYLGDRVIVMSARPGKIKEIIQVP 229
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLN 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-225 |
6.25e-63 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 196.57 E-value: 6.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---- 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQE--HRLLPWLTVFENIH--LALEETPLTREERNLRVNEHIEIVGL-KGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:cd03257 81 rkeiQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIVEE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-235 |
1.99e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 203.98 E-value: 1.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSF-QRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQ---TQIKGTDLKR 85
Cdd:COG1123 260 LLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdlTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -----GLIFQ--EHRLLPWLTVFENIHLALE-ETPLTREERNLRVNEHIEIVGL-KGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:COG1123 340 lrrrvQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEII---QVpLTHP 233
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVEDGpteEV-FANP 496
|
..
gi 375134789 234 RH 235
Cdd:COG1123 497 QH 498
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-225 |
2.04e-62 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 200.17 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KR 85
Cdd:PRK09452 13 PLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THVpaeNR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GL--IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:PRK09452 87 HVntVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIEQD 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-222 |
2.86e-62 |
|
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: 195.58 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---- 85
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG1127 81 rrriGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD--GKI 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-225 |
6.41e-62 |
|
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: 194.48 E-value: 6.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRdqntLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---GLIF 89
Cdd:cd03296 5 VRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENIHLALEETPLTRE----ERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK--GRIEQV 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-216 |
1.06e-60 |
|
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: 190.37 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQ- 90
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLVFQn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 -EHRLLPwLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:cd03225 84 pDDQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 170 GALDAITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-236 |
1.44e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 194.14 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQ---TQIKGTDLKR-- 85
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 163 LLLDEPFGALD-AITRSHLQAeLQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKE---IIQVpLTHPRHK 236
Cdd:COG1135 162 LLCDEATSALDpETTRSILDL-LKDINRELGLTIVLITHEMDVVRRICDRVAVLEN--GRIVEqgpVLDV-FANPQSE 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-235 |
1.75e-60 |
|
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: 191.17 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---- 85
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -GLIFQEHR--LLPWLTVFENIHLALEETPLTREERnlRVNEHIEIVGL-KGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:COG1124 81 vQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEIIQV--PLTHPRH 235
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVadLLAGPKH 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-233 |
2.97e-60 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 194.94 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 20 FQRDQNTLTVLDgINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILlnqtqIKGTDL----KRGLI------- 88
Cdd:COG4175 34 LEKTGQTVGVND-ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVL-----IDGEDItklsKKELRelrrkkm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 ---FQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG4175 108 smvFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLM 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGkikEIIQV--P---LTHP 233
Cdd:COG4175 188 DEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDG---RIVQIgtPeeiLTNP 255
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
13-225 |
4.95e-60 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 189.63 E-value: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN---QTQIKGTDLKRGLIF 89
Cdd:TIGR00968 3 IANISKRFGSFQ----ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNgqdATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 170 GALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN--GKIEQI 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
28-244 |
4.96e-60 |
|
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: 189.82 E-value: 4.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD---LKR--GLIFQEHRLLPWLTVFE 102
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpveLRRkiGYVIQQIGLFPHMTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHL--ALEETPltREERNLRVNEHIEIVGL--KGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRS 178
Cdd:cd03295 95 NIALvpKLLKWP--KEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 179 HLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpgkiKEIIQV--PLTHPRHKESELLFGF 244
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN-----GEIVQVgtPDEILRSPANDFVAEF 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-224 |
8.56e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 188.34 E-value: 8.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDLKR----- 85
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL--SRLKRreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -----GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG2884 77 lrrriGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 161 DILLLDEPFGALDAITRshlqaelQRIWQH-EKI-----TMILVTHDIEEAVYLGDRVIVMSArpGKIKE 224
Cdd:COG2884 157 ELLLADEPTGNLDPETS-------WEIMELlEEInrrgtTVLIATHDLELVDRMPKRVLELED--GRLVR 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-222 |
1.39e-59 |
|
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: 188.31 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLnkSFQRDQNTlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:COG1122 1 IELENL--SFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQ--EHRLL-PwlTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:COG1122 78 GLVFQnpDDQLFaP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 163 LLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDD--GRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-217 |
2.19e-59 |
|
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: 185.85 E-value: 2.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --GLIFQEHRLLPWLTVFENIHLALeetpltreernlrvnehieivglkgfekayphelSGGMAQRVAIARGLVNKPDIL 163
Cdd:cd03229 77 riGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
33-229 |
3.69e-59 |
|
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: 188.62 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---------GLIFQEHRLLPWLTVFEN 103
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAE 183
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 184 LQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI------KEIIQVP 229
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRLvqvgtpEEILTNP 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-225 |
8.42e-59 |
|
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: 185.54 E-value: 8.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KR-- 85
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLppkDRdi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND--GQIQQI 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-224 |
2.10e-58 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 185.48 E-value: 2.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---- 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:cd03258 81 rrriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKE 224
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEVVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-234 |
2.90e-58 |
|
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: 185.01 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDLKR-- 85
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ---GLIFQEHRLLPWLTVFENIHLAL-EETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:cd03261 77 rrmGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSAR----PGKIKEIIQVplTHPR 234
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGkivaEGTPEELRAS--DDPL 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-235 |
1.09e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 180.96 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI--KGTDLKR-- 85
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ---GLIFQEHRLLPWLTVFENIHLALEET-PLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:COG1126 77 rkvGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 162 ILLLDEPFGALD---------AITrshlqaELQRiwqhEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI---IQVp 229
Cdd:COG1126 157 VMLFDEPTSALDpelvgevldVMR------DLAK----EGMTMVVVTHEMGFAREVADRVVFMDG--GRIVEEgppEEF- 223
|
....*.
gi 375134789 230 LTHPRH 235
Cdd:COG1126 224 FENPQH 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-225 |
1.12e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.52 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSfslLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtQIKGTDLKR 85
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGTDVSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --------GLIFQEHRLLPWLTVFENIHLALeeTPLTREER------NLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVA 151
Cdd:PRK10851 69 lhardrkvGFVFQHYALFRHMTVFDNIAFGL--TVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ--GNIEQA 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-235 |
1.15e-56 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 183.72 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDY---DGEILLNQTQI---KGTDL 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLlklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KR------GLIFQE--HRLLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGL---KGFEKAYPHELSGGMAQRVA 151
Cdd:COG0444 81 RKirgreiQMIFQDpmTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITrshlQAE----LQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEIIQ 227
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTI----QAQilnlLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRIVEEGP 234
|
250
....*....|
gi 375134789 228 VP--LTHPRH 235
Cdd:COG0444 235 VEelFENPRH 244
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
45-225 |
4.61e-56 |
|
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: 182.31 E-value: 4.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 45 IVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLR 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 122 VNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHD 201
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 375134789 202 IEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:TIGR01187 161 QEEAMTMSDRIAIM--RKGKIAQI 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-215 |
4.41e-55 |
|
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: 176.33 E-value: 4.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIE---QGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI----KGTDL-----KRGLIFQEHRLLPW 97
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLppqqrKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 98 LTVFENIHLALEEtpLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITR 177
Cdd:cd03297 90 LNVRENLAFGLKR--KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 375134789 178 SHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-224 |
6.09e-55 |
|
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: 184.34 E-value: 6.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSfSLLSIKKLNKSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL---DQDYDGEILLNQTQIKGTD 82
Cdd:COG1123 1 MT-PLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 LKR-----GLIFQE--HRLLPwLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARG 155
Cdd:COG1123 78 EALrgrriGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 156 LVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKE 224
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVE 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-222 |
9.96e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.33 E-value: 9.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRdqntLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR----- 85
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-----GEDVARdpaev 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:COG1131 72 rrriGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-231 |
2.32e-53 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 176.95 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR---- 85
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-----GVDLSHvppy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:PRK11607 90 qrpiNMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS----ARPGKIKEIIQVPLT 231
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNrgkfVQIGEPEEIYEHPTT 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-222 |
1.78e-52 |
|
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: 169.63 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI--KGTDLKR--- 85
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINElrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --GLIFQEHRLLPWLTVFENIHLALEET-PLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 163 LLLDEPFGALDaitrSHLQAELQRIWQ---HEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03262 157 MLFDEPTSALD----PELVGEVLDVMKdlaEEGMTMVVVTHEMGFAREVADRVIFMDD--GRI 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
10-246 |
5.54e-52 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 172.57 E-value: 5.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQntltvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KRG 86
Cdd:NF040840 1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDI--TNLppeKRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 L--IFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:NF040840 74 IayVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 165 LDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEIIQVP--LTHPRHKESELLF 242
Cdd:NF040840 154 LDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIM--LNGRLSQVGDVRevFRRPKNEFVARFV 231
|
....
gi 375134789 243 GFRN 246
Cdd:NF040840 232 GFEN 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-235 |
6.90e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.91 E-value: 6.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQ---TQIKGTDLKR---- 85
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKELRKarrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:PRK11153 84 iGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 165 LDEPFGALD-AITRSHLQAeLQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKE---IIQVpLTHPRH 235
Cdd:PRK11153 164 CDEATSALDpATTRSILEL-LKDINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRLVEqgtVSEV-FSHPKH 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-222 |
9.19e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.70 E-value: 9.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDLKR 85
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -----GLIFQEHRLLPWLTVFENI-HLALEETPL--------TREERNlRVNEHIEIVGLKgfEKAY--PHELSGGMAQR 149
Cdd:COG3638 78 lrrriGMIFQQFNLVPRLSVLTNVlAGRLGRTSTwrsllglfPPEDRE-RALEALERVGLA--DKAYqrADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD--GRV 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-225 |
1.18e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 171.83 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILlnqtqIKGTDL-KRG- 86
Cdd:PRK11432 5 NFVVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-----IDGEDVtHRSi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 ------LIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:PRK11432 76 qqrdicMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK--GKIMQI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-224 |
2.17e-51 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 167.23 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR 85
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-----GQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --------------GLIFQEHRLLPWLTVFENIHLALEEtpltREERNL--RVNEHIEIVGLKGFEKAYPHELSGGMAQR 149
Cdd:COG4181 79 ldedararlrarhvGFVFQSFQLLPTLTALENVMLPLEL----AGRRDAraRARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLgDRVIVMSArpGKIKE 224
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARC-DRVLRLRA--GRLVE 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-214 |
3.99e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 166.47 E-value: 3.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDL------KRGL--IFQEHRLLPWLTVFENI 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-----GQDLtalppaERPVsmLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALeeTP---LTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQ 181
Cdd:COG3840 93 GLGL--RPglkLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190
....*....|....*....|....*....|...
gi 375134789 182 AELQRIWQHEKITMILVTHDIEEAVYLGDRVIV 214
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPEDAARIADRVLL 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
33-225 |
2.83e-49 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.97 E-value: 2.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KR--GLIFQEHRLLPWLTVFENIHLA 107
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVppaERgvGMVFQSYALYPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 108 LEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRI 187
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 375134789 188 WQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK11000 180 HKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
10-224 |
3.49e-49 |
|
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: 161.37 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---------KG 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssneraKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 TDLKRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLgDRVIVMsaRPGKIKE 224
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEM--KDGQLFN 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-246 |
5.24e-49 |
|
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: 161.35 E-value: 5.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL---KRGLIF--QEHRLLPWLTVFEN 103
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLppeKRDISYvpQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAE 183
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 184 LQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEI--IQVPLTHPRHKESELLFGFRN 246
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQVgkPEEVFKKPKNEFVAEFLGFNN 234
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
28-229 |
4.15e-48 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 162.86 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDyDGeiLLNQTQIKGTDL------KRGL--IFQEHRLLPWLT 99
Cdd:TIGR03258 19 TVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKA-AG--LTGRIAIADRDLthapphKRGLalLFQNYALFPHLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:TIGR03258 96 VEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 180 LQAELQRIwqHEK---ITMILVTHDIEEAVYLGDRVIVMS----ARPGKIKEIIQVP 229
Cdd:TIGR03258 176 MREEIAAL--HEElpeLTILCVTHDQDDALTLADKAGIMKdgrlAAHGEPQALYDAP 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-225 |
4.27e-48 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 162.32 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDLK---RG- 86
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEpadRDi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 -LIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:PRK11650 79 aMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG--GVAEQI 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-223 |
1.15e-47 |
|
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: 161.42 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDgINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN----QTQIKGTDL---KR--GLIFQEHRLLPWLTV 100
Cdd:COG4148 16 LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlQDSARGIFLpphRRriGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPltREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHL 180
Cdd:COG4148 95 RGNLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 375134789 181 QAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRVV 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-215 |
2.32e-46 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 153.80 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 15 KLNKSFQRDQNTLTVLDginLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---GLIFQE 91
Cdd:cd03298 2 RLDKIRFSYGEQPMHFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 172 LDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-222 |
3.84e-46 |
|
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: 153.33 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDLKR----------GLIFQEHRL 94
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV--SDLRGraipylrrkiGVVFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 95 LPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 375134789 175 ITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:cd03292 170 DTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIAL--ERGKL 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-218 |
6.03e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 152.64 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLnkSFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG-LDQD--YDGEILLNQTQIKG--TDLKR 85
Cdd:COG4136 2 LSLENL--TITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTAlpAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -GLIFQEHRLLPWLTVFENIHLALEETPlTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:COG4136 78 iGILFQDDLLFPHLSVGENLAFALPPTI-GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 165 LDEPFGALDAITRSHLqaelqRIW-----QHEKITMILVTHDIEEAVyLGDRVIVMSAR 218
Cdd:COG4136 157 LDEPFSKLDAALRAQF-----REFvfeqiRQRGIPALLVTHDEEDAP-AAGRVLDLGNW 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-217 |
6.86e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.28 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLnkSFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN---QTQIKGTDLKR-- 85
Cdd:COG4619 1 LELEGL--SFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkpLSAMPPPEWRRqv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPwLTVFENIhlaleetPLTREERNLRVNEHIEIVGLK--GFEKAY----PHELSGGMAQRVAIARGLVNK 159
Cdd:COG4619 77 AYVPQEPALWG-GTVRDNL-------PFPFQLRERKFDRERALELLErlGLPPDIldkpVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-213 |
1.19e-45 |
|
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: 151.61 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQrdqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQ------IKGTDLKR- 85
Cdd:TIGR03608 1 LKNISKKFG----DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtpplnsKKASKFRRe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:TIGR03608 77 klGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAvYLGDRVI 213
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVA-KQADRVI 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-222 |
2.06e-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 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: 153.38 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDLKR-----GLIFQ--EHRLLPw 97
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDlrkkvGLVFQfpEHQLFE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 98 LTVFENIHLALEETPLTREERNLRVNEHIEIVGLKG--FEKAyPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:TIGR04521 98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeyLERS-PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 176 TRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK--GKI 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-224 |
2.31e-45 |
|
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: 161.54 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEHR 93
Cdd:COG2274 480 SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqiGVVLQDVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 LLPwLTVFENIHLALEETPLTreernlRVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDI 162
Cdd:COG2274 560 LFS-GTIRENITLGDPDATDE------EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 163 LLLDEPFGALDAITRSHLQAELQRIWQheKITMILVTHDiEEAVYLGDRVIVMSArpGKIKE 224
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDK--GRIVE 689
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-225 |
4.28e-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: 152.20 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLnkSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL------LNQTQIKGTDLK 84
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 RGLIFQ--EHRLLPwLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:TIGR04520 79 VGMVFQnpDNQFVG-ATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 163 LLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVyLGDRVIVMSArpGKIKEI 225
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNK--GKIVAE 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-222 |
5.35e-45 |
|
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: 151.18 E-value: 5.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDLKR-- 85
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ---GLIFQEHRLLPWLTVFENI-HLALEETPL--------TREERnLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIA 153
Cdd:cd03256 78 rqiGMIFQQFNLIERLSVLENVlSGRLGRRSTwrslfglfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 154 RGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-222 |
7.02e-45 |
|
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: 148.70 E-value: 7.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK--GTDLKR--G 86
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkePEEVKRriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LIFQEHRLLPWLTVFENIhlaleetpltreernlrvnehieivglkgfekayphELSGGMAQRVAIARGLVNKPDILLLD 166
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 167 EPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03230 121 EPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-240 |
1.85e-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: 150.01 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRdqntLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---- 85
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 166 DEPFGALDAITRSHLQAELQRiWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEIIQVPLTHPRHKESEL 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLDELREEIGEENL 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-169 |
2.97e-44 |
|
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: 146.25 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEHRLLPWLTVFENI 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 105 HLALEETPLTREERNLRVNEHIEIVGLKGFEK----AYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-225 |
3.05e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 148.87 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDY-----DGEILLNQTQIKGTD--- 82
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDvdv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 --LKR--GLIFQEHRLLPwLTVFENIHLALE-ETPLTREERNLRVNEHIEIVGLKGFEK--AYPHELSGGMAQRVAIARG 155
Cdd:cd03260 77 leLRRrvGMVFQKPNPFP-GSIYDNVAYGLRlHGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 156 LVNKPDILLLDEPFGALDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLN--GRLVEF 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-215 |
3.57e-44 |
|
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: 146.76 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEhr 93
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAYVPQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 llPWL---TVFENIhlaleetpltreernlrvnehieivglkgfekaypheLSGGMAQRVAIARGLVNKPDILLLDEPFG 170
Cdd:cd03228 85 --PFLfsgTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 375134789 171 ALDAITRSHLQAELQRIwqHEKITMILVTHDIeEAVYLGDRVIVM 215
Cdd:cd03228 126 ALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-237 |
3.61e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.09 E-value: 3.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 14 KKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD-------LKRG 86
Cdd:PRK09493 5 KNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvderlirQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LIFQEHRLLPWLTVFENIHLA-LEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 166 DEPFGALDaitrSHLQAELQRIWQ---HEKITMILVTHDIEEAVYLGDRVIVMS----ARPGKIKEIIQVPLThPRHKE 237
Cdd:PRK09493 161 DEPTSALD----PELRHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDkgriAEDGDPQVLIKNPPS-QRLQE 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-222 |
5.70e-44 |
|
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: 149.04 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLnkSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLK----- 84
Cdd:COG1120 1 MLEAENL--SVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 RGLIFQEHRLLPWLTVFENI------HLALEETPlTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVN 158
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELValgrypHLGLFGRP-SAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 159 KPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-215 |
4.04e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.39 E-value: 4.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLnkSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIF 89
Cdd:COG1121 6 AIELENL--TVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QeHRLLPW---LTVFENI------HLALEEtPLTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG1121 82 Q-RAEVDWdfpITVRDVVlmgrygRRGLFR-RPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRiWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-225 |
5.70e-42 |
|
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: 146.41 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLTvLDgINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN----QTQIKGTDL---KR--GLIF 89
Cdd:TIGR02142 4 RFSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlFDSRKGIFLppeKRriGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENIHLALEETplTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 170 GALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVAAA 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-222 |
9.04e-42 |
|
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: 142.82 E-value: 9.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDL--- 83
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 --KRGLIFQEHRLLPWLTVFENI-HLALEETP--------LTREERnLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAI 152
Cdd:TIGR02315 78 rrRIGMIFQHYNLIERLTVLENVlHGRLGYKPtwrsllgrFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGL--KAGEI 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
30-217 |
1.86e-41 |
|
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: 141.23 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR-------------GLIFQEHRLLP 96
Cdd:TIGR02673 18 LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIA-----GEDVNRlrgrqlpllrrriGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 WLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:TIGR02673 93 DRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 375134789 177 RSHLQAELQRIWQHeKITMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:TIGR02673 173 SERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-225 |
2.21e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.79 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSF-------QRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---K 79
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 80 GTDLKR-----GLIFQEHR--LLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGLK-GFEKAYPHELSGGMAQRV 150
Cdd:COG4608 87 GRELRPlrrrmQMVFQDPYasLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 151 AIARGLVNKPDILLLDEPFGALDAITRSH-------LQAELqriwqheKITMILVTHDIeeAV--YLGDRVIVMSArpGK 221
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQvlnlledLQDEL-------GLTYLFISHDL--SVvrHISDRVAVMYL--GK 235
|
....
