|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
8.86e-113 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 323.15 E-value: 8.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSL 80
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-222 |
4.94e-101 |
|
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: 293.24 E-value: 4.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-229 |
2.23e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 230.71 E-value: 2.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKdLKATILMVTHD-AFTASYARRILFINDGKIFIELVRG 229
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDlELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-222 |
5.99e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 213.40 E-value: 5.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfr 84
Cdd:COG3839 4 LELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 165 LVLADEPTGSLDSK---SARLLLERfesLNKDLKATILMVTHD---AFTasYARRILFINDGKI 222
Cdd:COG3839 154 VFLLDEPLSNLDAKlrvEMRAEIKR---LHRRLGTTTIYVTHDqveAMT--LADRIAVMNDGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-222 |
8.94e-68 |
|
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: 208.53 E-value: 8.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDnvtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkfR 84
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-203 |
2.43e-66 |
|
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: 205.51 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH 203
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-204 |
3.82e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 203.39 E-value: 3.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKiqaVAKYLDIeqV-LS----KYPYQISGGQKQRVASARA 158
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKR---VAELLEL--VgLSdkadAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
9.41e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 202.64 E-value: 9.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksl 80
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:COG3842 75 ---EKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 161 TDPSLVLADEPTGSLDsksARLLLE-RFE--SLNKDLKATILMVTHD---AFTasYARRILFINDGKI 222
Cdd:COG3842 152 PEPRVLLLDEPLSALD---AKLREEmREElrRLQRELGITFIYVTHDqeeALA--LADRIAVMNDGRI 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-204 |
1.14e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 199.55 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksl 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfrknELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDgkiQAVAKYLDI---EQVLSKYPYQISGGQKQRVASAR 157
Cdd:COG1116 81 ------DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERR---ERARELLELvglAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-222 |
4.56e-63 |
|
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: 196.32 E-value: 4.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDkfr 84
Cdd:cd03301 1 VELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03301 74 ---IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
18-221 |
1.24e-62 |
|
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: 195.54 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTK-------AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKnELGF 90
Cdd:TIGR02673 5 HNVSKaypggvaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:TIGR02673 84 VFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 171 PTGSLDSKSARLLLERFESLNKdLKATILMVTHD-AFTASYARRILFINDGK 221
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDlSLVDRVAHRVIILDDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-222 |
3.79e-62 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 194.65 E-value: 3.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkSKSLDKF 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQD-FNLLD-TLTAYENIALALTIKGEASSKidgKIQAVAKYLDIEQV------LSKYPYQISGGQKQRVAS 155
Cdd:cd03257 80 RRKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKK---EARKEAVLLLLVGVglpeevLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-222 |
2.34e-61 |
|
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: 192.65 E-value: 2.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLD 81
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSkidgkiQAVAKYLdIEQV-----LSKYPYQISGGQKQRVASA 156
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA------RARARAL-LERVglghrLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 157 RAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-217 |
5.18e-61 |
|
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: 190.90 E-value: 5.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKN 86
Cdd:TIGR03608 1 LKNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 ELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLV 166
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 167 LADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDAFTASYARRILFI 217
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
5.56e-61 |
|
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: 191.53 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksksldkfR 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASY-ARRIL 215
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVV 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-222 |
6.11e-61 |
|
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: 199.74 E-value: 6.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYG-NKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDK 82
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKnELGFVFQD-FNLLD-TLTAYENIALALTIKGEASSKidGKIQAVAKYLDI----EQVLSKYPYQISGGQKQRVASA 156
Cdd:COG1123 340 LRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLLSRA--ERRERVAELLERvglpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 157 RAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
3.47e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 190.27 E-value: 3.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKnELGFVFQDFNLLDTLTAYENIALAL-----TIKGEAS--SKIDgkIQAVAKYLdiEQV-LSKYPYQ----ISGGQKQ 151
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTNVLAGRlgrtsTWRSLLGlfPPED--RERALEAL--ERVgLADKAYQradqLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIF 223
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-222 |
1.09e-58 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 185.30 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 8 EKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNe 87
Cdd:cd03292 4 INVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 88 LGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKdLKATILMVTHDA-FTASYARRILFINDGKI 222
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-222 |
1.47e-58 |
|
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: 189.48 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsl 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfrKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:TIGR03265 75 ----KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-223 |
2.95e-58 |
|
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: 184.48 E-value: 2.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIF 223
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-222 |
4.14e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.81 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrLKSKSLDKF 83
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKnELGFVFQDFNLLDTLTAYENIALAL-TIKGEasSKIDGKIQAVAkYLD---IEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:COG1126 76 RR-KVGMVFQQFNLFPHLTVLENVTLAPiKVKKM--SKAEAEERAME-LLErvgLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARlllerfESLN--KDLKA---TILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVG------EVLDvmRDLAKegmTMVVVTHEmGFAREVADRVVFMDGGRI 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-223 |
1.58e-57 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 182.53 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSK-IDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALELQPNLSYQeARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 163 PSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIF 223
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
2.36e-57 |
|
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: 182.87 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSL 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKnELGFVFQDFNLLDTLTAYENIALALTIKG-----EASSKIDGKIQAVakylDIEQVLSKYPYQISGGQKQRVAS 155
Cdd:COG1127 78 YELRR-RIGMLFQGGALFDSLTVFENVAFPLREHTdlseaEIRELVLEKLELV----GLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-222 |
5.74e-56 |
|
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: 179.07 E-value: 5.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKFRKnELGFVFQD-----F 95
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRR-KVGLVFQNpddqlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLldtlTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:COG1122 90 AP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 176 DSKSARLLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGK-TVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-221 |
6.60e-56 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 176.99 E-value: 6.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR 84
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KneLGFVFQDFNLLDTLTAYENIALALtikgeasskidgkiqavakyldieqvlskypyqiSGGQKQRVASARAIVTDPS 164
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGK 221
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-222 |
8.90e-55 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 175.41 E-value: 8.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrLKSKSLDKFR 84
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnELGFVFQDFNLLDTLTAYENIALAL-TIKGEAsskidgKIQAVAKYLDI-EQV-----LSKYPYQISGGQKQRVASAR 157
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLAPiKVKGMS------KAEAEERALELlEKVgladkADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-222 |
2.36e-54 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 174.73 E-value: 2.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfr 84
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-223 |
2.49e-54 |
|
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: 175.06 E-value: 2.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR 84
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnELGFVFQDFNLLDTLTAYENIALAL-----TIKGEAS--SKIDgkIQAVAKYLdiEQV-LSKYPYQ----ISGGQKQR 152
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGlfPKEE--KQRALAAL--ERVgLLDKAYQradqLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA-FTASYARRILFINDGKIF 223
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-222 |
2.62e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 178.42 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI-TRLKSksldkf 83
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKiqaVAKYLDIEQvLS----KYPYQISGGQKQRVASARAI 159
Cdd:COG1118 73 RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRAR---VEELLELVQ-LEgladRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 160 VTDPSLVLADEPTGSLDSKsARLLLER--FESLnKDLKATILMVTHD---AFTasYARRILFINDGKI 222
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAK-VRKELRRwlRRLH-DELGGTTVFVTHDqeeALE--LADRVVVMNQGRI 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-222 |
4.53e-54 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 174.22 E-value: 4.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkfRKN 86
Cdd:TIGR00968 3 IANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA------RDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 ELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLV 166
Cdd:TIGR00968 73 KIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 167 LADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAmEVADRIVVMSNGKI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-222 |
4.91e-54 |
|
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: 174.61 E-value: 4.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSldkFR 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---FR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQD--------FNLLDTLtayeniALALTIKGEAssKIDGKIQAVAKYLDI-EQVLSKYPYQISGGQKQRVAS 155
Cdd:COG1124 79 RR-VQMVFQDpyaslhprHTVDRIL------AEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASY-ARRILFINDGKI 222
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-225 |
1.44e-53 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 173.07 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR 84
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQDFNLLDTLTAYENIALALTIKGEAS-SKIDG----KIQAVAkyldIEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREHTRLSeEEIREivleKLEAVG----LRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIFIE 225
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAE 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-222 |
2.39e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 2.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfr 84
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG1131 75 ---IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAeRLCDRVAIIDKGRI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-221 |
4.26e-52 |
|
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: 168.41 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIEKYYGNKDnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkSKSLDKFRK 85
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT---KLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 NeLGFVFQDFNL-LDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03225 76 K-VGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGK 221
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
4.72e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 176.63 E-value: 4.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS-TIDH--VTTGKIIINNSDITRLKs 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgLLPHggRISGEVLLDGRDLLELS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 78 kslDKFRKNELGFVFQDF-NLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASA 156
Cdd:COG1123 78 ---EALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 157 RAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-222 |
1.01e-51 |
|
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: 168.29 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkfRKN 86
Cdd:cd03296 5 VRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV------QER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 ELGFVFQDFNLLDTLTAYENIALALTIKGEAS----SKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 163 PSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-203 |
1.03e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.52 E-value: 1.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 8 EKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNe 87
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 88 LGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH 203
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-222 |
9.04e-51 |
|
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: 165.94 E-value: 9.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFR 84
Cdd:cd03295 1 IEFENVTKRYGG---GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKY--LDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 163 PSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEI 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-223 |
1.11e-50 |
|
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: 165.93 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNeLGFVFQDFNLLDTLTAYENI---ALAL--TIKGeASSKIDGKIQAVAKYLdIEQV-LSKYPY----QISGGQKQRV 153
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVlhgRLGYkpTWRS-LLGRFSEEDKERALSA-LERVgLADKAYqradQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIF 223
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-204 |
8.79e-50 |
|
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: 166.00 E-value: 8.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTI---DHVTTGKIIINNSDITRLKSKSL 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNELGFVFQD-FNLLD-TLTAYENIALALTIKGEASSKidGKIQAVAKYLDI------EQVLSKYPYQISGGQKQR 152
Cdd:COG0444 81 RKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIHGGLSKA--EARERAIELLERvglpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLD-SKSA---RLLLErfesLNKDLKATILMVTHD 204
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDvTIQAqilNLLKD----LQRELGLAILFITHD 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-226 |
4.79e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 161.52 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKF 83
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIEL 226
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-222 |
3.72e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 157.17 E-value: 3.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSldkfr 84
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALaltikgeasskidgkiqavakyldieqvlskypyqiSGGQKQRVASARAIVTDPS 164
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-222 |
3.90e-48 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 159.04 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDnvtkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfr 84
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDaFT--ASYARRILFINDGKI 222
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD-FEeaWALADKVAIMLNGKL 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-222 |
1.05e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 161.40 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkfRKN 86
Cdd:PRK10851 5 IANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 ELGFVFQDFNLLDTLTAYENIALALTI----KGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 163 PSLVLADEPTGSLDSKsARLLLERF-ESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:PRK10851 155 PQILLLDEPFGALDAQ-VRKELRRWlRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-222 |
1.94e-47 |
|
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: 158.19 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 16 NKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQDF 95
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 176 DSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-225 |
2.00e-47 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 156.86 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDK 82
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 163 PSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-222 |
2.91e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 154.63 E-value: 2.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfR 84
Cdd:COG4555 2 IEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAFT-ASYARRILFINDGKI 222
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEvEALCDRVVILHKGKV 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-222 |
5.67e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 153.37 E-value: 5.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKfR 84
Cdd:COG3840 2 LRLDDLTYRYGDF------PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL---PPAE-R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG3840 72 P--VSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH---DAftASYARRILFINDGKI 222
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHdpeDA--ARIADRVLLVADGRI 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-222 |
8.80e-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: 8.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFR 84
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnELGFVFQDFNLLDTlTAYENIALALTIKGEASSkiDGKIQAVAKYLDI-EQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:COG4619 74 R-QVAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-172 |
1.25e-45 |
|
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: 149.72 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrknELGFVFQDFNLLDTLTA 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 104 YENIALALTIKGEASSKIDGKIQAVAKYLDIE----QVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-223 |
1.40e-45 |
|
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: 152.89 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKf 83
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rknELGFVFQDFNLLDTLTAYENIALA----LTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:COG1120 76 ---RIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD---AftASYARRILFINDGKIF 223
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlnlA--ARYADRLVLLKDGRIV 217
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
24-222 |
3.79e-45 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 154.46 E-value: 3.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVFQDFNLLDTLTA 103
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE------KRGIAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLL 183
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 184 LERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGRL 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-222 |
2.78e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 152.69 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDkfr 84
Cdd:PRK11650 4 LKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:PRK11650 78 ---IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 165 LVLADEPTGSLDSK---SARLLLERfesLNKDLKATILMVTHD---AFTasYARRILFINDGKI 222
Cdd:PRK11650 155 VFLFDEPLSNLDAKlrvQMRLEIQR---LHRRLKTTSLYVTHDqveAMT--LADRVVVMNGGVA 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-222 |
3.73e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.01 E-value: 3.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 8 EKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLL---NCIstIDHvTTGKIIINNSDITRLKsksLDKFR 84
Cdd:COG1125 5 ENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLrmiNRL--IEP-TSGRILIDGEDIRDLD---PVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKI----QAVAkyLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:COG1125 76 RR-IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVdellELVG--LDPEEYRDRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD---AFTasYARRILFINDGKI 222
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDideALK--LGDRIAVMREGRI 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-222 |
4.41e-44 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 148.10 E-value: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 8 EKIEK-YYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdKFRKN 86
Cdd:PRK10908 5 EHVSKaYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREV-PFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 ELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVakyLDIEQVLSK---YPYQISGGQKQRVASARAIVTDP 163
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA---LDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKdLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDiGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-222 |
5.27e-44 |
|
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: 147.83 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEgEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsDITRLKS-KSLD-KFRKNELGFVFQDFNLLDTLTA 103
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN--GTVLFDSrKKINlPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALTIKGEASSKIdgKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLL 183
Cdd:cd03297 93 RENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 184 LERFESLNKDLKATILMVTHDAFTASY-ARRILFINDGKI 222
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-222 |
1.42e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.94 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVT-------KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGF 90
Cdd:COG1132 343 ENVSfsypgdrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQ-IGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQDFNLLDTlTAYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAI 159
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYG---RPDAT---DEEVEEAAKAAQAHEFIEALPdgYDtvvgergvnLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
1.46e-43 |
|
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: 146.94 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS-TIDHV----TTGKIIINNSDITRLKSKS 79
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIpgapDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKneLGFVFQDFNLLDtLTAYENIALALTIKGEASSKIDGKIqavakyldIEQVLSK-----------YPYQISGG 148
Cdd:cd03260 77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDER--------VEEALRKaalwdevkdrlHALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 149 QKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLkaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNmQQAARVADRTAFLLNGRL 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-222 |
1.91e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 147.16 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 9 KIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItrLKSKSLDKFRKNEL 88
Cdd:PRK09493 6 NVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 89 GFVFQDFNLLDTLTAYENIALAlTIKGEASSKIDGKIQA---VAKyLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSL 165
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFG-PLRVRGASKEEAEKQArelLAK-VGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEiGFAEKVASRLIFIDKGRI 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-240 |
7.24e-43 |
|
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: 146.83 E-value: 7.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNeLGFVFQdF--NLL 98
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKK-VGLVFQ-FpeHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 DTLTAYENIALALTIKGEASSKIDgkiQAVAKYLDI----EQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGS 174
Cdd:TIGR04521 96 FEETVYKDIAFGPKNLGLSEEEAE---ERVKEALELvgldEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 175 LDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKIFIElvrgnDSRKEFFTKI 240
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD-----GTPREVFSDV 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-225 |
7.25e-43 |
|
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: 145.95 E-value: 7.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksl 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkFRKNELGFV--FQDFNLLDTLTAYENIALALTIKGEAS---------------SKIDGKIQAVAKYLDIEQVLSKYPY 143
Cdd:COG0411 74 --HRIARLGIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 144 QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
...
gi 447167138 223 FIE 225
Cdd:COG0411 232 IAE 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-225 |
1.14e-42 |
|
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: 144.89 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkFR 84
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-----HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFV--FQDFNLLDTLTAYENIALALTIKG----------EASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQR 152
Cdd:cd03219 72 IARLGIGrtFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKIFIE 225
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-221 |
1.93e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 142.14 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfR 84
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQDFNLLDTlTAYENIalaltikgeasskidgkiqavakyldieqvlskypyqISGGQKQRVASARAIVTDPS 164
Cdd:cd03228 76 KN-IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGK 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
1.93e-42 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 152.57 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSL 80
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-222 |
3.92e-42 |
|
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: 152.30 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFRKNeLGFVFQDFNL 97
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRRQ-IGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 L-DTLtaYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTDPSL 165
Cdd:COG2274 561 FsGTI--RENITLG---DPDAT---DEEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-222 |
5.01e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 147.02 E-value: 5.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkf 83
Cdd:PRK09452 14 LVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD---AFTASyaRRILFINDGKI 222
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeeALTMS--DRIVVMRDGRI 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-221 |
1.67e-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: 136.99 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrK 85
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 NELGFVFQdfnlldtltayenialaltikgeasskidgkiqavakyldieqvlskypyqISGGQKQRVASARAIVTDPSL 165
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDA-FTASYARRILFINDGK 221
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-223 |
1.89e-40 |
|
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: 137.57 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrk 85
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 nELGFVFQdfnlldtltayeniALALTikgeasskidgkiqavakylDIEQVLSKYPYQISGGQKQRVASARAIVTDPSL 165
Cdd:cd03214 74 -KIAYVPQ--------------ALELL--------------------GLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKIF 223
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRIV 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-204 |
7.30e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.46 E-value: 7.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkSKSLDKfr 84
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT---GPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 knelGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447167138 165 LVLADEPTGSLDSksarLLLERFESLNKDLKA----TILMVTHD 204
Cdd:COG4525 155 FLLMDEPFGALDA----LTREQMQELLLDVWQrtgkGVFLITHS 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-222 |
1.34e-39 |
|
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: 136.48 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlkskSLDKFR 84
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03263 75 QS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKdlKATILMVTHDAFTASY-ARRILFINDGKI 222
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-222 |
1.35e-39 |
|
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: 143.75 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGFVFQD---FNllD 99
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQ-IAWVPQNpylFA--G 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLtaYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP-----------YQISGGQKQRVASARAIVTDPSLVLA 168
Cdd:COG4988 426 TI--RENLRLG---RPDAS---DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447167138 169 DEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRI 549
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-222 |
1.46e-39 |
|
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: 139.55 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 39 IMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVFQDFNLLDTLTAYENIALALTIKGEAS 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 119 SKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATI 198
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 447167138 199 LMVTHDAFTA-SYARRILFINDGKI 222
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKI 179
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
2.13e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksksl 80
Cdd:COG1121 3 MMPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfRKNELGFVFQDFNLLDT--LTAYENIALALTIK----GEASSKIDGKIQAVAKYLDIEQVLSKypyQI---SGGQKQ 151
Cdd:COG1121 73 ---ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADR---PIgelSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGKIF 223
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDlGAVREYFDRVLLLNRGLVA 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-214 |
3.70e-39 |
|
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: 134.91 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItrlkSKSLDKFR 84
Cdd:COG4133 3 LEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDgkIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG4133 75 R-RLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAFTASYARRI 214
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVL 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-204 |
7.07e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 137.56 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYY-------GNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLK 76
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 SKSLDKFRKnELGFVFQD-FNLLDT-LTAYENIALALTIKGEASSK-IDGKIQAVakyldIEQV------LSKYPYQISG 147
Cdd:COG4608 87 GRELRPLRR-RMQMVFQDpYASLNPrMTVGDIIAEPLRIHGLASKAeRRERVAEL-----LELVglrpehADRYPHEFSG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 148 GQKQRVASARAIVTDPSLVLADEPTGSLD-SKSARL--LLERfesLNKDLKATILMVTHD 204
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVlnLLED---LQDELGLTYLFISHD 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-222 |
9.96e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 135.26 E-value: 9.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYgNKDNVTKAIDnisFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKS----KSLDK 82
Cdd:PRK11264 6 VKNLVKKF-HGQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKNELGFVFQDFNLLDTLTAYENIalaltIKGEASSKIDGKIQAVAKyldIEQVLSK---------YPYQISGGQKQRV 153
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENI-----IEGPVIVKGEPKEEATAR---ARELLAKvglagketsYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmSFARDVADRAIFMDQGRI 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-225 |
1.12e-38 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 134.42 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlkskSLDKFRKN 86
Cdd:cd03265 3 VENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 eLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLV 166
Cdd:cd03265 75 -IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 167 LADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIFIE 225
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAE 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-220 |
1.68e-38 |
|
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: 134.13 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrknelgFVFQDFNLLDTLTA 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALTI------KGEASSKIDGKIQAVAkyldIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDS 177
Cdd:TIGR01184 72 RENIALAVDRvlpdlsKSERRAIVEEHIALVG----LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447167138 178 KSARLLLERFESLNKDLKATILMVTHDAFTASY-ARRILFINDG 220