gi 375134789 222 IKEI 225
Cdd:COG4608 236 IVEI 239
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-215 |
2.30e-40 |
|
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: 136.61 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKRGLIFQE 91
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-----GKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLpwltvfenihlaleetpltreernlrvnehieivglkgfekAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:cd00267 72 RRRI-----------------------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 172 LDAITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd00267 111 LDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVL 153
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-247 |
2.67e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.50 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL-------------NQ 75
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 76 TQIKGTDLKRGLIFQEHRLLPWLTVFENI---HLALEETPltREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAI 152
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEP--KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMS----ARPGKIKEIIQV 228
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDqgriVEQGPAKALFAD 234
|
250
....*....|....*....
gi 375134789 229 PlTHPRHKesELLFGFRNQ 247
Cdd:PRK11264 235 P-QQPRTR--QFLEKFLLQ 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-215 |
4.56e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.10 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNT---LTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN-----QTQIKGTD 82
Cdd:PRK13637 1 MSIKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 LKR--GLIFQ--EHRLLPWlTVFENIHLALEETPLTREERNLRVNEHIEIVGLK--GFEKAYPHELSGGMAQRVAIARGL 156
Cdd:PRK13637 81 IRKkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
34-223 |
6.00e-39 |
|
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: 134.99 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 34 NLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR---GLIFQEHRLLPWLTVFENIHLALEE 110
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 111 TPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQH 190
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|...
gi 375134789 191 EKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQ--GKIK 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-219 |
7.21e-39 |
|
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: 134.58 E-value: 7.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQeHRLLPW---LTVFENI 104
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSIDRdfpISVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALE-----ETPLTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:cd03235 92 LMGLYghkglFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQED 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 375134789 180 LqAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARP 219
Cdd:cd03235 171 I-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-235 |
7.96e-39 |
|
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: 141.36 E-value: 7.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKS----TLLRLIAGLDQDYDGEILLNQTQIKGT 81
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 82 DLKR---------GLIFQE--HRLLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGLKGFE---KAYPHELSGGM 146
Cdd:COG4172 82 SERElrrirgnriAMIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 147 AQRVAIARGLVNKPDILLLDEPFGALDAITRSH---LQAELQRiwqHEKITMILVTHDieeavyLG------DRVIVMsa 217
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQildLLKDLQR---ELGMALLLITHD------LGvvrrfaDRVAVM-- 230
|
250 260
....*....|....*....|..
gi 375134789 218 RPGKIKEiiQVP----LTHPRH 235
Cdd:COG4172 231 RQGEIVE--QGPtaelFAAPQH 250
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-214 |
1.20e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.71 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 34 NLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN-QTQIKGTDLKR--GLIFQEHRLLPWLTVFENIHLALEe 110
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDHTTTPPSRRpvSMLFQENNLFSHLTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 111 tP---LTREERNLRvnEHI-EIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQR 186
Cdd:PRK10771 98 -PglkLNAAQREKL--HAIaRQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180
....*....|....*....|....*...
gi 375134789 187 IWQHEKITMILVTHDIEEAVYLGDRVIV 214
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-224 |
1.21e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 141.43 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT---QIKGTDLKRGLIFQEHRll 95
Cdd:COG4988 343 SFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsDLDPASWRRQIAWVPQN-- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 96 PWL---TVFENIHLALEEtpLTREErnlrVNEHIEIVGLKGFEKAYPHE-----------LSGGMAQRVAIARGLVNKPD 161
Cdd:COG4988 420 PYLfagTIRENLRLGRPD--ASDEE----LEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEkiTMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRL-ALLAQADRILVLDD--GRIVE 551
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-218 |
2.74e-38 |
|
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: 132.60 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLnkSFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK--GTDLKRGL 87
Cdd:COG4133 2 MLEAENL--SCRRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHR--LLPWLTVFENIHL--ALEETPLTREernlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:COG4133 78 AYLGHAdgLKPELTVRENLRFwaALYGLRADRE----AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRiWQHEKITMILVTHDieEAVYLGDRVIVMSAR 218
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ--PLELAAARVLDLGDF 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-223 |
1.49e-37 |
|
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: 131.47 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKgTDLKR----- 85
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAarqsl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQeHRLLPW-LTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:cd03263 78 GYCPQ-FDALFDeLTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 165 LDEPFGALDAITRSHLQAELQRIwQHEKiTMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEALCDRIAIMSD--GKLR 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-228 |
1.60e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 135.93 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 14 KKLNKSFQRDQNTLTV-LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI-KGTDL-------- 83
Cdd:PRK10070 27 QGLSKEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAelrevrrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpgkiKEIIQV 228
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQV 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-235 |
3.13e-37 |
|
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: 137.12 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSF-------QRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTD 82
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 ------LKRGL--IFQE--HRLLPWLTVFENIH--LALEETPLTREERNLRVNEHIEIVGLK-GFEKAYPHELSGGMAQR 149
Cdd:COG4172 354 rralrpLRRRMqvVFQDpfGSLSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDaitRShLQAE----LQRIWQHEKITMILVTHDIeeAV--YLGDRVIVMsaRPGKIK 223
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALD---VS-VQAQildlLRDLQREHGLAYLFISHDL--AVvrALAHRVMVM--KDGKVV 505
|
250
....*....|....*.
gi 375134789 224 EiiQVP----LTHPRH 235
Cdd:COG4172 506 E--QGPteqvFDAPQH 519
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-225 |
6.02e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 6.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNksFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGT---D 82
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 LKR--GLIFQEhrllP-----WLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARG 155
Cdd:PRK13635 79 VRRqvGMVFQN----PdnqfvGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 156 LVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMsaRPGKIKEI 225
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEILEE 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-205 |
6.74e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 129.94 E-value: 6.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG----- 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 -TDLKR---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:PRK11629 81 kAELRNqklGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEA 205
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-224 |
7.82e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSfslLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI--------LLNQTQ 77
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 78 IK-GTDLKR--GLIFQEHRLLPWLTVFENihlaLEETP-----LTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQR 149
Cdd:PRK11124 74 DKaIRELRRnvGMVFQQYNLWPHLTVQQN----LIEAPcrvlgLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDA-ITrshlqAELQRI---WQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKE 224
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPeIT-----AQIVSIireLAETGITQVIVTHEVEVARKTASRVVYMEN--GHIVE 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-224 |
2.15e-36 |
|
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: 135.28 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK---GTDLKR--GLIFQEhr 93
Cdd:COG4987 340 SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldEDDLRRriAVVPQR-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 llPWL---TVFENIHLALEEtpLTREErnlrVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNK 159
Cdd:COG4987 418 --PHLfdtTLRENLRLARPD--ATDEE----LWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRiWQHEKiTMILVTHDiEEAVYLGDRVIVMSArpGKIKE 224
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLE-ALAGR-TVLLITHR-LAGLERMDRILVLED--GRIVE 549
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-215 |
2.42e-36 |
|
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: 129.39 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQrdqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDLK---- 84
Cdd:COG0411 3 PLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPphri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 --RGLI--FQEHRLLPWLTVFENI----HLALEETPLT---------REERNLR--VNEHIEIVGLKGFEKAYPHELSGG 145
Cdd:COG0411 77 arLGIArtFQNPRLFPELTVLENVlvaaHARLGRGLLAallrlprarREEREARerAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 146 MAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-225 |
4.29e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.52 E-value: 4.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdYD---GEILLNQTQIKGTDLKR-----GLIFQEHRLLPwLTV 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF---YDptsGRILIDGVDIRDLTLESlrrqiGVVPQDTFLFS-GTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETplTREErnlrVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:COG1132 431 RENIRYGRPDA--TDEE----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 170 GALDAITRSHLQAELQRIWQHekITMILVTHD---IEEAvylgDRVIVMSArpGKIKEI 225
Cdd:COG1132 505 SALDTETEALIQEALERLMKG--RTTIVIAHRlstIRNA----DRILVLDD--GRIVEQ 555
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
9-251 |
7.25e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 134.47 E-value: 7.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD------ 82
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 LKR---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNK 159
Cdd:PRK10535 83 LRRehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYlGDRVI------VMSARPGKIKEIIQ---VPL 230
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIeirdgeIVRNPPAQEKVNVAggtEPV 240
|
250 260
....*....|....*....|.
gi 375134789 231 THPRHKESELLFGFRnQALNM 251
Cdd:PRK10535 241 VNTASGWRQFVSGFR-EALTM 260
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-224 |
9.10e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 127.44 E-value: 9.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL-----------LNQTQIK 79
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfsqkPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 80 GTDLKRGLIFQEHRLLPWLTVFENihlaLEETP-----LTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIAR 154
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMEN----LIEAPckvlgLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 155 GLVNKPDILLLDEPFGALD-AITRShlQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKE 224
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDpEITAQ--VVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEK--GRIIE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-215 |
1.78e-35 |
|
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: 124.86 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKRglifqehrllpwl 98
Cdd:cd03214 6 SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-----GKDLAS------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 tvfenihlaleetpLTREERNLR---VNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:cd03214 66 --------------LSPKELARKiayVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 375134789 176 TRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILL 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-215 |
2.35e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.16 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL----- 83
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQE-HRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 375134789 163 LLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEaVYLGDRVIVM 215
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-223 |
2.75e-35 |
|
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: 125.06 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQRDQNtltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR--GLIF 89
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKsiGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QE-HRLLPWLTVFENIHLALEETPltreERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:cd03226 78 QDvDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 169 FGALDaitRSHLQ--AELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:cd03226 154 TSGLD---YKNMErvGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN--GAIV 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-225 |
3.47e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GL 87
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkkiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEhrllP-----WLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:PRK13632 88 IFQN----PdnqfiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 163 LLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVyLGDRVIVMSA----RPGKIKEI 225
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEgkliAQGKPKEI 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-215 |
6.07e-34 |
|
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: 122.55 E-value: 6.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRG 86
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LI--FQEHRLLPWLTVFENIHLALE--------ETPLTREERNLR--VNEHIEIVGLKGFEKAYPHELSGGMAQRVAIAR 154
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAAQartgsgllLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 155 GLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHeKITMILVTHDIeEAVY-LGDRVIVM 215
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDM-DVVMsLADRVTVL 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-222 |
1.28e-33 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 121.32 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI--KGTDLKR--GLI 88
Cdd:cd03265 3 VENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREVRRriGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPWLTVFEN--IHLALEETPltREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLD 166
Cdd:cd03265 79 FQDLSVDDELTGWENlyIHARLYGVP--GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 167 EPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH--GRI 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-230 |
1.42e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.67 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRdqntLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL----- 83
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--THLpmhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 -KRGLIF--QEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG1137 76 aRLGIGYlpQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 161 DILLLDEPFGALDAITrshlQAELQRIWQHEK---ITmILVT-HDIEEAVYLGDRVIVMSArpGKI------KEIIQVPL 230
Cdd:COG1137 156 KFILLDEPFAGVDPIA----VADIQKIIRHLKergIG-VLITdHNVRETLGICDRAYIISE--GKVlaegtpEEILNNPL 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-222 |
1.96e-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: 121.34 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG-LDQDYDGEI-LLNQTqiKGT----DLKR--GLIFQ 90
Cdd:COG1119 10 TVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVrLFGER--RGGedvwELRKriGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 E--HRLLPWLTVFE--------NIHLALEETPLTREernlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG1119 86 AlqLRFPRDETVLDvvlsgffdSIGLYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRV 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-233 |
2.74e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 123.28 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQ-RDQN--------TLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL-LNQTQIK 79
Cdd:PRK15079 8 LLEVADLKVHFDiKDGKqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 80 GTDLKR-------GLIFQE--HRLLPWLTVFENIHLALE--ETPLTREERNLRVNEHIEIVGL-KGFEKAYPHELSGGMA 147
Cdd:PRK15079 88 MKDDEWravrsdiQMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 148 QRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM----SARPGKIK 223
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMylghAVELGTYD 247
|
250
....*....|
gi 375134789 224 EIIQVPLtHP 233
Cdd:PRK15079 248 EVYHNPL-HP 256
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-236 |
4.36e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 121.10 E-value: 4.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQ------RDQnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL 83
Cdd:COG4167 4 LLEVRNLSKTFKyrtglfRRQ-QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRG-----LIFQ--EHRLLPWLtvfeNIHLALEE-----TPLTREERNLRVNEHIEIVGLKGfEKA--YPHELSGGMAQR 149
Cdd:COG4167 83 KYRckhirMIFQdpNTSLNPRL----NIGQILEEplrlnTDLTAEEREERIFATLRLVGLLP-EHAnfYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDAITRS---HLQAELQriwQHEKITMILVTHDIEEAVYLGDRVIVMSA----RPGKI 222
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSqiiNLMLELQ---EKLGISYIYVSQHLGIVKHISDKVLVMHQgevvEYGKT 234
|
250
....*....|....
gi 375134789 223 KEIiqvpLTHPRHK 236
Cdd:COG4167 235 AEV----FANPQHE 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-224 |
5.09e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.84 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR 85
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 G------------------LIFQEHRLLPWLTVFENIHLA-LEETPLTREERNLRVNEHIEIVGLKGFEKA-YPHELSGG 145
Cdd:PRK10619 77 GqlkvadknqlrllrtrltMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 146 MAQRVAIARGLVNKPDILLLDEPFGALDaitrSHLQAELQRIWQH---EKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFL--HQGKI 230
|
..