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-222 |
5.45e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.40 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlKSKSLDKFRKnELGFVFQ--DFNLL 98
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRK-KVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 DTlTAYENIALALTIKGEASSKIDGKIQAVAKY--LDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK13637 98 EE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 177 SKSARLLLERFESLNKDLKATILMVTHDAF-TASYARRILFINDGKI 222
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKC 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-222 |
1.22e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.23 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKA------IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDkfrkneLGFVF 92
Cdd:PRK11432 11 NITKRfgsntvIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD------ICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 93 QDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 173 GSLDSKSARLLLERFESLNKDLKATILMVTHD---AFTASYArrILFINDGKI 222
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDqseAFAVSDT--VIVMNKGKI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
19-222 |
1.38e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.16 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAID------NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVF 92
Cdd:PRK11000 8 NVTKAYGdvviskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 93 QDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447167138 173 GSLDsksARLLLE-RFE--SLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:PRK11000 162 SNLD---AALRVQmRIEisRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-222 |
4.95e-37 |
|
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: 129.62 E-value: 4.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFvGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKskslDKFR 84
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP----QKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 165 LVLADEPTGSLDSKSaRLlleRFESLNKDLKA--TILMVTH---DafTASYARRILFINDGKI 222
Cdd:cd03264 151 ILIVDEPTAGLDPEE-RI---RFRNLLSELGEdrIVILSTHiveD--VESLCNQVAVLNKGKL 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
5.22e-37 |
|
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: 129.86 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkFR 84
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-----HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELG--FVFQDFNLLDTLTAYENIALALTIKGEASSKIdgkiqavakylDIEQVLSKYP----------YQISGGQKQR 152
Cdd:cd03224 72 RARAGigYVPEGRRIFPELTVEENLLLGAYARRRAKRKA-----------RLERVYELFPrlkerrkqlaGTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNkDLKATILMVTHDA-FTASYARRILFINDGKIFIE 225
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNArFALEIADRAYVLERGRVVLE 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-223 |
1.00e-36 |
|
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: 128.81 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 14 YGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinnsditRLKSKSLDKFRKnELGFVFQ 93
Cdd:cd03235 9 YGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI--------RVFGKPLEKERK-RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 94 DFNLLDT--LTAYENIALALTIKGEASSKIDG----KIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKadkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDAFTAS-YARRILFINDGKIF 223
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLeYFDRVLLLNRTVVA 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-222 |
1.22e-36 |
|
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: 132.53 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsdiTRLKSKSLDKFRKNE---LGFVFQDFNLLDTLT 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG---EVLQDSARGIFLPPHrrrIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSKIDgkIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARL 182
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 183 LLERFESLNKDLKATILMVTHDAFTASY-ARRILFINDGKI 222
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-222 |
2.16e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 129.32 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKDnvtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSK--SL 80
Cdd:PRK10619 4 NKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNEL-------GFVFQDFNLLDTLTAYENIALAlTIKGEASSKIDGKIQAVaKYLD----IEQVLSKYPYQISGGQ 149
Cdd:PRK10619 80 KVADKNQLrllrtrlTMVFQHFNLWSHMTVLENVMEA-PIQVLGLSKQEARERAV-KYLAkvgiDERAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEmGFARHVSSHVIFLHQGKI 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-222 |
5.80e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 128.38 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDnVTKAIdniSFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItRLK-------- 76
Cdd:COG4598 9 LEVRDLHKSFGDLE-VLKGV---SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 ---SKSLDKFRKNeLGFVFQDFNLLDTLTAYENIALA-LTIKGEAsskidgKIQAVAK---YLD---IEQVLSKYPYQIS 146
Cdd:COG4598 84 padRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEApVHVLGRP------KAEAIERaeaLLAkvgLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 147 GGQKQRVASARAIVTDPSLVLADEPTGSLDS-------KSARLLLE--RfeslnkdlkaTILMVTHD-AFTASYARRILF 216
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPelvgevlKVMRDLAEegR----------TMLVVTHEmGFARDVSSHVVF 226
|
....*.
gi 447167138 217 INDGKI 222
Cdd:COG4598 227 LHQGRI 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-203 |
1.15e-35 |
|
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: 125.74 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKD-NVTKAI-DNISFKVDEGEFVGIMGPSGSGKTTLLNCIS--TIDHVTTGKIIINNsditrlKSKSL 80
Cdd:cd03213 4 LSFRNLTVTVKSSPsKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING------RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKnELGFVFQDFNLLDTLTAYENIALALTIKGeasskidgkiqavakyldieqvlskypyqISGGQKQRVASARAIV 160
Cdd:cd03213 78 RSFRK-IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTH 203
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIH 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
23-222 |
2.25e-35 |
|
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: 132.58 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGFVFQDFNLLDTlT 102
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRR-IAVVPQRPHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:COG4987 425 LRENLRLA---RPDAT---DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 172 TGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG4987 499 TEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-222 |
2.80e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.56 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSldkf 83
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-222 |
2.97e-35 |
|
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: 125.30 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 31 VDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVFQDFNLLDTLTAYENIALA 110
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 111 LTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESL 190
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 447167138 191 NKDLKATILMVTH---DAftASYARRILFINDGKI 222
Cdd:cd03298 175 HAETKMTVLMVTHqpeDA--KRLAQRVVFLDNGRI 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-222 |
5.83e-35 |
|
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: 124.59 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 28 SFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVFQDFNLLDTLTAYENI 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 108 ALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERF 187
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 447167138 188 ESLNKDLKATILMVTH---DAftASYARRILFINDGKI 222
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHhlsDA--RAIASQIAVVSQGKI 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-225 |
6.11e-35 |
|
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: 126.01 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsDITRLKSKSLDKFRKNeLGFVFQ--Df 95
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLWEIRKK-VGMVFQnpD- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:TIGR04520 88 NQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447167138 176 DSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-220 |
9.50e-35 |
|
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: 124.08 E-value: 9.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYG--NKDNVT-KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNS----DIT 73
Cdd:COG4778 1 MTTLLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 74 RLKSKSLDKFRKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVL-SKYPYQISGGQKQR 152
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHD-AFTASYARRILFINDG 220
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDeEVREAVADRVVDVTPF 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-222 |
1.05e-34 |
|
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: 123.85 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGFVFQDFNLLDT 100
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN-IGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 lTAYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP-----------YQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:cd03245 93 -TLRDNITLG---APLAD---DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 170 EPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-239 |
1.75e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS----TIDHV-TTGKIIINNSDItRL 75
Cdd:COG1117 8 LEPKIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmndLIPGArVEGEILLDGEDI-YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 76 KSKSLDKFRKNeLGFVFQDFNLLdTLTAYENIALALTIKGEAS-SKIDGKI----QAVAKYLDIEQVLSKYPYQISGGQK 150
Cdd:COG1117 83 PDVDVVELRRR-VGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSkSELDEIVeeslRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDSKSARllleRFESLNKDLKA--TILMVTHdafTASYARRI----LFINDGKIfI 224
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTA----KIEELILELKKdyTIVIVTH---NMQQAARVsdytAFFYLGEL-V 232
|
250
....*....|....*
gi 447167138 225 ELvrgnDSRKEFFTK 239
Cdd:COG1117 233 EF----GPTEQIFTN 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-222 |
3.03e-34 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 121.17 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVTkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFr 84
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLD-TLTayENIalaltikgeasskidgkiqavakyldieqvlskypyqISGGQKQRVASARAIVTDP 163
Cdd:cd03246 78 ---VGYLPQDDELFSgSIA--ENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-222 |
5.56e-34 |
|
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: 122.34 E-value: 5.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVT-------KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKsksLDKFRKNeLGF 90
Cdd:cd03253 4 ENVTfaydpgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRA-IGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQDFNLLDTlTAYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAI 159
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYG---RPDAT---DEEVIEAAKAAQIHDKIMRFPdgYDtivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-225 |
7.76e-34 |
|
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: 121.88 E-value: 7.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFR 84
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAF-TASYARRILFINDGKIFIE 225
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAE 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-222 |
1.56e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIE-KYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksksldKFR 84
Cdd:cd03226 1 RIENISfSYKKG----TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-------KER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNL-LDTLTAYENIALALtikgEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:cd03226 70 RKSIGYVMQDVDYqLFTDSVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKAtILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDyEFLAKVCDRVLLLANGAI 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-222 |
2.24e-33 |
|
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: 120.84 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDH---VTTGKIIINNSDITRlksk 78
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 slDKFRKNeLGFVFQDFNLLDTLTAYENIALALTIKG--EASSKIDGKIQAVA--KYLDIEQVLSKYPYQISGGQKQRVA 154
Cdd:cd03234 77 --DQFQKC-VAYVRQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 155 SARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMV---THDAFtaSYARRILFINDGKI 222
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIhqpRSDLF--RLFDRILLLSSGEI 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-223 |
3.61e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.46 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 28 SFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfrKNELGFVFQDFNLLDTLTAYENI 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 108 ALALT--IKGEASSKIdgKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLE 185
Cdd:PRK10771 93 GLGLNpgLKLNAAQRE--KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 186 RFESLNKDLKATILMVTH---DAftASYARRILFINDGKIF 223
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHsleDA--ARIAPRSLVVADGRIA 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-226 |
4.02e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.79 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTK------AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkfRKNELGFVF 92
Cdd:PRK11607 24 NLTKsfdgqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 93 QDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 173 GSLDSK-SARLLLERFESLNKdLKATILMVTHDAFTA-SYARRILFINDGKiFIEL 226
Cdd:PRK11607 178 GALDKKlRDRMQLEVVDILER-VGVTCVMVTHDQEEAmTMAGRIAIMNRGK-FVQI 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-222 |
8.59e-33 |
|
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: 119.26 E-value: 8.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 14 YGNKDNvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQ 93
Cdd:cd03251 10 YPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 94 DFNLLDTlTAYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTD 162
Cdd:cd03251 84 DVFLFND-TVAENIAYG---RPGAT---REEVEEAARAANAHEFIMELPegYDtvigergvkLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 163 PSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.59e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.84 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYgnKDNvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlksKSL 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----AEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNELGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:PRK13647 74 EKWVRSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDA-FTASYARRILFINDGKIFIE 225
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVdLAAEWADQVIVLKEGRVLAE 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-222 |
2.87e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIEKYYGNKDNvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKFRK 85
Cdd:PRK13632 9 KVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 NeLGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:PRK13632 84 K-IGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-225 |
3.26e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 118.19 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI---TRLKSKSLD 81
Cdd:COG4161 3 IQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNeLGFVFQDFNLLDTLTAYEN-IALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:COG4161 79 LLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 161 TDPSLVLADEPTGSLDSKsarlLLERFESLNKDLKAT-I--LMVTHD-AFTASYARRILFINDGKIfIE 225
Cdd:COG4161 158 MEPQVLLFDEPTAALDPE----ITAQVVEIIRELSQTgItqVIVTHEvEFARKVASQVVYMEKGRI-IE 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-225 |
4.57e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.19 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYgnkdNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS---TIDHVTTGKIIINNSDITRLKS 77
Cdd:PRK09984 1 MQTIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 78 KSLDkFRKN--ELGFVFQDFNLLDTLTAYENI---ALALTIKGEASSKIDGKIQAVAKYLDIEQV-LSKYPYQ----ISG 147
Cdd:PRK09984 77 LARD-IRKSraNTGYIFQQFNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQALTRVgMVHFAHQrvstLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 148 GQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA-FTASYARRILFINDGKIFIE 225
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYD 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-236 |
5.17e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHV-----TTGKIIINNSDITRLKSK 78
Cdd:PRK14239 5 ILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 SLDkFRKnELGFVFQDFNLLdTLTAYENIALALTIKGEASSKI-----DGKIQAVAKYLDIEQVLSKYPYQISGGQKQRV 153
Cdd:PRK14239 81 TVD-LRK-EIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVldeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLkaTILMVTHDAFTAS-YARRILFINDGkifiELVRGNDS 232
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASrISDRTGFFLDG----DLIEYNDT 231
|
....