gi 375134789 223 KE 224
Cdd:PRK10619 231 EE 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-222 |
7.50e-33 |
|
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: 119.23 E-value: 7.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT---QIKGTDLKR--GLIFQEHRLLpWLTVFEN 103
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirQLDPADLRRniGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALeetPLTREERNLRVnehIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:cd03245 98 ITLGA---PLADDERILRA---AELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 173 DAITRSHLQAELQRiWQHEKiTMILVTHDIeEAVYLGDRVIVMSArpGKI 222
Cdd:cd03245 172 DMNSEERLKERLRQ-LLGDK-TLIIITHRP-SLLDLVDRIIVMDS--GRI 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-228 |
7.79e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 120.30 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQ-----RDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL---NQTQIKG 80
Cdd:TIGR02769 1 SLLEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 TDLKR-----GLIFQE--HRLLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGLKG-FEKAYPHELSGGMAQRVA 151
Cdd:TIGR02769 81 KQRRAfrrdvQLVFQDspSAVNPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEIIQV 228
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQIVEECDV 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-222 |
1.09e-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: 119.18 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDL------K 84
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI--TKLpmhkraR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 RGLIF--QEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDI 162
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 163 LLLDEPFGALDAITRShlqaELQRIWQH--EKITMILVT-HDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03218 155 LLLDEPFAGVDPIAVQ----DIQKIIKIlkDRGIGVLITdHNVRETLSITDRAYIIYE--GKV 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-205 |
1.10e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 117.72 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILlnqtqiKGTDLKRGLIFQEHRL---LPwLTVFENI 104
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVpdsLP-LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLAL-----EETPLTREERnLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:NF040873 79 AMGRwarrgLWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|....*.
gi 375134789 180 LQAELQRiWQHEKITMILVTHDIEEA 205
Cdd:NF040873 158 IIALLAE-EHARGATVVVVTHDLELV 182
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-222 |
1.95e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.03 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQ-NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG---LDQdydGEILLNQTQI-KGTDLKR 85
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslpPDS---GSILIDGKDVtKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRL--LPWLTVFENIHLALEET-------PLTREERNlRVNEHIEIVGLkGFEKAYPHE---LSGGmaQR 149
Cdd:COG1101 79 akyiGRVFQDPMMgtAPSMTIEENLALAYRRGkrrglrrGLTKKRRE-LFRELLATLGL-GLENRLDTKvglLSGG--QR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 150 VAIArgLV----NKPDILLLDEPFGALDAITrSHLQAEL-QRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG1101 155 QALS--LLmatlTKPKLLLLDEHTAALDPKT-AALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHE--GRI 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
2.60e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GL 87
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQ--EHRLLPWLTVFEnIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVM 215
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-210 |
3.15e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 118.71 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL--------LNQTQIKGTDLKRGLIFQ 90
Cdd:PRK11831 14 SFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipaMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EHRLLPWLTVFENIHLALEE-TPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:PRK11831 92 SGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 375134789 170 GALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGD 210
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-215 |
6.43e-32 |
|
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: 116.76 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRG 86
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LIF--QEHRLLPWLTVFENIHLAleETPLTREERNLRVNEHIEIV-GLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:cd03224 77 IGYvpEGRRIFPELTVEENLLLG--AYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-223 |
6.44e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 119.98 E-value: 6.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 45 IVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI----KGTDL---KR--GLIFQEHRLLPWLTVFENIHLALEETplTR 115
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLppeKRriGYVFQDARLFPHYKVRGNLRYGMAKS--MV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 116 EERNlrvnehiEIVGLKGFE---KAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEK 192
Cdd:PRK11144 107 AQFD-------KIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190
....*....|....*....|....*....|.
gi 375134789 193 ITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:PRK11144 180 IPILYVSHSLDEILRLADRVVVLEQ--GKVK 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-239 |
6.75e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 6.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLR-------LIAGldQDYDGEILLNQTQI--KGT 81
Cdd:COG1117 12 IEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG--ARVEGEILLDGEDIydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 82 DL----KR-GLIFQEHRLLPwLTVFENIHLALEET-PLTREERNLRVNEHIEIVGL----KGFEKAYPHELSGGMAQRVA 151
Cdd:COG1117 86 DVvelrRRvGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSH---LQAELQriwqhEKITMILVTHDIEEAVYLGDRVIVMSArpGKI------ 222
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKieeLILELK-----KDYTIVIVTHNMQQAARVSDYTAFFYL--GELvefgpt 237
|
250
....*....|....*..
gi 375134789 223 KEIiqvpLTHPRHKESE 239
Cdd:COG1117 238 EQI----FTNPKDKRTE 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-224 |
8.89e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI-LLNQTQIKGTDLKR-- 85
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQPLHQMDEEARak 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ------GLIFQEHRLLPWLTVFENIHL-ALEETPLTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVN 158
Cdd:PRK10584 85 lrakhvGFVFQSFMLIPTLNALENVELpALLRGESSRQSRN-GAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 159 KPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRvivMSARPGKIKE 224
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRR---LRLVNGQLQE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-241 |
2.52e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQ-----RDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT---QIKG 80
Cdd:PRK10419 2 TLLNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 TDLK--RG---LIFQEH--RLLPWLTVFENI-----HLaleeTPLTREERNLRVNEHIEIVGLK-GFEKAYPHELSGGMA 147
Cdd:PRK10419 82 AQRKafRRdiqMVFQDSisAVNPRKTVREIIreplrHL----LSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 148 QRVAIARGLVNKPDILLLDEPFGALDAitrsHLQAE----LQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDL----VLQAGvirlLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIV 231
|
250
....*....|....*....
gi 375134789 224 EIIQV-PLTHPRHKESELL 241
Cdd:PRK10419 232 ETQPVgDKLTFSSPAGRVL 250
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-216 |
2.94e-31 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 117.11 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGeillnQTQIKGTDLKR---------GLIFQEHRLLPWLTV 100
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG-----TARVAGYDVVReprkvrrsiGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHl 180
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 375134789 181 qaelqrIWQH------EKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:TIGR01188 163 ------IWDYiralkeEGVTILLTTHYMEEADKLCDRIAIID 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-215 |
3.14e-31 |
|
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: 120.47 E-value: 3.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQehrlLPWL---TV 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQ----HPFLfagTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETplTREErnlrVNEHIEIVGLKGFEKAYP-----------HELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:TIGR02857 413 AENIRLARPDA--SDAE----IREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 375134789 170 GALDAITRSHLQAELQRIWQHEkiTMILVTHDIEEAvYLGDRVIVM 215
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGR--TVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-215 |
3.61e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.88 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL---DQDYDG--EILLNQTQIKGT-- 81
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGShiELLGRTVQREGRla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 82 -DLKR-----GLIFQEHRLLPWLTVFENIHL-ALEETPLTR-------EERNLRVNEHIEIVGLKGFEKAYPHELSGGMA 147
Cdd:PRK09984 79 rDIRKsrantGYIFQQFNLVNRLSVLENVLIgALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 148 QRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-233 |
4.26e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 117.15 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTDLKR--- 85
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLEFNGQDLQRise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 -----------GLIFQE--HRLLPWLTVFENIHLALE-ETPLTREERNLRVNEHIEIVGLKGFEK---AYPHELSGGMAQ 148
Cdd:PRK11022 81 kerrnlvgaevAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 149 RVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSA----RPGKIKE 224
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAgqvvETGKAHD 240
|
....*....
gi 375134789 225 IIQVPLtHP 233
Cdd:PRK11022 241 IFRAPR-HP 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-233 |
1.02e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 116.22 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 18 KSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD-LKRGLIFQEHRLlp 96
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpEAQKLLRQKIQI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 wltVFEN----------IHLALEE-----TPLTREERNLRVNEHIEIVGLKG-FEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:PRK11308 97 ---VFQNpygslnprkkVGQILEEpllinTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 161 DILLLDEPFGALDAITRS---HLQAELQriwQHEKITMILVTHDIEEAVYLGDRVIVM----SARPGKIKEIIQVPLtHP 233
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAqvlNLMMDLQ---QELGLSYVFISHDLSVVEHIADEVMVMylgrCVEKGTKEQIFNNPR-HP 249
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-222 |
1.79e-30 |
|
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: 112.70 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQrdqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGT--DLKR-GL 87
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNieALRRiGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHRLLPWLTVFENIHLALEETPLtreeRNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 168 PFGALDAITRSHLQaELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:cd03268 153 PTNGLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGII--NKGKL 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-202 |
2.46e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.66 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL---NQTQIKGTD---LKR--GLIFQEHRLLPWLTVF 101
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghDITRLKNREvpfLRRqiGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD-AITRSHL 180
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGIL 177
|
170 180
....*....|....*....|....
gi 375134789 181 Q--AELQRIwqheKITMILVTHDI 202
Cdd:PRK10908 178 RlfEEFNRV----GVTVLMATHDI 197
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-223 |
8.31e-30 |
|
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: 110.75 E-value: 8.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntltVLDGINLNIEQGeFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR----- 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID-----GQDVLKqpqkl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENI-HLA-LEETPLTREERnlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNK 159
Cdd:cd03264 71 rrriGYLPQEFGVYPNFTVREFLdYIAwLKGIPSKEVKA--RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 160 PDILLLDEPFGALDAITR---SHLQAELQriwqhEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:cd03264 149 PSILIVDEPTAGLDPEERirfRNLLSELG-----EDRIVILSTHIVEDVESLCNQVAVLNK--GKLV 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-222 |
9.62e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.48 E-value: 9.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK--GTDL-----KRGLIFQ---EHRLLPwl 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLlevrkTVGIVFQnpdDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 TVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRS 178
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 179 HLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:PRK13639 175 QIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSD--GKI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-215 |
1.06e-29 |
|
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: 110.92 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN----QTQIKGTDLKR 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
33-215 |
1.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI----KGTDLKR-----GLIFQ--EHRLLPwLTVF 101
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPlrkkvGIVFQfpEHQLFE-ETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETPLTREERNLRVNEHIEIVGL--KGFEKAyPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:PRK13634 105 KDICFGPMNFGVSEEDAKQKAREMIELVGLpeELLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 375134789 180 LQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13634 184 MMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-224 |
3.35e-29 |
|
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: 109.94 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdYD---GEILLNQTQIKGTDLKR-----GLIFQEHRLLPwLTV 100
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF---YDptsGEILLDGVDIRDLNLRWlrsqiGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPLTREERNLRV-NEHIEIVGL-KGFEK---AYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKaNIHDFIMSLpDGYDTlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 176 TRSHLQAELQRIwqHEKITMILVTH---DIEEAvylgDRVIVMSarPGKIKE 224
Cdd:cd03249 174 SEKLVQEALDRA--MKGRTTIVIAHrlsTIRNA----DLIAVLQ--NGQVVE 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-222 |
7.81e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT---QIKGTDL--KRGLIFQEHR 93
Cdd:COG4559 8 SVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaAWSPWELarRRAVLPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 L-LPWlTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGF-EKAYPhELSGGMAQRVAIARGLV-------NKPDILL 164
Cdd:COG4559 86 LaFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLaGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 165 LDEPFGALDAitrSHLQAELQ--RIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG4559 164 LDEPTSALDL---AHQHAVLRlaRQLARRGGGVVAVLHDLNLAAQYADRILLLHQ--GRL 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-217 |
9.61e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNtLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL-----K 84
Cdd:PRK13642 4 ILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 RGLIFQE-HRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDIL 163
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMSA 217
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-222 |
1.01e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 106.74 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDlkrglifq 90
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 ehrllpwltvfenihlaleetplTREERNLRvnehIEIVglkgfekaypHELSGGMAQRVAIARGLVNKPDILLLDEPFG 170
Cdd:cd03216 69 -----------------------PRDARRAG----IAMV----------YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 171 ALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:cd03216 112 ALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-223 |
1.52e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 23 DQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD------LKRGLIFQ--EHRL 94
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 95 LPWLtVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:PRK13633 99 VATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 375134789 175 ITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMSArpGKIK 223
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDS--GKVV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-201 |
1.83e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQtqikgtDLKRGLIFQEH 92
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 93 RLLPWLTVFENIHLALEE----------------TPLTREERNLRVNEHIE--------------IVGLkGFEKAYPH-- 140
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAElraleaeleeleaklaEPDEDLERLAELQEEFEalggweaearaeeiLSGL-GFPEEDLDrp 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 141 --ELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRiwqhEKITMILVTHD 201
Cdd:COG0488 150 vsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHD 208
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-233 |
1.25e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 108.07 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQD----------YDGEILLNQT--- 76
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrWNGIDLLKLSpre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 77 --QIKGTDLkrGLIFQEHR--LLPWLTVFENIHLALEETPLT------REERNLRVNEHIEIVGLKGFE---KAYPHELS 143
Cdd:COG4170 83 rrKIIGREI--AMIFQEPSscLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKDHKdimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 144 GGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM----SARP 219
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqTVES 240
|
250
....*....|....
gi 375134789 220 GKIKEIIQVPLtHP 233
Cdd:COG4170 241 GPTEQILKSPH-HP 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-239 |
1.56e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDY-----DGEILLNQTQIKGTD- 82
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 --LKR--GLIFQEHRLLPWLTVFENIHLALEETPLTREERNL--RVNEHIEIVGL----KGFEKAYPHELSGGMAQRVAI 152
Cdd:PRK14247 78 ieLRRrvQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELqeRVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLQA---ELQRiwqheKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI--IQ 227
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESlflELKK-----DMTIVLVTHFPQQAARISDYVAFLYK--GQIVEWgpTR 230
|
250
....*....|..
gi 375134789 228 VPLTHPRHKESE 239
Cdd:PRK14247 231 EVFTNPRHELTE 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-215 |
1.63e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKR 85
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 G--LIFQEHRLLPWLTVFENIHLALEETP--------LTREERNL--RVNEHI---EIVGlkgfekayphELSGGMAQRV 150
Cdd:COG1129 80 GiaIIHQELNLVPNLSVAENIFLGREPRRgglidwraMRRRARELlaRLGLDIdpdTPVG----------DLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 151 AIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-215 |
1.88e-27 |
|
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: 104.67 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRdqntLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-GLIF 89
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFEN-IHLAlEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:cd03269 77 EERGLYPKMKVIDQlVYLA-QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVM 215
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLL 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-215 |
2.12e-27 |
|
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: 103.45 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQE 91
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWlTVFENIhlaleetpltreernlrvnehieivglkgfekaypheLSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:cd03246 85 DELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 172 LDAITRSHLQAELQRIwQHEKITMILVTHDIeEAVYLGDRVIVM 215
Cdd:cd03246 127 LDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
29-224 |
3.76e-27 |
|
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: 104.61 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEhrllPWL---TV 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQD----TFLfsgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLAleeTPLTREErnlRVNEHIEIVGLKGF----EKAYPHE-------LSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:cd03254 94 MENIRLG---RPNATDE---EVIEAAKEAGAHDFimklPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 170 GALDAITRSHLQAELQRIwqHEKITMILVTH---DIEEAvylgDRVIVMsaRPGKIKE 224
Cdd:cd03254 168 SNIDTETEKLIQEALEKL--MKGRTSIIIAHrlsTIKNA----DKILVL--DDGKIIE 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-217 |
1.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI-----LLNQTQIKGTDLKRGLIFQE-HRLLPWLTVFEN 103
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrEVNAENEKWVRSKVGLVFQDpDDQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAE 183
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190
....*....|....*....|....*....|....
gi 375134789 184 LQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:PRK13647 181 LDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKE 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-222 |
1.04e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQ---TQIKGTDL--KRGLIFQEHR 93
Cdd:PRK13548 9 SVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrplADWSPAELarRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 L-LPWlTVFENIHLALeeTPLTREERNLR--VNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLV------NKPDILL 164
Cdd:PRK13548 87 LsFPF-TVEEVVAMGR--APHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 165 LDEPFGALDAitrSHLQAELQ---RIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:PRK13548 164 LDEPTSALDL---AHQHHVLRlarQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ--GRL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-224 |
1.43e-26 |
|
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: 103.33 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD---LKR--GLIFQEHRLLPwLTVFEN 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawLRRqvGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREERNLRV---NEHI--------EIVGLKGFekayphELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:cd03252 96 IALADPGMSMERVIEAAKLagaHDFIselpegydTIVGEQGA------GLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 173 DAITRSHLQAELQRIWQHEkiTMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRL-STVKNADRIIVMEK--GRIVE 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-216 |
1.63e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.86 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 3 GIYMSFSLLSIKKLNKSFQrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL--DQDYDGEILLNQTQIKG 80
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSK---SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 TDLKR--GLIFQEHRLLPWLTVFENIHLALEetpltreernlrvnehieivgLKGfekaypheLSGGMAQRVAIARGLVN 158
Cdd:cd03213 78 RSFRKiiGYVPQDDILHPTLTVRETLMFAAK---------------------LRG--------LSGGERKRVSIALELVS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 159 KPDILLLDEPFGALDAITRSHLQAELQRIWQhEKITMILVTHDI-EEAVYLGDRVIVMS 216
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLS 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-201 |
2.49e-26 |
|
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: 106.94 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQRDQNtltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQtqikgtDLKRGLIFQE 91
Cdd:TIGR03719 6 TMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP------GIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWLTVFENIHLALEETP--LTR------------------EERNLRVNEHIEIVGLKGFEK--------------- 136
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEIKdaLDRfneisakyaepdadfdklAAEQAELQEIIDAADAWDLDSqleiamdalrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 137 AYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwqheKITMILVTHD 201
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTHD 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-215 |
6.22e-26 |
|
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: 101.21 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF--QEHRLLPWLTVFE 102
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphriARLGIGYvpEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHLALeetpLTREERNlRVNEHIEIVG-----LKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITR 177
Cdd:COG0410 98 NLLLGA----YARRDRA-EVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 375134789 178 SHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:COG0410 173 EEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVL 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
10-174 |
1.02e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.88 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLnkSFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK--GTDLKRGL 87
Cdd:PRK13538 1 MLEARNL--ACERDERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IFQEHR--LLPWLTVFENIHLALEETPLTREErnlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:PRK13538 77 LYLGHQpgIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
....*....
gi 375134789 166 DEPFGALDA 174
Cdd:PRK13538 154 DEPFTAIDK 162
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-225 |
1.14e-25 |
|
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: 100.30 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 4 IYMSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtQIKGTDl 83
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 kRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRV--AIARGLvnKPD 161
Cdd:cd03220 86 -SSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-221 |
1.17e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN--QTQIKGT----DL 83
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRSPrdaiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNlRVNEHIEIVGLK-GFE---KAYPHELSGGMAQRVAIARGLVNK 159
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRK-AARARIRELSERyGLDvdpDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 160 PDILLLDEP------------FGALDAITRshlqaelqriwqhEKITMILVTHDIEEAVYLGDRVIVMsaRPGK 221
Cdd:COG3845 160 ARILILDEPtavltpqeadelFEILRRLAA-------------EGKSIIFITHKLREVMAIADRVTVL--RRGK 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-201 |
1.21e-25 |
|
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: 104.75 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN---QTQIKGTDLKRGLIFQEHRllPWL---TVFE 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpVSSLDQDEVRRRVSVCAQD--AHLfdtTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHLALEETplTREErnlrVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:TIGR02868 428 NLRLARPDA--TDEE----LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|.
gi 375134789 172 LDAITRSHLqaeLQRIWQ-HEKITMILVTHD 201
Cdd:TIGR02868 502 LDAETADEL---LEDLLAaLSGRTVVLITHH 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-225 |
1.28e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.11 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-GLIF 89
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRiGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENI-HLAlEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:COG4152 78 EERGLYPKMKVGEQLvYLA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 169 FGALDAITRSHLQAELQRiwQHEK-ITMILVTHDIEEAVYLGDRVIVMSA-RP---GKIKEI 225
Cdd:COG4152 157 FSGLDPVNVELLKDVIRE--LAAKgTTVIFSSHQMELVEELCDRIVIINKgRKvlsGSVDEI 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-239 |
1.48e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQ-----DYDGEILLNQTQIKG 80
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 81 -----TDLKR--GLIFQEHRLLPwLTVFENIHLALEetpLTREERNLRVNEHIEiVGLKGFE-----KAYPHE----LSG 144
Cdd:PRK14239 77 prtdtVDLRKeiGMVFQQPNPFP-MSIYENVVYGLR---LKGIKDKQVLDEAVE-KSLKGASiwdevKDRLHDsalgLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 145 GMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRVIVMSArpgkiKE 224
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLD-----GD 224
|
250 260
....*....|....*....|
gi 375134789 225 IIQVPLTH-----PRHKESE 239
Cdd:PRK14239 225 LIEYNDTKqmfmnPKHKETE 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-225 |
1.53e-25 |
|
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: 104.50 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 23 DQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGE--ILLNQTQIKGTDL--------KR--GLIFQ 90
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPgpdgrgraKRyiGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EHRLLPWLTVFENIHLALE-ETPltreeRNLRVNEHIEIVGLKGF--EKA------YPHELSGGMAQRVAIARGLVNKPD 161
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGlELP-----DELARMKAVITLKMVGFdeEKAeeildkYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKIVKI 509
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-227 |
2.10e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI----KGTDLKR-----GLIFQ--EHRLLPWl 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQirkkvGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 TVFENIHLALEETPLTREERNLRVNEHIEIVGLKG--FEKAyPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 177 RShlqaELQRIWQ--HEK-ITMILVTHDIEEAVYLGDRVIVMSA----RPGKIKEIIQ 227
Cdd:PRK13649 181 RK----ELMTLFKklHQSgMTIVLVTHLMDDVANYADFVYVLEKgklvLSGKPKDIFQ 234
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
31-229 |
2.53e-25 |
|
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: 99.75 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 31 DGINLNIEQGEFISIVGSSGCGKST----LLRLIAGLDQDYDGEILL-----NQTQIKGTDLkrGLIFQEHR--LLPWLT 99
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLdgrplLPLSIRGRHI--ATIMQNPRtaFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 vfenIHLALEETPLTRE----ERNLRVNEHIEIVGLKGFE---KAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:TIGR02770 81 ----MGNHAIETLRSLGklskQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 173 DAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI------KEIIQVP 229
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIvergtvKEIFYNP 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-215 |
3.07e-25 |
|
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: 98.70 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTLT-VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikgtdlkRGLIF 89
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEhrllPWL---TVFENIHLALEEtpltREERNLRV------NEHIEI--------VGLKGFEkaypheLSGGMAQRVAI 152
Cdd:cd03250 73 QE----PWIqngTIRENILFGKPF----DEERYEKVikacalEPDLEIlpdgdlteIGEKGIN------LSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHL-QAELQRIWQHEKiTMILVTHDIEEAVYLgDRVIVM 215
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNK-TRILVTHQLQLLPHA-DQIVVL 200
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-215 |
3.60e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLnkSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL---DQDYDGEIL-----LNQTQ 77
Cdd:PRK13640 1 MKDNIVEFKHV--SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITvdgitLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 78 IKGTDLKRGLIFQE-HRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:PRK13640 79 VWDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVyLGDRVIVM 215
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVL 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-225 |
5.13e-25 |
|
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: 98.84 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdYD---GEILLNQTQIKG---TDLKR--GLI 88
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRF---YDvdsGRILIDGHDVRDytlASLRRqiGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPWlTVFENIHLALEETPLTREERNLR-VNEH--IE--------IVGLKGFEkaypheLSGGMAQRVAIARGLV 157
Cdd:cd03251 82 SQDVFLFND-TVAENIAYGRPGATREEVEEAARaANAHefIMelpegydtVIGERGVK------LSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 158 NKPDILLLDEPFGALDAITRSHLQAELQRIWQHEkiTMILVTH---DIEEAvylgDRVIVMSArpGKIKEI 225
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHrlsTIENA----DRIVVLED--GKIVER 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-233 |
5.67e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.40 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKS----TLLRLI--AGLDQDYDGEILLNQTQ------ 77
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSRqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 78 ---------IKGTDLkrGLIFQE--HRLLPWLTVFENIHLALE-ETPLTREERNL---RVNEHIEIVGLKGFEKAYPHEL 142
Cdd:PRK10261 92 eqsaaqmrhVRGADM--AMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVeakRMLDQVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 143 SGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM----SAR 218
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMyqgeAVE 249
|
250
....*....|....*
gi 375134789 219 PGKIKEIIQVPlTHP 233
Cdd:PRK10261 250 TGSVEQIFHAP-QHP 263
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-225 |
6.29e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 6.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL-----DQDYDGEILLNQTQIKGTDL-------KRGLIFQEHRLLP 96
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVdpievrrEVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 WLTVFENIHLALEETPLTREERNL--RVNEHIEIVGL----KGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFG 170
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLVKSKKELdeRVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 171 ALDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK14267 179 NIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYL--GKLIEV 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-217 |
1.35e-24 |
|
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: 97.50 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSF---QRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGldqDY---DGEILLNQT------- 76
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---NYlpdSGSILVRHDggwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 77 -----QIkgTDLKR---GLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKgfEK---AYPHELSGG 145
Cdd:COG4778 81 qasprEI--LALRRrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLP--ERlwdLPPATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 146 MAQRVAIARGLVNKPDILLLDEPFGALDAITRshlQAELQRIwqHEK----ITMILVTHDIE--EAVylGDRVIVMSA 217
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANR---AVVVELI--EEAkargTAIIGIFHDEEvrEAV--ADRVVDVTP 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-233 |
1.78e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.41 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKS----TLLRLIA-----GLDQDYDGEILLNqt 76
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAangriGGSATFNGREILN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 77 qIKGTDLKR------GLIFQE--HRLLPWLTVFENIH--LALEETPLTRE--ERNLRVNEHIEIVGLKGFEKAYPHELSG 144
Cdd:PRK09473 86 -LPEKELNKlraeqiSMIFQDpmTSLNPYMRVGEQLMevLMLHKGMSKAEafEESVRMLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 145 GMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSA----RPG 220
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAgrtmEYG 244
|
250
....*....|...
gi 375134789 221 KIKEIIQVPlTHP 233
Cdd:PRK09473 245 NARDVFYQP-SHP 256
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-231 |
2.13e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQdYDGEI-------LLNQT-- 76
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVrvegrveFFNQNiy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 77 --QIKGTDLKR--GLIFQEHRLLPwLTVFENI---------HLALEETPLTreERNLRVNEHIEIVGLKGFEKAYphELS 143
Cdd:PRK14258 78 erRVNLNRLRRqvSMVHPKPNLFP-MSVYDNVaygvkivgwRPKLEIDDIV--ESALKDADLWDEIKHKIHKSAL--DLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 144 GGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGKIK 223
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIG 232
|
....*...
gi 375134789 224 EIIQVPLT 231
Cdd:PRK14258 233 QLVEFGLT 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
10-215 |
2.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLT-VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL---------NQTQIK 79
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 80 GTDLKRGLIFQ--EHRLLPWlTVFENIHLALEETPLTREERNLRVNEHIEIVGL-KGFEKAYPHELSGGMAQRVAIARGL 156
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLL 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-224 |
2.19e-24 |
|
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: 97.30 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNtLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdYD---GEILLNQTQIKGTDLKR-----GLI 88
Cdd:cd03253 5 NVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRF---YDvssGSILIDGQDIREVTLDSlrraiGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPwLTVFENIHLALEETplTREE-----RNLRVNEHIE--------IVGLKGFEkaypheLSGGMAQRVAIARG 155
Cdd:cd03253 81 PQDTVLFN-DTIGYNIRYGRPDA--TDEEvieaaKAAQIHDKIMrfpdgydtIVGERGLK------LSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 156 LVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEkiTMILVTHDIEEaVYLGDRVIVMSArpGKIKE 224
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLST-IVNADKIIVLKD--GRIVE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-224 |
2.24e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSF-------QRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKST----LLRLIAGldqdyDGEILLNQTQI 78
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 79 KGTDLKRGL--------IFQE--HRLLPWLTVFENIH--LALEETPLTREERNLRVNEHIEIVGLKGFEKA-YPHELSGG 145
Cdd:PRK15134 350 HNLNRRQLLpvrhriqvVFQDpnSSLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 146 MAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKE 224
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL--RQGEVVE 506
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-182 |
3.12e-24 |
|
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: 95.89 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 27 LTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI-KGTDL-KRGLIFQEHR--LLPWLTVFE 102
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEpHENILYLGHLpgLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHLAleeTPLTREERnLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD--------A 174
Cdd:TIGR01189 93 NLHFW---AAIHGGAQ-RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvallaG 168
|
....*...
gi 375134789 175 ITRSHLQA 182
Cdd:TIGR01189 169 LLRAHLAR 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-216 |
5.90e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI----KG-TDLKR--GLIFQ--EHRLLPwLTV 100
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGlMKLREsvGMVFQdpDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHL 180
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 375134789 181 QAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMK 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-174 |
5.92e-24 |
|
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: 95.25 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 27 LTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikGTDLKRGLIfqeHRLLPWLTvfeniHL 106
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSI---ARGLLYLG-----HA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 107 ALEETPLTREErNLR----------VNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:cd03231 82 PGIKTTLSVLE-NLRfwhadhsdeqVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-215 |
6.20e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG----T 81
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSrarhA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 82 DLKRGLIFQEHRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPD 161
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 375134789 162 ILLLDEPFGALDAITRsHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13537 159 VLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-215 |
8.72e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI------LLNQTQIKG-TDLKR--GLIFQehrlLPWLTV 100
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNKNlKKLRKkvSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLA-LEETPL----TREERNLRVNEHIEIVGLKG--FEKAyPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PRK13641 99 FENTVLKdVEFGPKnfgfSEDEAKEKALKWLKKVGLSEdlISKS-PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 375134789 174 AITRSHLQaELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13641 178 PEGRKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-216 |
8.98e-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: 95.42 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYD---GEILLNQTQIKGTDLKR 85
Cdd:cd03234 2 RVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIF--QEHRLLPWLTVFENIHLALeETPLTREERNLRVNEHIEIVGLKGFE-----KAYPHELSGGMAQRVAIARGLVN 158
Cdd:cd03234 82 CVAYvrQDDILLPGLTVRETLTYTA-ILRLPRKSSDAIRKKRVEDVLLRDLAltrigGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 159 KPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLS 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-222 |
9.59e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQNT-LTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI------------------LL 73
Cdd:PRK13651 5 VKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 74 NQTQIKGTDLKR-----------GLIFQ--EHRLLPwLTVFENIHLALEETPLTREERNLRVNEHIEIVGL-KGFEKAYP 139
Cdd:PRK13651 85 EKLVIQKTRFKKikkikeirrrvGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 140 HELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMsaRP 219
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFF--KD 240
|
...