gi 447167138 233 RKEF 236
Cdd:PRK14239 232 KQMF 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-204 |
6.17e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 117.88 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldkf 83
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rknELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:PRK11248 71 ---ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-222 |
1.72e-31 |
|
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: 116.47 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSD-----ITRLKSK 78
Cdd:TIGR02323 3 LLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 SLDKFRKNELGFVFQdfNLLDTL----TAYENIALALTIKGEASSkidGKIQAVA----KYLDIEQV-LSKYPYQISGGQ 149
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQ--NPRDGLrmrvSAGANIGERLMAIGARHY---GNIRATAqdwlEEVEIDPTrIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLD-SKSARlLLERFESLNKDLKATILMVTHDAFTAS-YARRILFINDGKI 222
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDvSVQAR-LLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRV 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-222 |
2.24e-31 |
|
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: 115.71 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDFNLLDTl 101
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 TAYENIALAltikgeASSKIDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:cd03249 92 TIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
3.56e-31 |
|
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: 120.56 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKT----TLLNCISTIDHVTTGKIIINNSDITRLK 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 SKSLDKFRKNELGFVFQD----FNLLdtLTAYENIALALTIKGEASSKidgkiQAVAKYLD-IEQV--------LSKYPY 143
Cdd:COG4172 83 ERELRRIRGNRIAMIFQEpmtsLNPL--HTIGKQIAEVLRLHRGLSGA-----AARARALElLERVgipdperrLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 144 QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
3.61e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIekYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsdiTRLKSKSL 80
Cdd:PRK13635 2 KEEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKnELGFVFQ--DFNLLDTlTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARA 158
Cdd:PRK13635 77 WDVRR-QVGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-222 |
4.90e-31 |
|
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: 120.17 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTL----LNCISTidhvtTGKIIINNSDITRLKSKSLDKFRKnELGFVFQD-FN 96
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDpFG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDT-LTAYENIALALTIKGEASSKIDgKIQAVAKYLdiEQV------LSKYPYQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:COG4172 374 SLSPrMTVGQIIAEGLRVHGPGLSAAE-RRARVAEAL--EEVgldpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 170 EPTGSLD-SKSARlLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4172 451 EPTSALDvSVQAQ-ILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKV 504
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
6.30e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.02 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSL 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRK-----NELGFVFQdfNLLDTL----TAYENIALALTIKGEassKIDGKIQAVAkyLD-IEQV------LSKYPYQ 144
Cdd:PRK11701 79 SEAERrrllrTEWGFVHQ--HPRDGLrmqvSAGGNIGERLMAVGA---RHYGDIRATA--GDwLERVeidaarIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 145 ISGGQKQRVASARAIVTDPSLVLADEPTGSLD-SKSARLL-LERfeSLNKDLKATILMVTHDAFTAS-YARRILFINDGK 221
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARLLdLLR--GLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGR 229
|
.
gi 447167138 222 I 222
Cdd:PRK11701 230 V 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-225 |
8.69e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 8.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI---TRLKSKSLD 81
Cdd:PRK11124 3 IQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNeLGFVFQDFNLLDTLTAYENIAlaltikgEASSKIDG--KIQAVAKYLDIEQVL------SKYPYQISGGQKQRV 153
Cdd:PRK11124 79 ELRRN-VGMVFQQYNLWPHLTVQQNLI-------EAPCRVLGlsKDQALARAEKLLERLrlkpyaDRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSK-SARLLlerfeSLNKDLKAT-I--LMVTHD-AFTASYARRILFINDGKIfIE 225
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEiTAQIV-----SIIRELAETgItqVIVTHEvEVARKTASRVVYMENGHI-VE 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-222 |
1.28e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.59 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 12 KYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGFV 91
Cdd:TIGR03375 472 AYPGQE---TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRN-IGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 92 FQDFNLLdTLTAYENIALAltikgeASSKIDGKIQAVAKYLDIEQVLSKYP----YQI-------SGGQKQRVASARAIV 160
Cdd:TIGR03375 545 PQDPRLF-YGTLRDNIALG------APYADDEEILRAAELAGVTEFVRRHPdgldMQIgergrslSGGQRQAVALARALL 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
1.86e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.03 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYgNKDNVT--KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSld 81
Cdd:COG1101 1 MLELKNLSKTF-NPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 kfRKNELGFVFQDfNLLDT---LTAYENIALALTiKGEASSKIDGKIQAVAKY---------LDIEQVLSKYPYQISGGQ 149
Cdd:COG1101 78 --RAKYIGRVFQD-PMMGTapsMTIEENLALAYR-RGKRRGLRRGLTKKRRELfrellatlgLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH---DAFtaSYARRILFINDGKI 222
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeQAL--DYGNRLIMMHEGRI 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-222 |
2.79e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 115.22 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKT-TLLNCISTIDH---VTTGKIIINNSDITRLKSKS 79
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYpgrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKNELGFVFQD--FNLLDTLTAYENIALALTIKGEASSKIdgKIQAVAKYL------DIEQVLSKYPYQISGGQKQ 151
Cdd:PRK11022 83 RRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKT--RRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSLD----SKSARLLLErfesLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLE----LQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-215 |
3.46e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 117.77 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNvtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfr 84
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 knELGFVFQDFNLLDTlTAYENIALAltiKGEAS-SKIDGKIQAVAkyLD---------IEQVLSKYPYQISGGQKQRVA 154
Cdd:TIGR02857 397 --QIAWVPQHPFLFAG-TIAENIRLA---RPDASdAEIREALERAG--LDefvaalpqgLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 155 SARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRIL 215
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALADRIV 527
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-226 |
3.79e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 113.23 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdNVTKAIDnisFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNS------DITRLksk 78
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaearEDTRL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 sldkfrknelgfVFQDFNLLDTLTAYENIALALtiKGEASSKIDGKIQAVAkyldIEQVLSKYPYQISGGQKQRVASARA 158
Cdd:PRK11247 86 ------------MFQDARLLPWKKVIDNVGLGL--KGQWRDAALQALAAVG----LADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIFIEL 226
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIGLDL 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-222 |
4.16e-30 |
|
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: 112.38 E-value: 4.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSkslDKF 83
Cdd:COG0410 3 MLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP---HRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALaltikGEASSKIDGKIQAvakylDIEQVLSKYPY----------QISGGQKQRV 153
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLL-----GAYARRDRAEVRA-----DLERVYELFPRlkerrrqragTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLdsksARLLLER-FESLnKDLKA---TILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL----APLIVEEiFEII-RRLNRegvTILLVEQNARFAlEIADRAYVLERGRI 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-222 |
6.49e-30 |
|
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: 114.44 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQDFNLLDTLTAYEN 106
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IALALTIKGEASSKIdgKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLER 186
Cdd:TIGR02142 96 LRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 447167138 187 FESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-215 |
8.03e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS-TIDHV--TTGKIIINNSDITRLKSksldkfRKNELGFVFQDFNLLDT 100
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPA------EQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALAL--TIKGEAsskidgKIQAVakyldiEQVLSK---------YPYQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:COG4136 91 LSVGENLAFALppTIGRAQ------RRARV------EQALEEaglagfadrDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 170 EPTGSLDsKSARLLLER--FESLnKDLKATILMVTHDAFTASYARRIL 215
Cdd:COG4136 159 EPFSKLD-AALRAQFREfvFEQI-RQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-222 |
9.18e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 9.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI-----TRLKSKSLD-------KFRK---- 85
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkkTKEKEKVLEklviqktRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 ----NELGFVFQ--DFNLLDTlTAYENIALALTIKGeaSSKIDGKIQAvAKYLDI----EQVLSKYPYQISGGQKQRVAS 155
Cdd:PRK13651 101 keirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMG--VSKEEAKKRA-AKYIELvgldESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFFKDGKI 243
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-222 |
1.03e-28 |
|
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: 108.61 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTtlLNCISTI------DHVTTGKIIINNSDITRLKsksldkFRKNELGFVFQD-- 94
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKS--LTCLAILgllppgLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNpr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 --FNLLDTLT--AYENIALALTIKGEASSKIDGKIQAVAkYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:TIGR02770 73 taFNPLFTMGnhAIETLRSLGKLSKQARALILEALEAVG-LPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:TIGR02770 152 PTTDLDVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-244 |
2.05e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItRLKSKSLDKFRKnELGFVFQdfNLLDT 100
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRK-TVGIVFQ--NPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 L---TAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDS 177
Cdd:PRK13639 91 LfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 178 KSARLLLERFESLNKDlKATILMVTHDA-FTASYARRILFINDGKIF-----------IELVRGNDSRKEFFTKIIEVI 244
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTHDVdLVPVYADKVYVMSDGKIIkegtpkevfsdIETIRKANLRLPRVAHLIEIL 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-223 |
3.55e-28 |
|
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: 107.48 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKiiinnsDIT----RLKSKS 79
Cdd:COG1119 3 LLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRlfgeRRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKNeLGFVFQDF--NLLDTLTAYENIALALT----IKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRV 153
Cdd:COG1119 73 VWELRKR-IGLVSPALqlRFPRDETVLDVVLSGFFdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH------DAFTasyarRILFINDGKIF 223
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveeipPGIT-----HVLLLKDGRVV 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-222 |
3.69e-28 |
|
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: 106.93 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDFNL 97
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTlTAYENIALA-LTIKGEasskidgKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTDPSL 165
Cdd:cd03254 89 FSG-TIMENIRLGrPNATDE-------EVIEAAKEAGAHDFIMKLPngYDtvlgenggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-222 |
1.31e-27 |
|
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: 106.03 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDfNLLDTLT 102
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALAltikGEASSKidGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:cd03252 92 IRDNIALA----DPGMSM--ERVIEAAKLAGAHDFISELPegYDtivgeqgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 172 TGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
1.35e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 110.28 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKD-NVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSD--ITRLKSKSL 80
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFR-KNELGFVFQDFNLLDTLTAYENI--ALALTIKGEAsskidGKIQAV-----AKYLD--IEQVLSKYPYQISGGQK 150
Cdd:TIGR03269 359 GRGRaKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDEL-----ARMKAVitlkmVGFDEekAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA-FTASYARRILFINDGKI 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdFVLDVCDRAALMRDGKI 506
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-171 |
2.18e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKF 83
Cdd:COG1137 3 TLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL---PMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGF------VFQDfnlldtLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASAR 157
Cdd:COG1137 76 ARLGIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 447167138 158 AIVTDPSLVLADEP 171
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-225 |
2.66e-27 |
|
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: 103.55 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 14 YGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkskSLDKFRKNELGFVFQ 93
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-----DLEKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 94 DFNLLDTlTAYENIALaltikgeasskidgkiqavakyldieqvlskypyQISGGQKQRVASARAIVTDPSLVLADEPTG 173
Cdd:cd03247 83 RPYLFDT-TLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 174 SLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-222 |
3.01e-27 |
|
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: 109.45 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFrkneLGFVFQDFNLLDTlTA 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIA-LaltikGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:COG4618 423 AENIArF-----GDAD---PEKVVAAAKLAGVHEMILRLPdgYDtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 172 TGSLDSKSARLLLERFESLnKDLKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:COG4618 495 NSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-246 |
8.09e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIE-KYYGNKDNVTkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlKSKS 79
Cdd:PRK13650 1 MSNIIEVKNLTfKYKEDQEKYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKneLGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARA 158
Cdd:PRK13650 77 WDIRHK--IGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKifielVRGNDSRKEFFT 238
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ-----VESTSTPRELFS 229
|
....*...