gi 375134789 220 GKI 222
Cdd:PRK13651 241 GKI 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-216 |
1.60e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.97 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQ---DYDGEILLNQTQIKGTDLKR-- 85
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAis 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENI----HLALEETpLTREERNLRVNEHIEIVGLK----------GFEKAypheLSGGMAQRVA 151
Cdd:TIGR00955 102 AYVQQDDLFIPTLTVREHLmfqaHLRMPRR-VTKKEKRERVDEVLQALGLRkcantrigvpGRVKG----LSGGERKRLA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVY-LGDRVIVMS 216
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFeLFDKIILMA 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-225 |
3.28e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKK-LNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtQIKGT-----DLkr 85
Cdd:COG1134 23 SLKElLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRvsallEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQehrllPWLTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFE----KAYphelSGGMAQRVAIARGLVNKPD 161
Cdd:COG1134 96 GAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpvKTY----SSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 162 ILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEK--GRLVMD 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-227 |
3.72e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQrdqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYD-GEILLNQ---TQIKGTDLKRGL 87
Cdd:COG4604 3 EIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRL-LPPDsGEVLVDGldvATTPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 -IF-QEHRLLPWLTVFENIhlALEETP-----LTREERNLrVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:COG4604 78 aILrQENHINSRLTVRELV--AFGRFPyskgrLTAEDREI-IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 161 DILLLDEPFGALDaITRS-HLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI------KEIIQ 227
Cdd:COG4604 155 DYVLLDEPLNNLD-MKHSvQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM--KDGRVvaqgtpEEIIT 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-224 |
3.90e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 97.86 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI---KGTDLKRGLIF-QEHRLLPWLTVFENI 104
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLadyTLASLRRQVALvSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 -HLALEETPLTREERNLRVNEHIEIV-----------GLKGfekaypHELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:TIGR02203 427 aYGRTEQADRAEIERALAAAYAQDFVdklplgldtpiGENG------VLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 173 DAITRSHLQAELQRIWQHEkiTMILVTH---DIEEAvylgDRVIVMSArpGKIKE 224
Cdd:TIGR02203 501 DNESERLVQAALERLMQGR--TTLVIAHrlsTIEKA----DRIVVMDD--GRIVE 547
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-216 |
2.10e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.01 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 20 FQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI----LLNQTQIKGTDLKRGLIFQEHRLL 95
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 96 PW-LTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:cd03267 107 WWdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 375134789 175 ITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-215 |
3.00e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD--- 82
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 -LKRGLI--FQEHRLLPWLTVFENIHLA------------LEETPLTRE-ERNL--RVNEHIEIVGLKGFEKAYPHELSG 144
Cdd:PRK11300 77 iARMGVVrtFQHVRLFREMTVIENLLVAqhqqlktglfsgLLKTPAFRRaESEAldRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 145 GMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-215 |
3.36e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKS----TLLRLIAGLDQDY-DGEILLN------ 74
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHgesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 75 ---QT--QIKGTdlKRGLIFQE--------HRLLPWLTVFENIHLALEETPlTREERnLRVNEHIEIVGLKGFEKAYPHE 141
Cdd:PRK15134 81 aseQTlrGVRGN--KIAMIFQEpmvslnplHTLEKQLYEVLSLHRGMRREA-ARGEI-LNCLDRVGIRQAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 142 LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-201 |
3.62e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.80 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQRDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtqikGTDLKRGLIFQE 91
Cdd:PRK11819 8 TMNRVSKVVPPKK---QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWLTVFENIHLALEETPLTREERNlrvnehiEIVGLKGFEKAYPHE------------------------------ 141
Cdd:PRK11819 79 PQLDPEKTVRENVEEGVAEVKAALDRFN-------EIYAAYAEPDADFDAlaaeqgelqeiidaadawdldsqleiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 142 ------------LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwqheKITMILVTHD 201
Cdd:PRK11819 152 lrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY----PGTVVAVTHD 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-220 |
3.77e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQikgtdlkrGLIFqehrL-----LPWLTVFE 102
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--------RVLF----LpqrpyLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHLALEETPLTREErnlrVNEHIEIVGLKGF------EKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:COG4178 445 ALLYPATAEAFSDAE----LREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 177 RSHLQAELQRiwQHEKITMILVTHDIEEAVYLgDRVIVMSARPG 220
Cdd:COG4178 521 EAALYQLLRE--ELPGTTVISVGHRSTLAAFH-DRVLELTGDGS 561
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
31-241 |
3.80e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.68 E-value: 3.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 31 DGINLNIEQGEFISIVGSSGCGKS-----TLLRLIAGLDQdYDGEILLNQTQIKGTDLkRG----LIFQEHRllpwlTVF 101
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCAL-RGrkiaTIMQNPR-----SAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ---ENIHLALEET--PLTREERNLRVNEHIEIVGLKGFE---KAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PRK10418 93 nplHTMHTHARETclALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 174 AITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEIIQV-PLTH-PRHKESELL 241
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVEQGDVeTLFNaPKHAVTRSL 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-222 |
3.89e-22 |
|
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: 89.80 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF-----QEHRLLPWLT 99
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdaIRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFENIHLaleetpltreernlrvnehieivglkgfekayPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 375134789 180 LQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:cd03215 143 IYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-221 |
5.66e-22 |
|
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: 91.32 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEF-----ISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI-----------KGT--DLKRGLIFQE 91
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadyEGTvrDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWLTVFENihlaleetPLTRE---ERNLRvnehieivglkgfekayphELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:cd03237 90 YTHPYFKTEIAK--------PLQIEqilDREVP-------------------ELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGK 221
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-222 |
1.40e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTDLKrglifQEHRLLPWL---------TVFEN 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPE-----SWRKHLSWVgqnpqlphgTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLAleeTPLTREERnlrVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:PRK11174 443 VLLG---NPDASDEQ---LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 173 DAITRSHLQAELQRIWQHEkiTMILVTHDIEEAVYLgDRVIVMsaRPGKI 222
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVM--QDGQI 561
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-216 |
1.61e-21 |
|
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: 89.51 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRG 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LIF--QEHRLLPWLTVFENIHLALEETPltREERnlRVNEHI--------EIVGLKGfekaypHELSGGMAQRVAIARGL 156
Cdd:TIGR03410 77 IAYvpQGREIFPRLTVEENLLTGLAALP--RRSR--KIPDEIyelfpvlkEMLGRRG------GDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 157 VNKPDILLLDEPfgaLDAITRS---HLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:TIGR03410 147 VTRPKLLLLDEP---TEGIQPSiikDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVME 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-233 |
1.66e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtQIKGTDL-KRGL---------IFQE-HRLLPW 97
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW---QGKPLDYsKRGLlalrqqvatVFQDpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 98 LTVFENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITR 177
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 178 SHLQAELQRIWQHEKiTMILVTHDIE------EAVYLGDRVIVMSA-RPGKI----KEIIQVPLTHP 233
Cdd:PRK13638 173 TQMIAIIRRIVAQGN-HVIISSHDIDliyeisDAVYVLRQGQILTHgAPGEVfactEAMEQAGLTQP 238
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-224 |
3.48e-21 |
|
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: 87.37 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI-KGTDLKRGLIfqehrll 95
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsDLEKALSSLI------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 96 pwLTVFENIHLAleetpltreERNLRVNehieiVGLKgfekaypheLSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:cd03247 78 --SVLNQRPYLF---------DTTLRNN-----LGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 176 TRSHLqaeLQRIWQH-EKITMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:cd03247 133 TERQL---LSLIFEVlKDKTLIWITHHL-TGIEHMDKILFLEN--GKIIM 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-215 |
4.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQ---EHRLLPwlTV 100
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLVFQnpdDQIFSP--TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHL 180
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 375134789 181 QAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-224 |
4.95e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.23 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtqiKGTDLKRgLIFQEHR-------LLPW 97
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-----EGEDIST-LKPEIYRqqvsycaQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 98 L---TVFENIHLALEEtpltreeRNLRVNEHIEIVGLKGFE------KAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:PRK10247 92 LfgdTVYDNLIFPWQI-------RNQQPDPAIFLDDLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMSARPGKIKE 224
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQPHAGEMQE 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
9-230 |
6.70e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.69 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQ------RDQnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD 82
Cdd:PRK15112 3 TLLEVRNLSKTFRyrtgwfRRQ-TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 L-----KRGLIFQE--HRLLPWLTVFENIHLALE-ETPLTREERNLRVNEHIEIVGLKGFEKAY-PHELSGGMAQRVAIA 153
Cdd:PRK15112 82 YsyrsqRIRMIFQDpsTSLNPRQRISQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 154 RGLVNKPDILLLDEPFGALDAITRS---HLQAELQriwQHEKITMILVTHDIEEAVYLGDRVIVMSA----RPGKIKEII 226
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSqliNLMLELQ---EKQGISYIYVTQHLGMMKHISDQVLVMHQgevvERGSTADVL 238
|
....
gi 375134789 227 QVPL 230
Cdd:PRK15112 239 ASPL 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-222 |
7.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL------NQTQIKGTDLKRGLIFQ--EHRLLPwLTVF 101
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgDFSKLQGIRKLVGIVFQnpETQFVG-RTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRshlQ 181
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG---I 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 375134789 182 AELQRIWQ-HEK-ITMILVTHDIEEaVYLGDRVIVMSArpGKI 222
Cdd:PRK13644 174 AVLERIKKlHEKgKTIVYITHNLEE-LHDADRIIVMDR--GKI 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
28-216 |
2.07e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL----KRGLIF--QEHRLLPWLTVF 101
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLharaRRGIGYlpQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALE-ETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITrshl 180
Cdd:PRK10895 97 DNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS---- 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 375134789 181 QAELQRIWQHEK---ITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:PRK10895 173 VIDIKRIIEHLRdsgLGVLITDHNVRETLAVCERAYIVS 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-215 |
2.13e-20 |
|
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: 86.23 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 27 LTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQEHRLL-----PWL--- 98
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAyaaqkPWLlna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 TVFENIHLaleETPLTREernlRVNEHIEIVGLKGFEKAYPH-----------ELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:cd03290 94 TVEENITF---GSPFNKQ----RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 375134789 168 PFGALDAITRSHL-QAELQRIWQHEKITMILVTHDIEeavYL--GDRVIVM 215
Cdd:cd03290 167 PFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ---YLphADWIIAM 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
29-217 |
2.64e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG-TDLKR---GLIFQEHRLLPWLTVFENI 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArARLARariGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRsHLQAEL 184
Cdd:PRK13536 136 LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR-HLIWER 214
|
170 180 190
....*....|....*....|....*....|...
gi 375134789 185 QRIWQHEKITMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:PRK13536 215 LRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-216 |
2.73e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.55 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQ--DYDGEILLNQTQIKGTDLKR-GLIFQEHRLLPWLTVFEN- 103
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETP--LTREERNLRVNEHIEIVGLKGFE-----KAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:PLN03211 162 VFCSLLRLPksLTKQEKILVAESVISELGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 375134789 177 RSHLQAELQRIWQHEKiTMILVTHDIEEAVY-LGDRVIVMS 216
Cdd:PLN03211 242 AYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYqMFDSVLVLS 281
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-224 |
3.02e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLnkSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAgldQDYD---GEILLNQTQIKG---TDL 83
Cdd:PRK11160 338 SLTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT---RAWDpqqGEILLNGQPIADyseAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQEHRL-LPWLTVFENIHLALeetPLTREERNLRVnehIEIVGL-------KGFEkAYPHE----LSGGMAQRVA 151
Cdd:PRK11160 413 RQAISVVSQRVhLFSATLRDNLLLAA---PNASDEALIEV---LQQVGLeklleddKGLN-AWLGEggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEkiTMILVTHDIEEAVYLgDRVIVMSArpGKIKE 224
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDN--GQIIE 553
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-201 |
3.22e-20 |
|
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: 83.65 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikgtdlkrglifq 90
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 ehrllpwltvfenihlaleetpltreernlrvnehIEIvglkgfekAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFG 170
Cdd:cd03221 63 -----------------------------------VKI--------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|.
gi 375134789 171 ALDAITRSHLQAELQRiwqhEKITMILVTHD 201
Cdd:cd03221 100 HLDLESIEALEEALKE----YPGTVILVSHD 126
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-225 |
3.93e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG--------TDLKR--GLIFQ--EHRLLPw 97
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikevKRLRKeiGLVFQfpEYQLFQ- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 98 LTVFENIHLALEETPLTREERNLRVNEHIEIVGL-KGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 375134789 177 RSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM--HEGKVISI 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-216 |
5.71e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG---TDLKRGL 87
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 IF--QEH--------RLL------PWLTVFENihlaleetpLTREERNLrVNEHIEIVGLKGFEKAYPHELSGGMAQRVA 151
Cdd:PRK11231 79 ALlpQHHltpegitvRELvaygrsPWLSLWGR---------LSAEDNAR-VNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAitrSHlQAELQ---RIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDI---NH-QVELMrlmRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-221 |
5.77e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL--DQDYDGEIL-----LNQTQI 78
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIfegeeLQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 79 KGTDlKRG--LIFQEHRLLPWLTVFENIHLALEETPLTR---EERNLRVNEHIEIVGLkGFEKAYP-HELSGGMAQRVAI 152
Cdd:PRK13549 77 RDTE-RAGiaIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLqAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGK 221
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVL-LDIIRDLKAHGIACIYISHKLNEVKAISDTICVI--RDGR 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-224 |
1.08e-19 |
|
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: 87.95 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdYD---GEILlnqtqIKGTDLK-------RGLI--------- 88
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF---YDvtsGRIL-----IDGQDIRdvtqaslRAAIgivpqdtvl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEhrllpwlTVFENIHLALEETplTREErnlrVNE-----HIE--IVGL-KGFE--------KaypheLSGGMAQRVAI 152
Cdd:COG5265 444 FND-------TIAYNIAYGRPDA--SEEE----VEAaaraaQIHdfIESLpDGYDtrvgerglK-----LSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEkiTMILVTH---DIEEAvylgDRVIVMSArpGKIKE 224
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHrlsTIVDA----DEILVLEA--GRIVE 572
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-212 |
1.17e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT---------QIKGTDLKR--GLIFQEHR 93
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLRKevGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 LLPWLTVFENIHLALEETPLtREERNLR--VNEHIEIVGLkgFEKAY------PHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGI-KEKREIKkiVEECLRKVGL--WKEVYdrlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 166 DEPFGALDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRV 212
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-222 |
2.93e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQ-NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL---------------DQDYDGE--- 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyiGDKKNNHeli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 71 ILLNQTQIKgtDLKR-----GLIFQ--EHRLLPwLTVFENIHLALEETPLTREERNLRVNEHIEIVGLK-GFEKAYPHEL 142
Cdd:PRK13631 101 TNPYSKKIK--NFKElrrrvSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 143 SGGMAQRVAIARGLVNKPDILLLDEPFGALDAiTRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK--GKI 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-241 |
3.77e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.82 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 5 YMSFSLLSIKKLNKSFQRDQNtltvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLk 84
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 RGLIFQEHRLL---PWLTVFENIHLALE----------ETPLTREER---NLRVN-----EHIEIvGLKGFEKAyPHELS 143
Cdd:PRK11701 76 YALSEAERRRLlrtEWGFVHQHPRDGLRmqvsaggnigERLMAVGARhygDIRATagdwlERVEI-DAARIDDL-PTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 144 GGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIK 223
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM--KQGRVV 231
|
250 260
....*....|....*....|.
gi 375134789 224 E---IIQVpLTHPRHKESELL 241
Cdd:PRK11701 232 EsglTDQV-LDDPQHPYTQLL 251
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-241 |
3.82e-19 |
|
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: 83.73 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNtltvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRgLIF 89
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQ-LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLL---PWLTVFENIHLALE----------ETPLTREER---NLRVNEH-----IEIVGLKGFEKayPHELSGGMAQ 148
Cdd:TIGR02323 78 AERRRLmrtEWGFVHQNPRDGLRmrvsaganigERLMAIGARhygNIRATAQdwleeVEIDPTRIDDL--PRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 149 RVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKE--II 226
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVEsgLT 233
|
250
....*....|....*
gi 375134789 227 QVPLTHPRHKESELL 241
Cdd:TIGR02323 234 DQVLDDPQHPYTQLL 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-215 |
5.00e-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: 85.65 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL--DQDYDGEILLNQTQIKGTDLKR-- 85
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ----GLIFQEHRLLPWLTVFENIHLALEET-PLTREERN---LRVNEHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGL 156
Cdd:TIGR02633 77 ragiVIIHQELTLVPELSVAENIFLGNEITlPGGRMAYNamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 157 VNKPDILLLDEPFGALdaiTRSHLQAELQ--RIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:TIGR02633 157 NKQARLLILDEPSSSL---TEKETEILLDiiRDLKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-224 |
5.48e-19 |
|
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: 85.95 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKgtDLKRGLIFQEHRLLPWL------TVFE 102
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK--DIDRHTLRQFINYLPQEpyifsgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NihLALEETPLTREERNLRVNEHIEI-VGLKGFEKAYPHEL-------SGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:TIGR01193 567 N--LLLGAKENVSQDEIWAACEIAEIkDDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 175 ITRSHLQAELQRIwQHEkiTMILVTHDIEEAvYLGDRVIVMSArpGKIKE 224
Cdd:TIGR01193 645 ITEKKIVNNLLNL-QDK--TIIFVAHRLSVA-KQSDKIIVLDH--GKIIE 688
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-224 |
6.38e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtqikGTDLKRGLIF 89
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLL-PWLTVFENIHLALEETpltrEERNLRvnehiEIVGLKGF--EKAY-P-HELSGGMAQRVAIARGLVNKPDILL 164
Cdd:COG0488 385 QHQEELdPDKTVLDELRDGAPGG----TEQEVR-----GYLGRFLFsgDDAFkPvGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 165 LDEPFGALDAITRSHLQAELQRiWQHekiTMILVTHD---IEEAVylgDRVIVMsaRPGKIKE 224
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDD-FPG---TVLLVSHDryfLDRVA---TRILEF--EDGGVRE 509
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-215 |
7.42e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI--KGTD-------LKRGLIFQehrlLPWLTV 100
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDkyirpvrKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FE-NIHLALEETPltreeRNLRVNehIEIVGLK--------GFEK----AYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:PRK13646 99 FEdTVEREIIFGP-----KNFKMN--LDEVKNYahrllmdlGFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 375134789 168 PFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-225 |
8.58e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 20 FQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQI------KGTDLKRGL--IFQE 91
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgKLQALRRDIqfIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 --HRLLPWLTVFENIHLALEETPLTR-EERNLRVNEHIEIVGLKGfEKA--YPHELSGGMAQRVAIARGLVNKPDILLLD 166
Cdd:PRK10261 410 pyASLDPRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 167 EPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSArpGKIKEI 225
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL--GQIVEI 545
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-219 |
1.48e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLR-------LIAGLDqdYDGEIL-----LNQTQIKGTDLKR--GLIFQEHRLL 95
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTfhgknLYAPDVDPVEVRRriGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 96 PwLTVFENIHLA---------LEETPltreERNLR-------VNEHIEIVGLkgfekayphELSGGMAQRVAIARGLVNK 159
Cdd:PRK14243 104 P-KSIYDNIAYGaringykgdMDELV----ERSLRqaalwdeVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRVIVMSARP 219
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNVEL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-222 |
1.90e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF-----QEHRLLPWLT 99
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdaIRAGIAYvpedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFENIHLA-LEET----PLTREERNLRVNEHIEIVGLKgfekaYPH------ELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:COG1129 347 IRENITLAsLDRLsrggLLDRRRERALAEEYIKRLRIK-----TPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 169 F-----GAldaitrshlQAELQRIWQ---HEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG1129 422 TrgidvGA---------KAEIYRLIRelaAEGKAVIVISSELPELLGLSDRILVMRE--GRI 472
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-216 |
4.07e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasrrv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLAleETP-LTR-----EERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNK 159
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMG--RTPhRSRfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 160 PDILLLDEPFGALDaITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:PRK09536 158 TPVLLLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-243 |
4.30e-18 |
|
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: 82.93 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQ--DYDGEILLN-------------- 74
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 75 ----QTQIKGTDLKR--------------------GLIFQE-HRLLPWLTVFENIHLALEETPLTREERNLRVNEHIEIV 129
Cdd:TIGR03269 77 kvgePCPVCGGTLEPeevdfwnlsdklrrrirkriAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 130 GLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTH------DI- 202
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLs 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 375134789 203 EEAVYLGDRVIVMSARPGKIKEIIQVPLTHPRhKESELLFG 243
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAVFMEGVSEVE-KECEVEVG 276
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-215 |
4.67e-18 |
|
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: 80.21 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEHRLLPwLTVFEN 103
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlhskvSLVGQEPVLFA-RSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTR-EERNLRVNEHIEIvglKGFEKAYPHE-------LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:cd03248 108 IAYGLQSCSFECvKEAAQKAHAHSFI---SELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 375134789 176 TRSHLQAELQRiwQHEKITMILVTHDIeEAVYLGDRVIVM 215
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRL-STVERADQILVL 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-245 |
6.02e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 23 DQNTL-----TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEH 92
Cdd:PRK10253 11 EQLTLgygkyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 93 RLLPWLTVFENIHLA-LEETPLT---REERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:PRK10253 91 TTPGDITVQELVARGrYPHQPLFtrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI------KEIIQVPLThprhkesELLF 242
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIvaqgapKEIVTAELI-------ERIY 241
|
...
gi 375134789 243 GFR 245
Cdd:PRK10253 242 GLR 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-215 |
8.12e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLK---RGLIFQEHRLLP--WLTVFE 102
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQLPAaeGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NI-------HLALEEtpLTREERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:PRK10575 105 LVaigrypwHGALGR--FGAADRE-KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 375134789 176 TRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-200 |
1.12e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD---LKR--GLIFQEhrllPWL---TV 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhyLHRqvALVGQE----PVLfsgSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPLTrEERNLRV--NEHIEIvglKGFEKAYPHE-------LSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:TIGR00958 572 RENIAYGLTDTPDE-EIMAAAKaaNAHDFI---MEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180
....*....|....*....|....*....
gi 375134789 172 LDAITRSHLQAELQRiwqhEKITMILVTH 200
Cdd:TIGR00958 648 LDAECEQLLQESRSR----ASRTVLLIAH 672
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-215 |
1.35e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.62 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDyDGEILLNQTQIKGTDLKRGLIF 89
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKD-NWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLlpwltVFENIHLALEE-----TPLTREERNL-------------------RVNEHIEI---VGLKGFE---KAYP 139
Cdd:PRK15093 82 ERRKL-----VGHNVSMIFQEpqsclDPSERVGRQLmqnipgwtykgrwwqrfgwRKRRAIELlhrVGIKDHKdamRSFP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 140 HELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-174 |
2.93e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQEHR--LLPWLTVFE 102
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 103 NIHLALEetplTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:PRK13539 93 NLEFWAA----FLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-238 |
6.42e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQD-----YDGEILLNQTQIKG----TDLKR--GLIFQEHRLLP 96
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNyrdvLEFRRrvGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 wLTVFENIHLALEETPLT-REERNLRVNEHIEIVGL----KGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:PRK14271 115 -MSIMDNVLAGVRAHKLVpRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 172 LDAITRSHLQAELQRIwqHEKITMILVTHDIEEAVYLGDRVIVMSarPGKIKE--IIQVPLTHPRHKES 238
Cdd:PRK14271 194 LDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFF--DGRLVEegPTEQLFSSPKHAET 258
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-224 |
6.76e-17 |
|
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: 76.76 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKST----LLRLIagldQDYDGEILLNQTQIKGTDLKR-----GLIFQEhrllPWL- 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrsriSIIPQD----PVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 --TVFENIhlaleeTPLTR--EErnlRVNEHIEIVGLKGFEKAYPHEL-----------SGGMAQRVAIARGLVNKPDIL 163
Cdd:cd03244 91 sgTIRSNL------DPFGEysDE---ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 164 LLDEPFGALDAITRSHLQAELQRIWQHekITMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKD--CTVLTIAHRL-DTIIDSDRILVLDK--GRVVE 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-205 |
7.56e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 22 RDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGldqdydgeiLLNQTQIKGT-DLKRGLIFQEhrllpwLTV 100
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------ALKGTPVAGCvDVPDNQFGRE------ASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHlaleetpltreeRNLRVNEHIEIVGLKGFEKAY-----PHELSGGMAQRVAIARGLVNKPDILLLDEpFGA-LDA 174
Cdd:COG2401 103 IDAIG------------RKGDFKDAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDR 169
|
170 180 190
....*....|....*....|....*....|...
gi 375134789 175 ITRSHLQAELQRIWQHEKITMILVTH--DIEEA 205
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHhyDVIDD 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-222 |
1.88e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQ------TQIKGTDL 83
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarlTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQEHRLLPWLTVFENIHLALEETPLTREernlRVNEHIEIVG--LKgfekayPHELSGGM----AQRVAIARGLV 157
Cdd:PRK15439 87 GIYLVPQEPLLFPNLSVKENILFGLPKRQASMQ----KMKQLLAALGcqLD------LDSSAGSLevadRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 158 NKPDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVM--RDGTI 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-216 |
2.09e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.52 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN----QTQIKGTDLKRGLIFQEHRLLPWLTVFENIH 105
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdiETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 106 LALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRshlqaelQ 185
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR-------R 1098
|
170 180 190
....*....|....*....|....*....|....*.
gi 375134789 186 RIWQ-----HEKITMILVTHDIEEAVYLGDRVIVMS 216
Cdd:TIGR01257 1099 SIWDlllkyRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-225 |
4.42e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 77.68 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 12 SIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILL--------NQTQIKGTDL 83
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkgsvayvpQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRGLIFQeHRLLPwltvfENIHLALEETPLTREERNLRVNEHIEIvGLKGFEkaypheLSGGMAQRVAIARGLVNKPDIL 163
Cdd:TIGR00957 716 RENILFG-KALNE-----KYYQQVLEACALLPDLEILPSGDRTEI-GEKGVN------LSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 164 LLDEPFGALDAITRSHlqaelqrIWQH--------EKITMILVTHDIEeavYLG--DRVIVMSArpGKIKEI 225
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKH-------IFEHvigpegvlKNKTRILVTHGIS---YLPqvDVIIVMSG--GKISEM 842
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-252 |
6.91e-16 |
|
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: 76.71 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTDLKR----------GLIFQEHRLLPWl 98
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-----GADLSQwdreelgrhiGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 TVFENIhlA-LEEtpLTREE-----RNLRVNEHIEivglkGFEKAY-------PHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG4618 421 TIAENI--ArFGD--ADPEKvvaaaKLAGVHEMIL-----RLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 166 DEPFGALDAITRSHLQAELQRIWQHeKITMILVTHD--IEEAVylgDRVIVMsaRPGKIKeiiqvplthprhkeselLFG 243
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRpsLLAAV---DKLLVL--RDGRVQ-----------------AFG 548
|
....*....
gi 375134789 244 FRNQALNML 252
Cdd:COG4618 549 PRDEVLARL 557
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-214 |
1.01e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 20 FQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqikGTD--------LKR-GLIF- 89
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVpfkrrkefARRiGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFE--NIHLALEETPltREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:COG4586 103 QRSQLWWDLPAIDsfRLLKAIYRIP--DAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 168 PFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIV 214
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-215 |
1.03e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIkgTDLKR 85
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQ----ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI--TDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQE--------HRLLPWLTVFENihLALEETPLTREERNLRVNEHIEIvglkgFEKAYPHE------LSGGMAQRVA 151
Cdd:PRK11614 75 AKIMREavaivpegRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYEL-----FPRLHERRiqragtMSGGEQQMLA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 152 IARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVL 210
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-222 |
1.16e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTDL-----KRGLIFQEHRLLPWLTVFENI 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAaelarHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALEEtPLTREERNLRVNEHIEIVGLkgfEKAYP---HELSGGMAQRVAIARGL------VNkPD--ILLLDEPFGALD 173
Cdd:COG4138 91 ALHQPA-GASSEAVEQLLAQLAEALGL---EDKLSrplTQLSGGEWQRVRLAAVLlqvwptIN-PEgqLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 375134789 174 AITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMSArpGKI 222
Cdd:COG4138 166 VAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQ--GKL 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-200 |
2.73e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtqikGTDLKRGLIFQEHRllPWLTVfenihla 107
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFLPQR--PYLPL------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 108 leetpltreeRNLRvnehiEIVglkgfekAYP--HELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITrshlQAELQ 185
Cdd:cd03223 78 ----------GTLR-----EQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES----EDRLY 131
|
170
....*....|....*
gi 375134789 186 RIWQHEKITMILVTH 200
Cdd:cd03223 132 QLLKELGITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-221 |
2.78e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL--DQDYDGEILLNQTQIKGTDLK----RGL--IFQEHRLLPWLTVF 101
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRdseaLGIviIHQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETP---LTREERNLRVNEHIEIVGLKgfEKayPHELSG----GMAQRVAIARGLVNKPDILLLDEPFGALDA 174
Cdd:NF040905 97 ENIFLGNERAKrgvIDWNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 175 ITRSHLqAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGK 221
Cdd:NF040905 173 EDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGR 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-215 |
6.69e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR 85
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 ------GLIFQEHRLLPWLTVFENIHLALEETP-------LTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAI 152
Cdd:PRK09700 77 aaqlgiGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 153 ARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-224 |
1.09e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.07 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLiagLDQDYD---GEILLNQTQIKGTDLKR-----GLI 88
Cdd:PRK13657 339 DVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL---LQRVFDpqsGRILIDGTDIRTVTRASlrrniAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPwLTVFENIHL----ALEETPLTREERNlRVNEHIE--------IVGLKGfekaypHELSGGMAQRVAIARGL 156
Cdd:PRK13657 415 FQDAGLFN-RSIEDNIRVgrpdATDEEMRAAAERA-QAHDFIErkpdgydtVVGERG------RQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 157 VNKPDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMI----LVThdIEEAvylgDRVIVMSArpGKIKE 224
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIiahrLST--VRNA----DRILVFDN--GRVVE 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-224 |
1.89e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEHRLLPwLTVFENI 104
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrnqvALVSQNVHLFN-DTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALEETpLTREE-----RNLRVNEHIE--------IVGLKGFEkaypheLSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:PRK11176 438 AYARTEQ-YSREQieeaaRMAYAMDFINkmdngldtVIGENGVL------LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 172 LDAITRSHLQAELQRIwQHEKiTMILVTH---DIEEAvylgDRVIVMSArpGKIKE 224
Cdd:PRK11176 511 LDTESERAIQAALDEL-QKNR-TSLVIAHrlsTIEKA----DEILVVED--GEIVE 558
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-200 |
2.05e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNtltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD---LKRGL 87
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 88 -IFQEHRLLPWLTVFENIHLAleetpltREERNLRVNEHIEIVGLKGFEKAYP-----------HELSGGMAQRVAIARG 155
Cdd:PRK10790 418 aMVQQDPVVLADTFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 375134789 156 LVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHekITMILVTH 200
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-221 |
2.35e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrDQNTLTVLDGinlNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT-----QIKGTDlk 84
Cdd:PRK13409 340 LVEYPDLTKKL--GDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpQYIKPD-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 rglifQEHRLLPWLtvfENIHLALEETPLTreernlrvNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:PRK13409 413 -----YDGTVEDLL---RSITDDLGSSYYK--------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 165 LDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGK 221
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
37-221 |
2.69e-14 |
|
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: 68.75 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 37 IEQGEFISIVGSSGCGKSTLLRLIAGldqdydgeillnqtQIKGTDlkrglifqehrllpwltvfenihlaleetpltre 116
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG--------------QLIPNG---------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 117 ernlrvnEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMI 196
Cdd:cd03222 54 -------DNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170 180
....*....|....*....|....*
gi 375134789 197 LVTHDIEEAVYLGDRVIVMSARPGK 221
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGEPGV 151
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-221 |
3.76e-14 |
|
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: 71.35 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFqrDQNTLTVLDGinlNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLN----------QTQIK 79
Cdd:COG1245 341 LVEYPDLTKSY--GGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 80 GT--DLKRGLIFQehrllPWLTVFENIHLAleeTPLTRE---ERNLRvnehieivglkgfekayphELSGGMAQRVAIAR 154
Cdd:COG1245 416 GTveEFLRSANTD-----DFGSSYYKTEII---KPLGLEkllDKNVK-------------------DLSGGELQRVAIAA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 155 GLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMSARPGK 221
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGV 535
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-222 |
4.81e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL---KR-GLIFQEHRLLPWLTVFEN 103
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIatrRRvGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 I--HLALEETPltREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRS--- 178
Cdd:NF033858 360 LelHARLFHLP--AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDmfw 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 179 HLQAELQRiwqHEKITMILVTHDIEEAVyLGDRVIVMSArpGKI 222
Cdd:NF033858 438 RLLIELSR---EDGVTIFISTHFMNEAE-RCDRISLMHA--GRV 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-222 |
5.38e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF-QEHR----LLPWLTV 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdgLANGIVYiSEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHL-ALEE-----TPLTREERNLRVNEHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PRK10762 348 KENMSLtALRYfsragGSLKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 375134789 174 AITRSHLqaeLQRIWQ--HEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:PRK10762 428 VGAKKEI---YQLINQfkAEGLSIILVSSEMPEVLGMSDRILVM--HEGRI 473
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-173 |
6.14e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 6.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGLIFQEH--RLLP 96
Cdd:PRK13543 18 AFSR--NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 97 WLTVFENIHL--ALEetplTREERNLRVNEhIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PRK13543 96 DLSTLENLHFlcGLH----GRRAKQMPGSA-LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-225 |
7.79e-14 |
|
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: 68.21 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKR-----GLIFQEHRLLPWlTVFEN 103
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREErNLRVNEHieivGLKgfekaypheLSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITrshlQAE 183
Cdd:cd03369 102 LDPFDEYSDEEIYG-ALRVSEG----GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT----DAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 375134789 184 LQRIWQHE--KITMILVTHDIeEAVYLGDRVIVMSArpGKIKEI 225
Cdd:cd03369 164 IQKTIREEftNSTILTIAHRL-RTIIDYDKILVMDA--GEVKEY 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-173 |
8.45e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG---LDqdyDGEILLNQtqikgtDLK------------RGLIF----- 89
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLD---DGRIIYEQ------DLIvarlqqdpprnvEGTVYdfvae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 --QEhrLLPWLTVFENIHLALEETPltrEERNL--------------------RVNEHIEIVGLKGFEKAypHELSGGMA 147
Cdd:PRK11147 90 giEE--QAEYLKRYHDISHLVETDP---SEKNLnelaklqeqldhhnlwqlenRINEVLAQLGLDPDAAL--SSLSGGWL 162
|
170 180
....*....|....*....|....*.
gi 375134789 148 QRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-229 |
1.32e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 18 KSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL---LNQTQIKGTDLKRGLIFQEHrl 94
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdIPLTKLQLDSWRSRLAVVSQ-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 95 LPWL---TVFENIHLAL-EETPLTREERNLRVNEHIEIVGL-KGFEKAYPHE---LSGGMAQRVAIARGLVNKPDILLLD 166
Cdd:PRK10789 397 TPFLfsdTVANNIALGRpDATQQEIEHVARLASVHDDILRLpQGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 167 EPFGALDAITRSHLQAELqRIWQHEKiTMILVTHDIeEAVYLGDRVIVMS----ARPGKIKEIIQVP 229
Cdd:PRK10789 477 DALSAVDGRTEHQILHNL-RQWGEGR-TVIISAHRL-SALTEASEILVMQhghiAQRGNHDQLAQQS 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-239 |
1.65e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKL---NKSFQRD-QNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQ-IKGTDL 83
Cdd:PTZ00265 376 KLKDIKKIqfkNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KR-----GLIFQEhRLLPWLTVFENIHLAL--------------EETPLTREERNLRV-------------------NEH 125
Cdd:PTZ00265 456 KWwrskiGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynEDGNDSQENKNKRNscrakcagdlndmsnttdsNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 126 IEI------------------VGLKGFEKAYP-----------HELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:PTZ00265 535 IEMrknyqtikdsevvdvskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375134789 177 RSHLQAELQRIWQHEKITMILVTHDIEEAVYlGDRVIVMSARPGKIKEIIQVPLTHPRHKESE 239
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDPTKDNKE 676
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-232 |
2.22e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 18 KSFQRDQNTLTVLDGINlnieqgEFISIVGSSGCGKSTLLRliagldqdYDGEILLNQTQIKGTDLK--RGL--IFQEHR 93
Cdd:PTZ00265 1240 QDYQGDEEQNVGMKNVN------EFSLTKEGGSGEDSTVFK--------NSGKILLDGVDICDYNLKdlRNLfsIVSQEP 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 LLPWLTVFENIHLALEETPLTREERNLR---VNEHIEIVGLKGFEKAYPH--ELSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:PTZ00265 1306 MLFNMSIYENIKFGKEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKITMILVTHDIeEAVYLGDRVIVMSaRPGKIKEIIQVPLTH 232
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFN-NPDRTGSFVQAHGTH 1447
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-216 |
4.30e-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: 66.13 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 8 FSLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDY---DGEILLNQTQIKGTDLK 84
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 85 --RGLIF--QEHRLLPWLTVFENIHLALeetpltreerNLRVNEHIeivglKGFekayphelSGGMAQRVAIARGLVNKP 160
Cdd:cd03233 81 ypGEIIYvsEEDVHFPTLTVRETLDFAL----------RCKGNEFV-----RGI--------SGGERKRVSIAEALVSRA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 161 DILLLDEPFGALDAITRSHLQAELQRIWQHEKIT-MILVTHDIEEAVYLGDRVIVMS 216
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLY 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-214 |
4.71e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGL------IFQEHRLLPWLTVFEN 103
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALaagvaiIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLAleETP-----LTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRS 178
Cdd:PRK11288 100 LYLG--QLPhkggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 375134789 179 HLQAELQRIWQHEKItMILVTHDIEEAVYLGDRVIV 214
Cdd:PRK11288 178 QLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITV 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-192 |
5.28e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQrDQntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKgTDL---KRG 86
Cdd:PRK13540 1 MLDVIELDFDYH-DQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLctyQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 87 LIFQEHR--LLPWLTVFENIHLALEETpltreERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILL 164
Cdd:PRK13540 76 LCFVGHRsgINPYLTLRENCLYDIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180
....*....|....*....|....*...