gi 447167138 239 KIIEVITL 246
Cdd:PRK13650 230 RGNDLLQL 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-222 |
1.09e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkDNVTKAIDnisFKVDEGEFVGIMGPSGSGKTTLLNCISTI-----DHVTTGKIIINNSDITrl 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGS-NHVIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIY-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 76 kSKSLDKFR-KNELGFVFQDFNLLDTLTAYENIALALTI------KGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGG 148
Cdd:PRK14267 75 -SPDVDPIEvRREVGMVFQYPNPFPHLTIYDNVAIGVKLnglvksKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 149 QKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLkaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSpAQAARVSDYVAFLYLGKL 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-222 |
1.27e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIekYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFr 84
Cdd:TIGR01842 317 LSVENV--TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLDTlTAYENIALAltikGEASSkiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRV 153
Cdd:TIGR01842 394 ---IGYLPQDVELFPG-TVAENIARF----GENAD--PEKIIEAAKLAGVHELILRLPdgYDtvigpggatLSGGQRQRI 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-225 |
2.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 12 KYYGNKDNVTK-AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlKSKSLDKFRkNELGF 90
Cdd:PRK13633 13 KYESNEESTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIR-NKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQ--DFNLLDTLTAyENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLA 168
Cdd:PRK13633 90 VFQnpDNQIVATIVE-EDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 169 DEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-222 |
2.45e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHV-----TTGKIIINNSDITRLK 76
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 SKSLDKfrknELGFVFQDFNLLDTLTAYENIALALTI------KGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQK 150
Cdd:PRK14247 77 VIELRR----RVQMVFQIPNPIPNLSIFENVALGLKLnrlvksKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLkaTILMVTHdaFTASYAR---RILFINDGKI 222
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH--FPQQAARisdYVAFLYKGQI 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-223 |
3.70e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDIT-RLKSKSLDKFRKnELGFVFQdF--NL 97
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRK-KVGIVFQ-FpeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTLTAYENIALALTIKG----EASSKIDGKIQAVAkyLDiEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTG 173
Cdd:PRK13634 98 LFEETVEKDICFGPMNFGvseeDAKQKAREMIELVG--LP-EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 174 SLDSKSARLLLERFESLNKDLKATILMVTH---DAftASYARRILFINDGKIF 223
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeDA--ARYADQIVVMHKGTVF 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-172 |
3.82e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.83 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSldkfR 84
Cdd:TIGR03410 1 LEVSNLNVYYGQ----SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 -KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLdiEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:TIGR03410 73 aRAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
....*....
gi 447167138 164 SLVLADEPT 172
Cdd:TIGR03410 151 KLLLLDEPT 159
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-238 |
8.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDIT-RLKSKSLDKFRKnELGFVFQdfnlLD 99
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLRK-KVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIALALTIKGEAS---SKIDGKIQAVaKYLD----IEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK13641 95 EAQLFENTVLKDVEFGPKNfgfSEDEAKEKAL-KWLKkvglSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 173 GSLDSKSARLLLERFESLNKDlKATILMVTHDA-FTASYARRILFINDGKifieLVRgNDSRKEFFT 238
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMdDVAEYADDVLVLEHGK----LIK-HASPKEIFS 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-224 |
1.34e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 7 VEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsDITrlksksldkfrkn 86
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 eLGFVFQDFNLLDTLTAYENIALALTIKGEASSKID----------------GKIQAVAKYLD-------IEQVLSK--- 140
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDGDAELRALEAELEeleaklaepdedlerlAELQEEFEALGgweaearAEEILSGlgf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 141 ---YPYQ----ISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSaRLLLERFesLnKDLKATILMVTHD-AFTASYAR 212
Cdd:COG0488 142 peeDLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-IEWLEEF--L-KNYPGTVLVVSHDrYFLDRVAT 217
|
250
....*....|..
gi 447167138 213 RILFINDGKIFI 224
Cdd:COG0488 218 RILELDRGKLTL 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-222 |
1.68e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 16 NKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQDF 95
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 176 DSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-222 |
1.78e-25 |
|
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: 100.10 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsditRLKSKSLDKFRKNeLGFVF-QDFNLLDTL 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRR-IGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 TAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSAR 181
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447167138 182 LLLERFESLNKDLKATILMVTHDAF-TASYARRILFINDGKI 222
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRL 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-203 |
1.96e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAIDNISFKVDE---GEFV-GIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsditRLKSKSLDKF----RKNELGF 90
Cdd:PRK11144 5 NFKQQLGDLCLTVNLtlpAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RVLFDAEKGIclppEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQDFNLLDTLTAYENiaLALTIKGEASSKIDgkiqAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:PRK11144 81 VFQDARLFPHYKVRGN--LRYGMAKSMVAQFD----KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190
....*....|....*....|....*....|...
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDLKATILMVTH 203
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSH 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-225 |
2.17e-25 |
|
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: 99.21 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfr 84
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDgkiqAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKIFIE 225
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLIEE 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-204 |
3.60e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.91 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKD-----NVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsdiTRL 75
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 76 KSKSlDKFRKNELGFVFQDFNllDTLTAYENIALALtikgEASSKIDGKIQAVAKYLDIEQVLSK----------YPYQI 145
Cdd:COG4167 78 EYGD-YKYRCKHIRMIFQDPN--TSLNPRLNIGQIL----EEPLRLNTDLTAEEREERIFATLRLvgllpehanfYPHML 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 146 SGGQKQRVASARAIVTDPSLVLADEPTGSLD----SKSARLLLErfesLNKDLKATILMVTHD 204
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDmsvrSQIINLMLE----LQEKLGISYIYVSQH 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-230 |
4.80e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.50 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKNeLGFVFQDFNL 97
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRN-IAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTlTAYENIALAltiKGEASskiDGKIQAVAKY---LD-IEQVLSKYPY-------QISGGQKQRVASARAIVTDPSLV 166
Cdd:PRK13657 421 FNR-SIEDNIRVG---RPDAT---DEEMRAAAERaqaHDfIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 167 LADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI-----FIELVRGN 230
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVvesgsFDELVARG 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-222 |
5.16e-25 |
|
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: 97.11 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskslDKFR 84
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-----SPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGfvfqdfnlldtltayenialaltikgeasskidgkIQAVakyldieqvlskypYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03216 72 ARRAG-----------------------------------IAMV--------------YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTH---DAFtaSYARRILFINDGKI 222
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrldEVF--EIADRVTVLRDGRV 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-223 |
5.97e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.00 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 6 SVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrk 85
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 nELGFVFQDFNLLDTLTAYENIAL--------ALTIKGEAssKIDgkiQAVAkYLDIEQVLSKYPYQISGGQKQRVASAR 157
Cdd:COG4604 76 -RLAILRQENHINSRLTVRELVAFgrfpyskgRLTAEDRE--IID---EAIA-YLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA-FTASYARRILFINDGKIF 223
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInFASCYADHIVAMKDGRVV 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-222 |
6.48e-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: 98.37 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLksksldkfrknELGFVFQdfnllDTLT 102
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----------GLGGGFN-----PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKyPY-QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSAR 181
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL-PVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447167138 182 LLLERFESLNKDLKaTILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03220 180 KCQRRLRELLKQGK-TVILVSHDpSSIKRLCDRALVLEKGKI 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-230 |
1.05e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 102.21 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 25 DNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfRKnELGFVFQD---FNllDTL 101
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RA-AIGIVPQDtvlFN--DTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 taYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP--YQ---------ISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:COG5265 449 --AYNIAYG---RPDAS---EEEVEAAARAAQIHDFIESLPdgYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKIfIElvRGN 230
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRI-VE--RGT 575
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-228 |
1.20e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 25 DNISFKVDEGEFVGIMGPSGSGKTTLLNCIST-IDHvtTGKIIINNsdiTRLKSKSLDKFRKNeLGFVFQDFNLLDTlTA 103
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPY--QGSLKING---IELRELDPESWRKH-LSWVGQNPQLPHG-TL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYP----YQI-------SGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK11174 440 RDNVLLG---NPDAS---DEQLQQALENAWVSEFLPLLPqgldTPIgdqaaglSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 173 GSLDSKSARLLLerfESLNKDLKA-TILMVTHD-AFTASYaRRILFINDGKI-----FIELVR 228
Cdd:PRK11174 514 ASLDAHSEQLVM---QALNAASRRqTTLMVTHQlEDLAQW-DQIWVMQDGQIvqqgdYAELSQ 572
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-203 |
1.22e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSL 80
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF---RSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNELGFVFQDFNLLDTLTAYENIALALTIKGeaSSKID-GKIQAVAkyldiEQVLSKYPYQI---------SGGQK 150
Cdd:COG1129 74 RDAQAAGIAIIHQELNLVPNLSVAENIFLGREPRR--GGLIDwRAMRRRA-----RELLARLGLDIdpdtpvgdlSVAQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTH 203
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-203 |
1.34e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKsksldKF 83
Cdd:PRK13537 7 PIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-----RH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDP 163
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 164 SLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTH 203
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-222 |
1.98e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITR--LKSKSLDKFRKnELGFVFQ--DFNL 97
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRK-EIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTlTAYENIALALTIKGEASSKIDGKIQAVAKYLDI-EQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 177 SKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKI 222
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-223 |
2.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkSKSLDKFRKNeLGFVFQ--DFNLLDT 100
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRKH-IGIVFQnpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYEnIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSA 180
Cdd:PRK13648 100 IVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447167138 181 RLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIF 223
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVY 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-222 |
2.76e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.34 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTllnCISTIDHV---TTGKIIINNSDITRLKSKSLDKfrknELGFVFQDfNLLDTLT 102
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKST---VAALLQNLyqpTGGQVLLDGVPLVQYDHHYLHR----QVALVGQE-PVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTikgeasSKIDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:TIGR00958 571 VRENIAYGLT------DTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 172 TGSLDSKSARLLLERFESLNKdlkaTILMVTHDAFTASYARRILFINDGKI 222
Cdd:TIGR00958 645 TSALDAECEQLLQESRSRASR----TVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-222 |
3.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDIT-RLKSKSLDKFRKnELGFVFQdfnlLDT 100
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRPVRK-RIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTIKGEASSKID-GKIQAVAKYLDIE-----QVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGS 174
Cdd:PRK13646 96 SQLFEDTVEREIIFGPKNFKMNlDEVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447167138 175 LDSKSARLLLERFESLNKDLKATILMVTHDAF-TASYARRILFINDGKI 222
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-222 |
1.49e-23 |
|
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: 94.27 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsditrlksKSLDKFR 84
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAFTAS-YARRILFINDGKI 222
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-203 |
2.94e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItRLKSkSL 80
Cdd:COG3845 2 MPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRS-PR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKfRKNELGFVFQDFNLLDTLTAYENIALALTIKGEAS---SKIDGKIQAVA-KY-LDIEqvLSKYPYQISGGQKQRVAS 155
Cdd:COG3845 76 DA-IALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRldrKAARARIRELSeRYgLDVD--PDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLlerFESLnKDLKA---TILMVTH 203
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADEL---FEIL-RRLAAegkSIIFITH 199
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-205 |
3.17e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.01 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIekyyGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSkslD 81
Cdd:PRK10247 5 SPLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKnELGFVFQDFNLLDTlTAYENIALALTIKGEASSKidgkiQAVAKYLD----IEQVLSKYPYQISGGQKQRVASAR 157
Cdd:PRK10247 78 IYRQ-QVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP-----AIFLDDLErfalPDTILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA 205
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
3.19e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrLKSKSLDK 82
Cdd:PRK13636 4 YILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKNeLGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVT 161
Cdd:PRK13636 80 LRES-VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 162 DPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFT-ASYARRILFINDGKIFIE 225
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQ 223
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-241 |
4.63e-23 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 93.62 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDnvtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKfr 84
Cdd:TIGR03740 1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDLHK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDgkiqAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:TIGR03740 72 ---IGSLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKIFIE-LVRGNDSRKEFFTKII 241
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHIlSEVQQLADHIGIISEGVLGYQgKINKSENLEKLFVEVV 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-204 |
8.68e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.97 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKT----TLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQD-FN 96
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEpSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLD-TLTAYENIALAL---TIKGEASSKIDGKIQAVAKYL------DIEQVLSKYPYQISGGQKQRVASARAIVTDPSLV 166
Cdd:COG4170 101 CLDpSAKIGDQLIEAIpswTFKGKWWQRFKWRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 447167138 167 LADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
1.17e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 92.87 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIekyygnkdNVT----KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLk 76
Cdd:COG4674 7 HGPILYVEDL--------TVSfdgfKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 skslDKFRKNELGFV--FQDFNLLDTLTAYENIALAL--------TIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQIS 146
Cdd:COG4674 78 ----DEHEIARLGIGrkFQKPTVFEELTVFENLELALkgdrgvfaSLFARLTAEERDRIEEVLETIGLTDKADRLAGLLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 147 GGQKQRVASARAIVTDPSLVLADEPT-GSLDS---KSARLLLerfeSLNKDlkATILMVTHD-AFTASYARRILFINDGK 221
Cdd:COG4674 154 HGQKQWLEIGMLLAQDPKLLLLDEPVaGMTDAeteRTAELLK----SLAGK--HSVVVVEHDmEFVRQIARKVTVLHQGS 227
|
....
gi 447167138 222 IFIE 225
Cdd:COG4674 228 VLAE 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-204 |
1.87e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.02 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKT----TLLNCISTiDHVTTGKIIINNSDITRLK 76
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 77 SKSLDKFRKNELGFVFQDfnLLDTLTAYENIALALT---------IKGEASSKIDGKIQAVaKYLDIEQVLSKYPYQISG 147
Cdd:PRK09473 88 EKELNKLRAEQISMIFQD--PMTSLNPYMRVGEQLMevlmlhkgmSKAEAFEESVRMLDAV-KMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 148 GQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-204 |
1.98e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.91 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 25 DNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKnELGFVFQDFNLLDTLTAY 104
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 105 ENIALAL---TIKGEA--SSKIDGKIQAVAkyldIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKS 179
Cdd:PRK11831 103 DNVAYPLrehTQLPAPllHSTVMMKLEAVG----LRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180
....*....|....*....|....*
gi 447167138 180 ARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-203 |
2.40e-22 |
|
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: 95.25 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAID------NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHV--TTGKIIIN------------NSDITRLKS 77
Cdd:TIGR03269 4 KNLTKKFDgkevlkNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverPSKVGEPCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 78 KSLDKFRKNELGF-----------------VFQ-DFNLLDTLTAYENIALALTikgEASSKIDGKIQAVAKYLDIEQV-- 137
Cdd:TIGR03269 84 VCGGTLEPEEVDFwnlsdklrrrirkriaiMLQrTFALYGDDTVLDNVLEALE---EIGYEGKEAVGRAVDLIEMVQLsh 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 138 -LSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTH 203
Cdd:TIGR03269 161 rITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-222 |
3.32e-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: 90.18 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 20 VTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKFRKNELGFVFQD---FN 96
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR---RSPRDAIRAGIAYVPEDrkrEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDTLTAYENIALaltikgeasskidgkiqavakyldieqvlskyPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:cd03215 89 LVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 177 SKSARLLLERFESLNKDLKAtILMVTHD-AFTASYARRILFINDGKI 222
Cdd:cd03215 137 VGAKAEIYRLIRELADAGKA-VLLISSElDELLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-222 |
3.45e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.72 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR-----KNELGFVFqdfnll 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 dtlTAYENIALALTIKGEASSKIDgkiQAVAKYLDIEQVLS----KYPyQISGGQKQRVASARAIV-------TDPSLVL 167
Cdd:COG4559 91 ---TVEEVVALGRAPHGSSAAQDR---QIVREALALVGLAHlagrSYQ-TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 168 ADEPTGSLDSKSARLLLErfesLNKDL---KATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4559 164 LDEPTSALDLAHQHAVLR----LARQLarrGGGVVAVLHDlNLAAQYADRILLLHQGRL 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-230 |
4.07e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.70 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 13 YYGNKDnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVF 92
Cdd:PRK11176 350 TYPGKE--VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL----RNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 93 QDFNLL-DTLTayENIALAltiKGEASSKIDgkIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIV 160
Cdd:PRK11176 424 QNVHLFnDTIA--NNIAYA---RTEQYSREQ--IEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 161 TD-PSLVLaDEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKIfIElvRGN 230
Cdd:PRK11176 497 RDsPILIL-DEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEI-VE--RGT 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
4.11e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYY------------------GNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTT 62
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 63 GKIIINNSdITRLksksLdkfrknELGFVFQdfnllDTLTAYENIALALTIKGEASSKIDGKIQAVA------KYLDieQ 136
Cdd:COG1134 81 GRVEVNGR-VSAL----L------ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVefaelgDFID--Q 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 137 VLSKYpyqiSGGQKQRVASARAIVTDPSLVLADEPTGSLDS----KSARLLLERFESlnkdlKATILMVTHDAFT-ASYA 211
Cdd:COG1134 143 PVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRES-----GRTVIFVSHSMGAvRRLC 213
|
250
....*....|.
gi 447167138 212 RRILFINDGKI 222
Cdd:COG1134 214 DRAIWLEKGRL 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-238 |
4.86e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHV------TTGKIIINNSDITRLKSKSLDKfrknELGFVFQDFNL 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTLTAYENIALALTIKG-----EASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGikekrEIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 173 GSLDSKSARLLLERFESLNKDLkaTILMVTHD-AFTASYARRILFINDGkifiELVRGNDSrKEFFT 238
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYVAFLYNG----ELVEWGSS-NEIFT 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-239 |
5.13e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYgnKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTT---LLNCISTIDHVTTGKIIInnsDITRLKSKS 79
Cdd:PRK13640 4 NIVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITV---DGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKnELGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARA 158
Cdd:PRK13640 79 VWDIRE-KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFielvrGNDSRKEFFT 238
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL-----AQGSPVEIFS 232
|
.
gi 447167138 239 K 239
Cdd:PRK13640 233 K 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-204 |
5.34e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.85 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKnELGFVFQD--FNLLD 99
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIALAL-TIKGEAS-SKIDGKIQAV-AKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK15079 114 RMTIGEIIAEPLrTYHPKLSrQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|.
gi 447167138 177 -SKSARL--LLerfESLNKDLKATILMVTHD 204
Cdd:PRK15079 194 vSIQAQVvnLL---QQLQREMGLSLIFIAHD 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-222 |
5.57e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.37 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFR 84
Cdd:PRK13548 3 LEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 -----KNELGFVFqdfnlldtlTAYENIALALTIKGEASSKIDgkiQAVAKYLdiEQV----LSKYPY-QISGGQKQRVA 154
Cdd:PRK13548 79 avlpqHSSLSFPF---------TVEEVVAMGRAPHGLSRAEDD---ALVAAAL--AQVdlahLAGRDYpQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 155 SARAIV------TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-222 |
6.62e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 13 YYGNKDnvtkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFrkneLGFVF 92
Cdd:PRK13652 13 YSGSKE----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 93 Q--DFNLLDTlTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:PRK13652 85 QnpDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-209 |
9.48e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 9.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHV-----TTGKIIINNSDitrLKSK 78
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKN---LYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 SLDKFR-KNELGFVFQDFNLLDTlTAYENIALALTI---KGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVA 154
Cdd:PRK14243 83 DVDPVEvRRRIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 155 SARAIVTDPSLVLADEPTGSLDSKSARllleRFESLNKDLKA--TILMVTHDAFTAS 209
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTL----RIEELMHELKEqyTIIIVTHNMQQAA 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-222 |
1.03e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKDNVTKA-----IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKS 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 78 KSLDKFRKnELGFVFQD----FNLLDTLTAY--ENIALALTI-KGEASSKIDGKIQAVAkyLDIEqVLSKYPYQISGGQK 150
Cdd:PRK10419 82 AQRKAFRR-DIQMVFQDsisaVNPRKTVREIirEPLRHLLSLdKAERLARASEMLRAVD--LDDS-VLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDsksaRLLLERFESLNKDLKA----TILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKLQQqfgtACLFITHDlRLVERFCQRVMVMDNGQI 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-221 |
2.48e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.66 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrkneLGFV--FQDFNLLDT 100
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-----MGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENI-----------ALALTIKGEASSKIDGK-IQAVAKYLD---IEQVLSKYPYQISGGQKQRVASARAIVTDPSL 165
Cdd:PRK11300 95 MTVIENLlvaqhqqlktgLFSGLLKTPAFRRAESEaLDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGK 221
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmKLVMGISDRIYVVNQGT 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-204 |
2.78e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTT----LLNCISTidhvtTGKIIINNSDITRLKSKSLDKFRKnELGFVFQDFN-- 96
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDTLTAYENIALALTIKGEASSKIDGKIQAVAKY----LDIEqVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMeevgLDPE-TRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190
....*....|....*....|....*....|..