gi 375134789 165 LDEPFGALDAITrshLQAELQRIWQHEK 192
Cdd:PRK13540 151 LDEPLVALDELS---LLTIITKIQEHRA 175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-222 |
7.15e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtQIKGTDL--KRglifqeHR------------ 93
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLGGDMadAR------HRravcpriaympq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 94 -----LLPWLTVFENI--------HlaleetplTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKP 160
Cdd:NF033858 84 glgknLYPTLSVFENLdffgrlfgQ--------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 161 DILLLDEPFGALDAITRSH---LQAELQRiwQHEKITMILVTHDIEEAVYLgDRVIVMSArpGKI 222
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQfweLIDRIRA--ERPGMSVLVATAYMEEAERF-DWLVAMDA--GRV 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-224 |
7.66e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.24 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDqDY---DGEILLNqtqikGTDL---------KRG--LIFQ--- 90
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHP-KYevtSGSILLD-----GEDIlelspderaRAGifLAFQypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EhrlLPWLTVFENIHLALE---ETPLTREERNLRVNEHIEIVGL-KGFEKAYPHE-LSGGMAQRVAIARGLVNKPDILLL 165
Cdd:COG0396 88 E---IPGVSVSNFLRTALNarrGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 166 DEPFGALDaitrshlqaelqrIW------------QHEKITMILVTH-----DIEEAvylgDRVIVMSArpGKIKE 224
Cdd:COG0396 165 DETDSGLD-------------IDalrivaegvnklRSPDRGILIITHyqrilDYIKP----DFVHVLVD--GRIVK 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-222 |
7.97e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNksfQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKR 85
Cdd:COG3845 257 VLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSprerRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIF-----QEHRLLPWLTVFENihLALEETPLTREERNLRVNEH------IEIVglKGFEKAYPHE------LSGGMAQ 148
Cdd:COG3845 334 GVAYipedrLGRGLVPDMSVAEN--LILGRYRRPPFSRGGFLDRKairafaEELI--EEFDVRTPGPdtparsLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 149 RVAIARGLVNKPDILLLDEP-----FGALDAItrshlqaelqriwqHEKITM--------ILVTHDIEEAVYLGDRVIVM 215
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPtrgldVGAIEFI--------------HQRLLElrdagaavLLISEDLDEILALSDRIAVM 475
|
....*..
gi 375134789 216 SArpGKI 222
Cdd:COG3845 476 YE--GRI 480
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-222 |
9.21e-13 |
|
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: 65.24 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGlDQDY---DGEILLnqtqiKGTDL---------KRG--LIFQEhrl 94
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYevtEGEILF-----KGEDItdlppeeraRLGifLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 95 lPwltvfenihlalEETPLTREERNLR-VNEhieivglkGFekayphelSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:cd03217 86 -P------------PEIPGVKNADFLRyVNE--------GF--------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 174 aITRSHLQAELQRIWQHEKITMILVTHDIEEAVYL-GDRVIVMSArpGKI 222
Cdd:cd03217 137 -IDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYD--GRI 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-224 |
5.25e-12 |
|
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: 65.35 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIL---LNQTQIKGTDLKRGLIfqehrLLPWLTVFENIH 105
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidgLNIAKIGLHDLRFKIT-----IIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 106 LALEETPLTR--EErnlRVNEHIEIVGLKGFEKAYP----HE-------LSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:TIGR00957 1376 LRMNLDPFSQysDE---EVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 173 DAITRSHLQAELQRiwQHEKITMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:TIGR00957 1453 DLETDNLIQSTIRT--QFEDCTVLTIAHRL-NTIMDYTRVIVLDK--GEVAE 1499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
7.01e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 21 QRDQNTLTVLD-------GINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF 89
Cdd:PRK15439 263 AAGAPVLTVEDltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrLARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 -----QEHRL-----LPW----LTVFEN---IHLALEETPLTREER--NLRVNEHIEIVGlkgfekayphELSGGMAQRV 150
Cdd:PRK15439 343 lpedrQSSGLyldapLAWnvcaLTHNRRgfwIKPARENAVLERYRRalNIKFNHAEQAAR----------TLSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375134789 151 AIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVM 215
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-220 |
9.36e-12 |
|
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: 63.15 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 40 GEFISIVGSSGCGKSTLLRLIAGL----------DQDYD-------GEILLNQ-TQIKGTDLKRGLIFQEHRLLPwLTVF 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddPPDWDeildefrGSELQNYfTKLLEGDVKVIVKPQYVDLIP-KAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETpltrEERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQ 181
Cdd:cd03236 105 GKVGELLKKK----DERG-KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 375134789 182 AELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMSARPG 220
Cdd:cd03236 180 RLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
37-217 |
1.22e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 37 IEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQT---QIKGTDL--KRGLIFQEHRLLPWLTVFEniHLALEET 111
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQpleAWSAAELarHRAYLSQQQTPPFAMPVFQ--YLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 112 PLTRE-ERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVN-KPDI------LLLDEPFGALDaITRshlQAE 183
Cdd:PRK03695 96 DKTRTeAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD-VAQ---QAA 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 375134789 184 LQRIWQH---EKITMILVTHDIEEAVYLGDRVIVMSA 217
Cdd:PRK03695 172 LDRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-225 |
1.41e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLkrglifQEHRLLpWLTVFENIHL------ 106
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP------EDYRKL-FSAVFTDFHLfdqllg 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 107 --------ALEETPLTREERNLRVN-EHIEIVGLKgfekaypheLSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITR 177
Cdd:PRK10522 415 pegkpanpALVEKWLERLKMAHKLElEDGRISNLK---------LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 375134789 178 SHLQAELQRIWQHEKITMILVTHDiEEAVYLGDRVIVMsaRPGKIKEI 225
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEM--RNGQLSEL 530
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-202 |
1.90e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQntltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikgtdLKRGLI 88
Cdd:PRK09544 3 SLVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------LRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 89 FQEHRLLPWLtvfenihlaleetPLTrEERNLRVNEHIE----IVGLKGFEKAYPHE-----LSGGMAQRVAIARGLVNK 159
Cdd:PRK09544 73 PQKLYLDTTL-------------PLT-VNRFLRLRPGTKkediLPALKRVQAGHLIDapmqkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDI 202
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-174 |
2.81e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 9 SLLSIKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG--LDQDYDGEILLNQTQIKGTDLKR- 85
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRSt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEHRLLPWLTVFENIHLALEETPLTREERnlrvnehieivglkgfekayphelsggmaQRVAIARGLVNKPDILLL 165
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRGLSVEQR-----------------------------KRLTIGVELAAKPSILFL 132
|
....*....
gi 375134789 166 DEPFGALDA 174
Cdd:cd03232 133 DEPTSGLDS 141
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-224 |
3.60e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKklNKSFQRDQNTLT-VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdqdydgeilLNQTQIKGTDLKRGLIF 89
Cdd:PLN03232 615 ISIK--NGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE---------LSHAETSSVVIRGSVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHrlLPWL---TVFENIHL-----------ALEETPLTREERNLRVNEHIEIvGLKGFEkaypheLSGGMAQRVAIARG 155
Cdd:PLN03232 684 VPQ--VSWIfnaTVRENILFgsdfeserywrAIDVTALQHDLDLLPGRDLTEI-GERGVN------ISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 156 LVNKPDILLLDEPFGALDA-----ITRSHLQAELQriwqheKITMILVTHDIeEAVYLGDRVIVMSArpGKIKE 224
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAhvahqVFDSCMKDELK------GKTRVLVTNQL-HFLPLMDRIILVSE--GMIKE 819
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-215 |
3.62e-11 |
|
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: 61.80 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI-------LLNQTQ--IKGT---DLKRGLIFQEHRllp 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisFSSQFSwiMPGTikeNIIFGVSYDEYR--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 WLTVFENIHlaLEETPLTREERNLRVnehieiVGLKGFekayphELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAIT 176
Cdd:cd03291 129 YKSVVKACQ--LEEDITKFPEKDNTV------LGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 375134789 177 RSHL-QAELQRIWQHEkiTMILVTHDIEEaVYLGDRVIVM 215
Cdd:cd03291 195 EKEIfESCVCKLMANK--TRILVTSKMEH-LKKADKILIL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-202 |
4.35e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 24 QNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTdLKRGLI--FQEHRLLPWL--T 99
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVayVPQSEEVDWSfpV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFENI-------HLALEETPLTREERnlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGAL 172
Cdd:PRK15056 96 LVEDVvmmgrygHMGWLRRAKKRDRQ--IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|
gi 375134789 173 DAITRSHLQAELQRIwQHEKITMILVTHDI 202
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNL 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-224 |
4.92e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKklNKSFQRD-QNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG-LDQDYDGEILLNQT-----QIKgtdl 83
Cdd:PLN03130 615 ISIK--NGYFSWDsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvpQVS---- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 krgLIFQEhrllpwlTVFENIHLALEETPlTREERNLRVN------------EHIEIvGLKGFEkaypheLSGGMAQRVA 151
Cdd:PLN03130 689 ---WIFNA-------TVRDNILFGSPFDP-ERYERAIDVTalqhdldllpggDLTEI-GERGVN------ISGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 152 IARGLVNKPDILLLDEPFGALDA-----ITRSHLQAELQriwqheKITMILVTHDIEEAVYLgDRVIVMSArpGKIKE 224
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAhvgrqVFDKCIKDELR------GKTRVLVTNQLHFLSQV-DRIILVHE--GMIKE 819
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-221 |
6.09e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQrdqnTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI--LLNQTQIKGTDLKR-- 85
Cdd:PRK10762 4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlyLGKEVTFNGPKSSQea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 --GLIFQEHRLLPWLTVFENIHLALEETP-----------------LTReeRNLRVNEHiEIVGlkgfekayphELSGGM 146
Cdd:PRK10762 80 giGIIHQELNLIPQLTIAENIFLGREFVNrfgridwkkmyaeadklLAR--LNLRFSSD-KLVG----------ELSIGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 147 AQRVAIARGLVNKPDILLLDEPFGAL-DAITRSHLQA--ELQRiwQHEKITMIlvTHDIEEAVYLGDRVIVMsaRPGK 221
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVirELKS--QGRGIVYI--SHRLKEIFEICDDVTVF--RDGQ 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-203 |
1.06e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtqikgtdlKRGLIFQEHRLLPWL---TVFENI- 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSGRISFSPQTSWImpgTIKDNIi 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 -HLALEETPLTREERNLRVNEHIEIVGLKgfEKAYPHE----LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSH 179
Cdd:TIGR01271 509 fGLSYDEYRYTSVIKACQLEEDIALFPEK--DKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180
....*....|....*....|....*
gi 375134789 180 L-QAELQRIWQHEkiTMILVTHDIE 203
Cdd:TIGR01271 587 IfESCLCKLMSNK--TRILVTSKLE 609
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-173 |
1.76e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEI---------LLNQTQIKGTDLKRGLIFQEHRLLPWLTvfen 103
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCFPGVP---- 603
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375134789 104 ihlaleetpltreERNLRVneHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PLN03073 604 -------------EQKLRA--HLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-176 |
5.12e-10 |
|
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: 59.18 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikgtdLKRGLIFQ 90
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------VKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EHRLL-PWLTVFENIHLALEETPLTREERNLRVnehieIVGLKGFEKA----YPHELSGGMAQRVAIARGLVNKPDILLL 165
Cdd:TIGR03719 393 SRDALdPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKGSdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170
....*....|.
gi 375134789 166 DEPFGALDAIT 176
Cdd:TIGR03719 468 DEPTNDLDVET 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-223 |
7.25e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL-DQDYDGEILLNQTQIK----GTDLKRGLIF-----QEHRLLPWLT 99
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDirnpAQAIRAGIAMvpedrKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFENIHLALEETPLTR----EERNLR-VNEHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKmridAAAELQiIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 174 AITRSHLQAELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGE--GKLK 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-217 |
8.50e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGldqDY-----------DGEILLNQTQIKGTDLK-----RGLIFQE 91
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLtgggaprgarvTGDVTLNGEPLAAIDAPrlarlRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRLLPWLTVFENIHL-----ALEETPLTREERNLrVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVN-------- 158
Cdd:PRK13547 92 AQPAFAFSAREIVLLgryphARRAGALTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 159 -KPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVYLGDRvIVMSA 217
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADR-IAMLA 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-226 |
1.23e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTD----LKRGLIF-----QEHRLLPWLTVFEN 103
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldaVKKGMAYitesrRDNGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLA-----------------LEETPLTREERNL------RVNEHIEivglkgfekayphELSGGMAQRVAIARGLVNKP 160
Cdd:PRK09700 362 MAISrslkdggykgamglfheVDEQRTAENQRELlalkchSVNQNIT-------------ELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 161 DILLLDEPFGALDAITRSHLQaELQRIWQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGKIKEII 226
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIY-KVMRQLADDGKVILMVSSELPEIITVCDRIAVF--CEGRLTQIL 491
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-201 |
2.69e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 28 TVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqtqiKGTDLKrglIFQEHRLLpwltvfeniHLA 107
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----KGIKLG---YFAQHQLE---------FLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 108 LEETPLT-------RE-ERNLRvnEHIEIVGLKGFEKAYPHE-LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRs 178
Cdd:PRK10636 390 ADESPLQhlarlapQElEQKLR--DYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR- 466
|
170 180
....*....|....*....|...
gi 375134789 179 hlQAELQRIWQHEKiTMILVTHD 201
Cdd:PRK10636 467 --QALTEALIDFEG-ALVVVSHD 486
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
33-83 |
3.72e-09 |
|
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: 56.73 E-value: 3.72e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDL 83
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR 401
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-203 |
5.67e-09 |
|
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: 56.46 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRA--VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTwrkaf 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEhrllpwLTVFE-NIHLALEETPLTREERNLRVNEHieiVGLKGFEKAYPHEL-----------SGGMAQRVAIA 153
Cdd:TIGR01271 1295 GVIPQK------VFIFSgTFRKNLDPYEQWSDEEIWKVAEE---VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 154 RGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHekITMILVTHDIE 203
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVE 1413
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-167 |
1.03e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtQIKGTdlkRGLIFQEHRLLPWLTVFENIHLALE 109
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGS---AALIAISSGLNGQLTGIENIELKGL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 110 ETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-215 |
1.17e-08 |
|
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: 55.40 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGL------DQDYDGEILLnqTQIKGTDLKRGLIFQEHRLLPWLTVFEN 103
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDttvtsgDATVAGKSIL--TNISDVHQNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAE 183
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190
....*....|....*....|....*....|..
gi 375134789 184 LQRIWQHEKiTMILVTHDIEEAVYLGDRVIVM 215
Cdd:TIGR01257 2113 IVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-200 |
1.20e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 6 MSFSLLSIKKLNKSFqrdqNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGlDQDYD---GEILLNQTQIkgTD 82
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAYKileGDILFKGESI--LD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 L------KRG--LIFQEHRLLPWLTVFENIHLALEEtplTREERNLR----------VNEHIEIVGLKG-FEKAYPHE-L 142
Cdd:CHL00131 76 LepeeraHLGifLAFQYPIEIPGVSNADFLRLAYNS---KRKFQGLPeldplefleiINEKLKLVGMDPsFLSRNVNEgF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 143 SGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTH 200
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-225 |
1.29e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 102 ENIHLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQ 181
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 375134789 182 AELQRIWQhEKITMILVTHDIEEAVYLGDRVIVMS----ARPGKIKEI 225
Cdd:NF000106 185 DEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDrgrvIADGKVDEL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
39-215 |
1.36e-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: 52.38 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 39 QGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtqIKGTDLKRGLIFQEHRLLpwltvfenihlaleetpltreer 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLII----------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 119 nlrvnehieivglkgfEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAE-----LQRIWQHEKI 193
Cdd:smart00382 54 ----------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNL 117
|
170 180
....*....|....*....|....*..
gi 375134789 194 TMILVTHDIE-----EAVYLGDRVIVM 215
Cdd:smart00382 118 TVILTTNDEKdlgpaLLRRRFDRRIVL 144
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-206 |
1.77e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 23 DQNTLTvLDgiNLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEiLLNQtqikgtdlkrgliFQEhrllPWLTVFE 102
Cdd:PRK10938 15 DTKTLQ-LP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQ-------------FSH----ITRLSFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 103 NIHLALEET-----------------PLTRE------ERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNK 159
Cdd:PRK10938 74 QLQKLVSDEwqrnntdmlspgeddtgRTTAEiiqdevKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 160 PDILLLDEPFGALDAITRSHLQAELQRIwQHEKITMILVT---HDIEEAV 206
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLVLnrfDEIPDFV 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-222 |
1.89e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIK----GTDLKRGLIF-QEHR----LLPWLTVFEN 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRDAIRAGIMLcPEDRkaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLALEETPLT--------REERNLRvnEHIEIVGLKGfekayPH------ELSGGMAQRVAIARGLVNKPDILLLDEPF 169
Cdd:PRK11288 352 INISARRHHLRagclinnrWEAENAD--RFIRSLNIKT-----PSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 170 GALDAITRS---HLQAELQRiwqhEKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:PRK11288 425 RGIDVGAKHeiyNVIYELAA----QGVAVLFVSSDLPEVLGVADRIVVM--REGRI 474
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-203 |
2.84e-08 |
|
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: 53.32 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFQRDQNTltVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLdQDYDGEILLNQTQIKGTDLKR----- 85
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKwrkaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 86 GLIFQEhrllpwLTVFE-NIHLALEETPLTREERNLRVNEHieiVGLKGFEKAYPHEL-----------SGGMAQRVAIA 153
Cdd:cd03289 80 GVIPQK------VFIFSgTFRKNLDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 375134789 154 RGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQheKITMILVTHDIE 203
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIE 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-215 |
3.25e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLrliagldqdydgEILLNQTQIKgtdlkRGLIFQEHRLL-----PWL---TV 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEIS-----EGRVWAERSIAyvpqqAWImnaTV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPlTREERNLRVNE------------HIEIvGLKGFEkaypheLSGGMAQRVAIARGLVNKPDILLLDEP 168
Cdd:PTZ00243 738 RGNILFFDEEDA-ARLADAVRVSQleadlaqlggglETEI-GEKGVN------LSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 375134789 169 FGALDAITRSHLQAELQRIWQHEKiTMILVTHDIeEAVYLGDRVIVM 215
Cdd:PTZ00243 810 LSALDAHVGERVVEECFLGALAGK-TRVLATHQV-HVVPRADYVVAL 854
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-224 |
6.02e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG---TDLKRGL-IFQEHRLLPWLTVFENI 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfglTDLRRVLsIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 hlaleeTPLTrEERNLRVNEHIEIVGLKGFEKAYPHEL-----------SGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:PLN03232 1331 ------DPFS-EHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 375134789 174 AITRSHLQAELQRiwQHEKITMILVTHDIEEAVYLgDRVIVMSArpGKIKE 224
Cdd:PLN03232 1404 VRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDC-DKILVLSS--GQVLE 1449
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-205 |
1.01e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGlD--QDYDGEILLNQTQiKGT-----DLKRGL------IFQE 91
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpQGYSNDLTLFGRR-RGSgetiwDIKKHIgyvsssLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 92 HRL-LPWLTV-----FENIHLALEetplTREERNLRVNEHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGLVNKPDILL 164
Cdd:PRK10938 349 YRVsTSVRNVilsgfFDSIGIYQA----VSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 375134789 165 LDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEA 205
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-217 |
1.25e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSfqRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG-LDQ---------DYDGeilLNQTQIKgtD 82
Cdd:TIGR00956 62 FRKLKKF--RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhigvegviTYDG---ITPEEIK--K 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 83 LKRG-LIF--QEHRLLPWLTVFENIHLALE-ETP------LTREERNLRVNEHI-EIVGLK-------GFEkaYPHELSG 144
Cdd:TIGR00956 135 HYRGdVVYnaETDVHFPHLTVGETLDFAARcKTPqnrpdgVSREEYAKHIADVYmATYGLShtrntkvGND--FVRGVSG 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375134789 145 GMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKITMILVTHDIEEAVY-LGDRVIVMSA 217
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYE 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-223 |
1.42e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQD-YDGEILLNQTQIK---------------GTDLKRglifqeH 92
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGrWEGEIFIDGKPVKirnpqqaiaqgiamvPEDRKR------D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 93 RLLPWLTVFENIHLALeetpLTREERNLRVNEHIEIVGLKGFEK------AYPH----ELSGGMAQRVAIARGLVNKPDI 162
Cdd:PRK13549 351 GIVPVMGVGKNITLAA----LDRFTGGSRIDDAAELKTILESIQrlkvktASPElaiaRLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375134789 163 LLLDEP-----FGALDAITRshLQAELQRiwqhEKITMILVTHDIEEAVYLGDRVIVMSArpGKIK 223
Cdd:PRK13549 427 LILDEPtrgidVGAKYEIYK--LINQLVQ----QGVAIIVISSELPEVLGLSDRVLVMHE--GKLK 484
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-204 |
2.77e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 25 NTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNqTQIKGTDLKRGLIFQehrllpwLTVFENI 104
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN-GEVSVIAISAGLSGQ-------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 105 HLALEETPLTREERNLRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEpfgALDAITRSHLQAEL 184
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCL 183
|
170 180
....*....|....*....|..
gi 375134789 185 QRIWQ--HEKITMILVTHDIEE 204
Cdd:PRK13546 184 DKIYEfkEQNKTIFFVSHNLGQ 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-176 |
2.89e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 14 KKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG-LDQDY--DGEILLNQTQIKGTDLKR-GLIF 89
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTGVitGGDRLVNGRPLDSSFQRSiGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEHRLLPWLTVFENIHL-ALEETP--LTREERNLRVNEHIEIVGLKGFEKAY---PHE-LSGGMAQRVAIARGLVNKPDI 162
Cdd:TIGR00956 843 QQDLHLPTSTVRESLRFsAYLRQPksVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKL 922
|
170
....*....|....*
gi 375134789 163 LL-LDEPFGALDAIT 176
Cdd:TIGR00956 923 LLfLDEPTSGLDSQT 937
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
45-167 |
3.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 45 IVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDlKRGLIFQEHRLLPWL--TVFENIHLALE-----ETpltree 117
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIGHNLGLKLemTVFENLKFWSEiynsaET------ 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 118 rnlrVNEHIEIVGLKGF--EKAYphELSGGMAQRVAIARGLVNKPDILLLDE 167
Cdd:PRK13541 104 ----LYAAIHYFKLHDLldEKCY--SLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-216 |
3.70e-07 |
|
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: 49.91 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 13 IKKLNKSFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILlnqtqIKGTDLKRglifqeh 92
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV-----IDGIDISK------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 93 rlLPWLTVFENIHLALEETPL-----------TREERNLRVNEHIEIVGLKGFEKAYPHEL-----------SGGMAQRV 150
Cdd:cd03288 88 --LPLHTLRSRLSIILQDPILfsgsirfnldpECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 375134789 151 AIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEK-ITMILVTHDIEEAvylgDRVIVMS 216
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTvVTIAHRVSTILDA----DLVLVLS 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-201 |
5.25e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 17 NKSFQRDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLnqtqikGTDLKRGLiFQEHR--L 94
Cdd:PRK11147 324 NVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKLEVAY-FDQHRaeL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 95 LPWLTVFENIHLALEETPLTREERNlrvnehieIVG-LKGF----------EKAypheLSGGMAQRVAIARGLVNKPDIL 163
Cdd:PRK11147 395 DPEKTVMDNLAEGKQEVMVNGRPRH--------VLGyLQDFlfhpkramtpVKA----LSGGERNRLLLARLFLKPSNLL 462
|
170 180 190
....*....|....*....|....*....|....*...
gi 375134789 164 LLDEPFGALDAITRSHLQaELQRIWQHekiTMILVTHD 201
Cdd:PRK11147 463 ILDEPTNDLDVETLELLE-ELLDSYQG---TVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-173 |
6.00e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 14 KKLNKSFqrDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQT-QIKGTDLKRGlifqeh 92
Cdd:PRK11819 328 ENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKLAYVDQSRD------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 93 RLLPWLTVFENIHLALEETPLTREERNLRVneHIEIVGLKGFEKAYP-HELSGGMAQRVAIARGLVNKPDILLLDEPFGA 171
Cdd:PRK11819 398 ALDPNKTVWEEISGGLDIIKVGNREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQGGNVLLLDEPTND 475
|
..
gi 375134789 172 LD 173
Cdd:PRK11819 476 LD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-222 |
1.11e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 11 LSIKKLNKSFqrDQNTLtvLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAgldqdydGEILLNQTQIKGTDLKR-GLIF 89
Cdd:PRK15064 320 LEVENLTKGF--DNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKWSENANiGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 90 QEH--------RLLPWLTVFenihlaleetplTREERNLRVnehieIVGLKG---FE----KAYPHELSGGMAQRVAIAR 154
Cdd:PRK15064 389 QDHaydfendlTLFDWMSQW------------RQEGDDEQA-----VRGTLGrllFSqddiKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 155 GLVNKPDILLLDEPFGALDAITRSHLQAELQRIwqheKITMILVTHDIEEAVYLGDRVIVMsaRPGKI 222
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALEKY----EGTLIFVSHDREFVSSLATRIIEI--TPDGV 513
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-200 |
3.38e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 10 LLSIKKLNKSFQRDqntlTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDqDYdgEILLNQTQIKGTDL------ 83
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-DY--EVTGGTVEFKGKDLlelspe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 84 KRG-----LIFQEHRLLPWL-------TVFENIHLALEETPLTREERNLRVNEHIEIVGLKG--FEKAYPHELSGGMAQR 149
Cdd:PRK09580 74 DRAgegifMAFQYPVEIPGVsnqfflqTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 375134789 150 VAIARGLVNKPDILLLDEPFGALDaITRSHLQAELQRIWQHEKITMILVTH 200
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-220 |
4.42e-06 |
|
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: 47.47 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 38 EQGEFISIVGSSGCGKSTLLRLIAGLDQ----DYDG-----EILlnqTQIKGTDLK---RGLIFQEHR---------LLP 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKpnlgDYDEepswdEVL---KRFRGTELQdyfKKLANGEIKvahkpqyvdLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 97 WL---TVFEnihlALEETpltrEERNlRVNEHIEIVGLKGFEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALD 173
Cdd:COG1245 174 KVfkgTVRE----LLEKV----DERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 375134789 174 A---ITRSHLQAELQRiwqhEKITMILVTHDIeeAV--YLGDRVIVMSARPG 220
Cdd:COG1245 245 IyqrLNVARLIRELAE----EGKYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-231 |
5.62e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 142 LSGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKiTMILVTHDIEEAVYLGDRVIVMSArpGK 221
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSN--GL 468
|
90
....*....|
gi 375134789 222 IKEIIQVPLT 231
Cdd:PRK10982 469 VAGIVDTKTT 478
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
149-201 |
5.90e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 5.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 375134789 149 RVAIARGLVNKPDILLLDEPFGALDAITRSHLQAEL-QRiwqheKITMILVTHD 201
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLnER-----NSTMIIISHD 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-174 |
6.68e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 24 QNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQD--YDGEILLNQTQIKGTDLKR--GLIFQEHRLLPWLT 99
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFARisGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 100 VFEN-IHLALEETP--LTREERNLRVNEHIE----------IVGLKGFEKaypheLSGGMAQRVAIARGLVNKPDILLLD 166
Cdd:PLN03140 970 VRESlIYSAFLRLPkeVSKEEKMMFVDEVMElveldnlkdaIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMD 1044
|
....*...
gi 375134789 167 EPFGALDA 174
Cdd:PLN03140 1045 EPTSGLDA 1052
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-221 |
8.86e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKGTDLKRGL------IFQEHRLLPWLTVFEN 103
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 104 IHLA--------LEETPLTREERNLRVNEHIEIVglkgfEKAYPHELSGGMAQRVAIARGLVNKPDILLLDEPFGALDAI 175
Cdd:PRK10982 94 MWLGryptkgmfVDQDKMYRDTKAIFDELDIDID-----PRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 375134789 176 TRSHLQAELQRIwQHEKITMILVTHDIEEAVYLGDRVIVMsaRPGK 221
Cdd:PRK10982 169 EVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL--RDGQ 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
30-221 |
1.16e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.62 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 30 LDGINLNIEQGEFISIVGSSGCGKSTLLRliAGLDQDydGEILLNQTQIKGTDLKRGLIFQEHRLlpwltvfenIHLALE 109
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS--GKARLISFLPKFSRNKLIFIDQLQFL---------IDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 110 ETPLTREERNLrvnehieivglkgfekayphelSGGMAQRVAIAR--GLVNKPDILLLDEPFGALDAITRSHLQAELQRI 187
Cdd:cd03238 78 YLTLGQKLSTL----------------------SGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170 180 190
....*....|....*....|....*....|....
gi 375134789 188 WQhEKITMILVTHDiEEAVYLGDRVIVMSARPGK 221
Cdd:cd03238 136 ID-LGNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
141-220 |
1.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 141 ELSGGMAQRVAIARGLVNKPDILLLDEPFGALDA---ITRSHLQAELQriwqhEKITMILVTHDIeeAV--YLGDRVIVM 215
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrLNVARLIRELA-----EGKYVLVVEHDL--AVldYLADNVHIA 284
|
....*
gi 375134789 216 SARPG 220
Cdd:PRK13409 285 YGEPG 289
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
33-200 |
1.82e-04 |
|
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: 42.43 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 33 INLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEIllnqtqikgTDLKRGLIF---QEhrllPWLTV--FENiHLA 107
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL---------TKPAKGKLFyvpQR----PYMTLgtLRD-QII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 108 LEETPLTREERNLRVNEHIEI---VGLK-------GFE--KAYPHELSGGMAQRVAIARGLVNKPDILLLDEpfgALDAI 175
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDKDLEQIldnVQLThileregGWSavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE---CTSAV 613
|
170 180
....*....|....*....|....*...
gi 375134789 176 TrshLQAElQRIWQHEK---ITMILVTH 200
Cdd:TIGR00954 614 S---VDVE-GYMYRLCRefgITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-200 |
2.57e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 375134789 143 SGGMAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRiWQHekiTMILVTH 200
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPK---TFIVVSH 399
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-215 |
2.83e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTQIKG---TDLKR--GLIFQEhrllPWL---TV 100
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyglRELRRqfSMIPQD----PVLfdgTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 101 FENIHLALEETPltrEErnlrVNEHIEIVGLKGfEKAYPHE------LSGG----MAQR--VAIARGLVNK-PDILLLDE 167
Cdd:PTZ00243 1401 RQNVDPFLEASS---AE----VWAALELVGLRE-RVASESEgidsrvLEGGsnysVGQRqlMCMARALLKKgSGFILMDE 1472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 375134789 168 PFGALDAITRSHLQAELQRIWQheKITMILVTHDIEE-AVYlgDRVIVM 215
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTvAQY--DKIIVM 1517
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-168 |
9.39e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 29 VLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAG--LDQDYDGEILLNQTQIKGTDLKR----------------GLIFQ 90
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVSTVSDaidaglayvtedrkgyGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 91 EhrllpwlTVFENIHLAleetPLTREERNLRVNEHIEIVGLKGFEKAY----PH------ELSGGMAQRVAIARGLVNKP 160
Cdd:NF040905 355 D-------DIKRNITLA----NLGKVSRRGVIDENEEIKVAEEYRKKMniktPSvfqkvgNLSGGNQQKVVLSKWLFTDP 423
|
....*...
gi 375134789 161 DILLLDEP 168
Cdd:NF040905 424 DVLILDEP 431
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
37-127 |
9.91e-04 |
|
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: 39.39 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 37 IEQGE-FISIVGSSGCGKSTLLR-LIAGLDQDYDGeILLNQTQIKGTDLKRGLIFQehrllpwltvfenihLALEETPLT 114
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRrLLERLPDDVKV-AYIPNPQLSPAELLRAIADE---------------LGLEPKGAS 102
|
90
....*....|...
gi 375134789 115 REERNLRVNEHIE 127
Cdd:COG3267 103 KADLLRQLQEFLL 115
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
142-213 |
1.47e-03 |
|
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: 38.74 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375134789 142 LSGG------MAQRVAIARGLVNKPDILLLDEPFGALDAITRSHLQAELQRIWQHEKI-TMILVTHDiEEAVYLGDRVI 213
Cdd:cd03240 116 CSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNfQLIVITHD-EELVDAADHIY 193
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-201 |
2.70e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 19 SFQRDQNTLTVLDGINLNIEQGEFISIVGSSGCGKSTLLRLIAGLDQDYDGEILLNQTqikgtdlkrglifqehrllpWL 98
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN--------------------WQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375134789 99 TVFENihlalEETPL------------TREERNLR-----VNEH-----IEIV---------------------GLkGFE 135
Cdd:PRK10636 66 LAWVN-----QETPAlpqpaleyvidgDREYRQLEaqlhdANERndghaIATIhgkldaidawtirsraasllhGL-GFS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 375134789 136 KAYPHE----LSGGMAQRVAIARGLVNKPDILLLDEPFGALDaitrshLQAE--LQRIWQHEKITMILVTHD 201
Cdd:PRK10636 140 NEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------LDAViwLEKWLKSYQGTLILISHD 205
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
45-94 |
7.92e-03 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 37.28 E-value: 7.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 375134789 45 IVGSSGCGKSTLLRLIA-GLDQDYDGEillnQTQIKGTDLKRGL---IFQEHRL 94
Cdd:TIGR03925 368 IFGDSESGKTTLLRTIArGIVRRYSPD----QARLVVVDYRRTLlgaVPEDYLA 417
|
|
| |