gi 447167138 173 GSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-204 |
3.86e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKT----TLLNCISTIDHV-TTGKIIINNSDITRLKSK 78
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 SLDKFRKNELGFVFQD----FNLLDTLTA--YENIALALTIKGEASSkidGKIQAVAKYLDIEQV---LSKYPYQISGGQ 149
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmvsLNPLHTLEKqlYEVLSLHRGMRREAAR---GEILNCLDRVGIRQAakrLTDYPHQLSGGE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
4.75e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKT-TLLNCISTIDH----VTTGKIIIN--NSDITR 74
Cdd:PRK10261 10 RDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQagglVQCDKMLLRrrSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 75 LKSKS---LDKFRKNELGFVFQD--FNLLDTLTAYENIALALTIKGEASSkiDGKIQAVAKYLDI------EQVLSKYPY 143
Cdd:PRK10261 90 LSEQSaaqMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASR--EEAMVEAKRMLDQvripeaQTILSRYPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 144 QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGK 221
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-204 |
5.28e-21 |
|
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: 91.65 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrknELGFVFQDFNLLDTlT 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALAltiKGEASskiDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:TIGR02868 425 VRENLRLA---RPDAT---DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*...
gi 447167138 172 TGSLDSKSARLLLErfeslnkDLKA-----TILMVTHD 204
Cdd:TIGR02868 499 TEHLDAETADELLE-------DLLAalsgrTVVLITHH 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-203 |
7.70e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 10 IEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKttllnciSTIDHVTTGKIIINNSDITRLKSKSLDKFR--KNE 87
Cdd:PRK13536 47 VSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGK-------STIARMILGMTSPDAGKITVLGVPVPARARlaRAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 88 LGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTH 203
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTH 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-222 |
1.17e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCI---STIDHVTTGKIIINNSDITRlkskslDKFRKNElGFVFQDFNLLDT 100
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDA------KEMRAIS-AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTIKGEASSKIDGKIQAVAkylDIEQVLSKYPYQ------------ISGGQKQRVASARAIVTDPSLVLA 168
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERVD---EVLQALGLRKCAntrigvpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 169 DEPTGSLDSKSARLLLERFESLNKDLKaTILMVTH-------DAFTasyarRILFINDGKI 222
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHqpsselfELFD-----KIILMAEGRV 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-222 |
1.43e-20 |
|
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: 86.78 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 12 KYYGNKDNVTKaidNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFRKNeLGFV 91
Cdd:cd03244 11 RYRPNLPPVLK---NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSR-ISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 92 FQD---------FNlLDTLTAY--ENIALALtikgeASSKIDGKIQAVAKYLDIEQVLSKypYQISGGQKQRVASARAIV 160
Cdd:cd03244 84 PQDpvlfsgtirSN-LDPFGEYsdEELWQAL-----ERVGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-225 |
1.66e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 9 KIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDiTRLKSKsLDKFRKnEL 88
Cdd:PRK13644 3 RLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSK-LQGIRK-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 89 GFVFQDFNLL--------DTLTAYENIALALTikgEASSKIDgkiQAVAKyLDIEQVLSKYPYQISGGQKQRVASARAIV 160
Cdd:PRK13644 80 GIVFQNPETQfvgrtveeDLAFGPENLCLPPI---EIRKRVD---RALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 161 TDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-222 |
1.72e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEkyYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfr 84
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KNELGFVFQDFNLL-DTLTayENIALAltikgeASSKIDGKIQAV------AKYLDIEQVLSKY----PYQISGGQKQRV 153
Cdd:PRK11160 413 RQAISVVSQRVHLFsATLR--DNLLLA------APNASDEALIEVlqqvglEKLLEDDKGLNAWlgegGRQLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-242 |
1.84e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYgnkdNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTT-----GKIIINNSDITRlKSKS 79
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE-RRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKnELGFVFQDFNLLdTLTAYENIALALTIKG-EASSKIDGKIQAVAKYLD----IEQVLSKYPYQISGGQKQRVA 154
Cdd:PRK14258 83 LNRLRR-QVSMVHPKPNLF-PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 155 SARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDaftasyARRILFINDgkiFIELVRGNDSRk 234
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN------LHQVSRLSD---FTAFFKGNENR- 230
|
....*...
gi 447167138 235 efFTKIIE 242
Cdd:PRK14258 231 --IGQLVE 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
1.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKDNVTKaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIInnsDITRLKSKSL 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKnELGFVFQD-FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:PRK13642 77 WNLRR-KIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIE 225
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-222 |
4.09e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsdiTRLKsksld 81
Cdd:COG0488 313 KKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVK----- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 kfrkneLGFVFQDFNLLD-TLTAYENIAlaltikgEASSkiDGKIQAVAKYL--------DIEQVLSKypyqISGGQKQR 152
Cdd:COG0488 380 ------IGYFDQHQEELDpDKTVLDELR-------DGAP--GGTEQEVRGYLgrflfsgdDAFKPVGV----LSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLL---LERFEslnkdlkATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALeeaLDDFP-------GTVLLVSHDrYFLDRVATRILEFEDGGV 507
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-204 |
4.90e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.33 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlKSKSLDKFRKNELGFVFQdfNLLDTL 101
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQ--NPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 TAYENIALALtikgEASSKIDGKIQAVAKYLDIEQVLSK----------YPYQISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:PRK11308 106 NPRKKVGQIL----EEPLLINTSLSAAERREKALAMMAKvglrpehydrYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|....
gi 447167138 172 TGSLD-SKSARlLLERFESLNKDLKATILMVTHD 204
Cdd:PRK11308 182 VSALDvSVQAQ-VLNLMMDLQQELGLSYVFISHD 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-222 |
6.73e-20 |
|
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: 85.22 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDfNLLDT 100
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQE-PVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTikgeasSKIDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:cd03248 102 RSLQDNIAYGLQ------SCSFECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 170 EPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-179 |
1.26e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKF 83
Cdd:PRK10895 3 TLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQDFNLLDTLTAYENIALALTIKGEASS-KIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTD 162
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAeQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170
....*....|....*..
gi 447167138 163 PSLVLADEPTGSLDSKS 179
Cdd:PRK10895 156 PKFILLDEPFAGVDPIS 172
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-222 |
1.50e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 83.62 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDFNLL 98
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 DTltayeNIALALTIKGEASskiDGKIQAVAKyldieqvLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSK 178
Cdd:cd03369 95 SG-----TIRSNLDPFDEYS---DEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447167138 179 SARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03369 160 TDALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-222 |
1.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIE-KYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRL-KSKSLD 81
Cdd:PRK13643 1 MIKFEKVNyTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKnELGFVFQ--DFNLLDTlTAYENIALA---LTIKGEASSKIDG-KIQAVAKYldiEQVLSKYPYQISGGQKQRVAS 155
Cdd:PRK13643 81 PVRK-KVGVVFQfpESQLFEE-TVLKDVAFGpqnFGIPKEKAEKIAAeKLEMVGLA---DEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTH--DAfTASYARRILFINDGKI 222
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHlmDD-VADYADYVYLLEKGHI 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-222 |
2.09e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKf 83
Cdd:PRK11231 2 TLRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rknELGFVFQDFNLLDTLTAYENIALA----LTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAI 159
Cdd:PRK11231 77 ---RLALLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVTHDAFTAS-YARRILFINDGKI 222
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASrYCDHLVVLANGHV 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-222 |
3.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.41 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDIT-RLKSKSLDKFRKnELGFVFQ--DFNLL 98
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKQIRK-KVGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 DTlTAYENIALALTIKGeaSSKIDGKIQAVAKYLDI---EQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PRK13649 100 EE-TVLKDVAFGPQNFG--VSQEEAEALAREKLALVgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447167138 176 DSKSARLLLERFESLNKDlKATILMVTH---DafTASYARRILFINDGKI 222
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHlmdD--VANYADFVYVLEKGKL 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-214 |
4.52e-19 |
|
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: 82.41 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkfRKNELGFVFQDFNLLDTLTAYE 105
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIALALTIKGEASSKIDGKIQAVAkYLDIEQVLSKypyQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLE 185
Cdd:TIGR01189 93 NLHFWAAIHGGAQRTIEDALAAVG-LTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180 190
....*....|....*....|....*....|
gi 447167138 186 RFES-LNKdlKATILMVTHDAFTASYARRI 214
Cdd:TIGR01189 169 LLRAhLAR--GGIVLLTTHQDLGLVEAREL 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-221 |
5.81e-19 |
|
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: 82.13 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 16 NKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSditrlksksldkfrkneLGFVFQDF 95
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLLDTlTAYENIALALTIKGEASSKIdgkIQAVAKYLDIEQVLSKYPYQI-------SGGQKQRVASARAIVTDPSLVLA 168
Cdd:cd03250 76 WIQNG-TIRENILFGKPFDEERYEKV---IKACALEPDLEILPDGDLTEIgekginlSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 169 DEPTGSLDSKSARLLLERfeSLNKDLK--ATILMVTHDAFTASYARRILFINDGK 221
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEN--CILGLLLnnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-188 |
6.66e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 25 DNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKskslDKFRKnelgfvfqdfNLL------ 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR----DEYHQ----------DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 ---DTLTAYENIALALTIKGEASSkiDGKIQAVAKY--LDIEQVLSKypyQISGGQKQRVASARAIVTDPSLVLADEPTG 173
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGPGDD--EALWEALAQVglAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170
....*....|....*
gi 447167138 174 SLDSKSARLLLERFE 188
Cdd:PRK13538 159 AIDKQGVARLEALLA 173
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-214 |
1.27e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 83.31 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTID----HVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQDFNl 97
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 lDTLTAYENIALAL-------TIKGEASSKIDGKIQAVAKYL------DIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:PRK15093 100 -SCLDPSERVGRQLmqnipgwTYKGRWWQRFGWRKRRAIELLhrvgikDHKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 165 LVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTAS-YARRI 214
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqWADKI 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-203 |
2.57e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFrkneLGFvfQDFnLLDTLTAYE 105
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LGH--RNA-MKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIALALTIKGEASSKIDGKIQAVAKYlDIEQVLSKYpyqISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLE 185
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEAVGLA-PLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*....
gi 447167138 186 RFES-LNKDlkATILMVTH 203
Cdd:PRK13539 169 LIRAhLAQG--GIVIAATH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-221 |
2.77e-18 |
|
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: 78.64 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinnsditrlksksldkfr 84
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 knelgfvfqdfnlldTLTAYENIAlaltikgeasskidgkiqavakYLDieqvlskypyQISGGQKQRVASARAIVTDPS 164
Cdd:cd03221 58 ---------------TWGSTVKIG----------------------YFE----------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 165 LVLADEPTGSLDSKSaRLLLERFesLnKDLKATILMVTHD-AFTASYARRILFINDGK 221
Cdd:cd03221 91 LLLLDEPTNHLDLES-IEALEEA--L-KEYPGTVILVSHDrYFLDQVATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-222 |
2.95e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNeLGFVFQD-FNLLDT- 100
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpYASLDPr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTIKG-----EASSKIDGKIQAVAkyLDIEQVLsKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PRK10261 418 QTVGDSIMEPLRVHGllpgkAAAARVAWLLERVG--LLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 176 DSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDmAVVERISHRVAVMYLGQI 542
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-222 |
3.45e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrknELGFVFQDFNLLDT 100
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR----RVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTI-KGEASSKIDGKIQAVAKYL---DIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK09536 92 FDVRQVVEMGRTPhRSRFDTWTETDRAAVERAMertGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 177 SKSARLLLERFESLNKDLKATILMVtHD-AFTASYARRILFINDGKI 222
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAI-HDlDLAARYCDELVLLADGRV 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-222 |
7.07e-18 |
|
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: 82.48 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 5 LSVEKIEKYYGNKDNVtkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFr 84
Cdd:TIGR01193 474 IVINDVSYSYGYGSNI---LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 kneLGFVFQD---F------NLLdtLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEqvLSKYPYQISGGQKQRVAS 155
Cdd:TIGR01193 550 ---INYLPQEpyiFsgsileNLL--LGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE--LSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlkaTILMVTHDAFTASYARRILFINDGKI 222
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-225 |
1.08e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 14 YGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrknELGFVFQ 93
Cdd:PRK10253 17 YGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 94 DFNLLDTLTAYENIA--------LALTIKGEASSKIDGKIQAVAkyldIEQVLSKYPYQISGGQKQRVASARAIVTDPSL 165
Cdd:PRK10253 89 NATTPGDITVQELVArgryphqpLFTRWRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 166 VLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTA-SYARRILFINDGKIFIE 225
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
34-221 |
1.32e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 34 GEFVGIMGPSGSGKTTLLNCIS--TIDHVTTGKIIINNSDITRLKSKsldkfrknELGFVFQDFNLLDTLTAYENIALAL 111
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTKQILK--------RTGFVTQDDILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 112 TIKGEASSKIDGKIQaVAKYLDIEQVLSK---------YPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARL 182
Cdd:PLN03211 166 LLRLPKSLTKQEKIL-VAESVISELGLTKcentiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 183 LLERFESLNKDLKaTILMVTHDAFTASYA--RRILFINDGK 221
Cdd:PLN03211 245 LVLTLGSLAQKGK-TIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-203 |
2.38e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.89 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNK-DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLN-----------CISTIDHVTTGKIIINNSD 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 72 ITRL--KSKSLDKFRKNeLGFVFQ--DFNLLDTlTAYENIALALTIKGEasSKIDGKiQAVAKYLDI----EQVLSKYPY 143
Cdd:PRK13631 101 TNPYskKIKNFKELRRR-VSMVFQfpEYQLFKD-TIEKDIMFGPVALGV--KKSEAK-KLAKFYLNKmgldDSYLERSPF 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 144 QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLErfesLNKDLKA---TILMVTH 203
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ----LILDAKAnnkTVFVITH 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-222 |
2.38e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSksldKFRKNeLGFVF-QDFNLLDT 100
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRK----EFARR-IGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD--SK 178
Cdd:COG4586 111 LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 179 SA--RLLLErfesLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4586 191 EAirEFLKE----YNRERGTTILLTSHDmDDIEALCDRVIVIDHGRI 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
5.61e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEkyYGNKDNVTkAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldKF 83
Cdd:COG3845 257 VLEVENLS--VRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR---ER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQD---FNLLDTLTAYENIALALTIKGEASSK--ID-GKIQAVAKYLdIEQvlskypYQI------------ 145
Cdd:COG3845 331 RRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPPFSRGgfLDrKAIRAFAEEL-IEE------FDVrtpgpdtparsl 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 146 SGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSA----RLLLERfeslnKDLKATILMVTHD---AFtaSYARRILFIN 218
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIefihQRLLEL-----RDAGAAVLLISEDldeIL--ALSDRIAVMY 476
|
....
gi 447167138 219 DGKI 222
Cdd:COG3845 477 EGRI 480
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-215 |
1.21e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.35 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGkiiinnsditrlkskSLDKFRKNELGFVFQDFNLLDTL- 101
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 -TAYENIALAL--------TIKGEASSKIDGKIQAVakylDIEQvLSKYPYQ-ISGGQKQRVASARAIVTDPSLVLADEP 171
Cdd:NF040873 72 lTVRDLVAMGRwarrglwrRLTRDDRAAVDDALERV----GLAD-LAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447167138 172 TGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTASYARRIL 215
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-215 |
1.70e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsditrlksksldkfRKNELGFV-----FQDFNLL 98
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLpqrpyLPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 DTLtAYENIALALTikgeasskiDGKIQAV---------AKYLDIEQVLSKypyQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:COG4178 444 EAL-LYPATAEAFS---------DAELREAleavglghlAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447167138 170 EPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRIL 215
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVL 554
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-204 |
2.24e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinnsditrlksKSL 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRkneLGFVFQDFNLLDTLtayenialALTIK-------GEASSKIDGKIQAV-AKYLdIEQVLSKypyqISGGQKQR 152
Cdd:PRK09544 65 GKLR---IGYVPQKLYLDTTL--------PLTVNrflrlrpGTKKEDILPALKRVqAGHL-IDAPMQK----LSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-225 |
2.76e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTI-DHVT----TGKIIINNSDItrLKSKSLDKFRKnELGFVFQDFNLL 98
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSI--FNYRDVLEFRR-RVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 dTLTAYENI-----ALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTG 173
Cdd:PRK14271 114 -PMSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 174 SLDSKSARLLLERFESLNKDLkaTILMVTHD-AFTASYARRILFINDGKIFIE 225
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
4.05e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsl 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dKFRKNELGFVFQDFNLLDTLTAYENIALaltikGEASSKIDGKIQAVAKYLDIEQVLSKYPYQ----ISGGQKQRVASA 156
Cdd:PRK11614 76 -KIMREAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 157 RAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTA-SYARRILFINDGKIFIE 225
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQAlKLADRGYVLENGHVVLE 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-222 |
4.26e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.45 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKDNvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKsksLD 81
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDH--PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRK-----NELGFVFQDfnlldtlTAYENIALAltiKGEASSKidgKIQAVAKYLDIEQVLSKYP--YQ---------I 145
Cdd:PRK10789 386 SWRSrlavvSQTPFLFSD-------TVANNIALG---RPDATQQ---EIEHVARLASVHDDILRLPqgYDtevgergvmL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 146 SGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKdlKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-222 |
4.55e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHvTTGKIIINNSDITRLKSKSLDKFRknelGFVFQDFNLLDTLTAYEN 106
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IALALTiKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV-----TDPS--LVLADEPTGSLD--S 177
Cdd:COG4138 90 LALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDvaQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 178 KSARL-LLERFeslnKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4138 169 QAALDrLLREL----CQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
6.12e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.53 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKF 83
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rknelGFV------FQDFNLLDTLtayenIALAlTIKGEASSKIDGKIQAVAKYLDIE-------QVLSKypyqisgGQK 150
Cdd:COG4152 74 -----GYLpeerglYPKMKVGEQL-----VYLA-RLKGLSKAEAKRRADEWLERLGLGdrankkvEELSK-------GNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 151 QRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQmELVEELCDRIVIINKGRK 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-185 |
6.26e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsldkFRKNELGFVFQDFNllDTL 101
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQRIRMIFQDPS--TSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 TAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQV------LSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PRK15112 101 NPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVgllpdhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170
....*....|....
gi 447167138 176 D----SKSARLLLE 185
Cdd:PRK15112 181 DmsmrSQLINLMLE 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-222 |
7.20e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTtlLNCISTID------HVTTGKIIInnsDITRLKSKSLdkfRKNELGFVFQD--- 94
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLL---DGKPVAPCAL---RGRKIATIMQNprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 -FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAkYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTG 173
Cdd:PRK10418 91 aFNPLHTMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447167138 174 SLDSKSARLLLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-219 |
1.29e-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: 72.19 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsditrlksksldkfRKNELGFVFQdfnlldtlta 103
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLFLPQ---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 yenialaltikgeasskidgkiqavAKYLDI----EQVLskYPYQ--ISGGQKQRVASARAIVTDPSLVLADEPTGSLDS 177
Cdd:cd03223 72 -------------------------RPYLPLgtlrEQLI--YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447167138 178 KSARLLLERFeslnKDLKATILMVTHDAFTASYARRILFIND 219
Cdd:cd03223 125 ESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-203 |
2.83e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIstidhvtTGKiiinnsdITRLKSKSLDKFRKNELGfvfQDFNL 97
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------AGA-------LKGTPVAGCVDVPDNQFG---REASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTLTAYENIALALtikgeasskidgKIQAVAKYLDIEQVLSKYPyQISGGQKQRVASARAIVTDPSLVLADEPTGSLDS 177
Cdd:COG2401 103 IDAIGRKGDFKDAV------------ELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*.
gi 447167138 178 KSARLLLERFESLNKDLKATILMVTH 203
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-222 |
2.84e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI-TRLKSkslDKFRkNELGFVFqDF------N 96
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvARLQQ---DPPR-NVEGTVY-DFvaegieE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDTLTAYEniALALTIKGEASSK-------------------IDGKIQAVAKY--LDIEQVLSkypyQISGGQKQRVAS 155
Cdd:PRK11147 94 QAEYLKRYH--DISHLVETDPSEKnlnelaklqeqldhhnlwqLENRINEVLAQlgLDPDAALS----SLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 156 ARAIVTDPSLVLADEPTGSLDSKSarllLERFESLNKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDrSFIRNMATRIVDLDRGKL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-223 |
5.96e-15 |
|
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: 74.28 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItrlkSKSLDKFRKNeLGFVFQDFNLLDTLT 102
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS-LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARL 182
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447167138 183 ---LLERFESlnkdlKATILMVTHDAFTAS-YARRILFINDGKIF 223
Cdd:TIGR01257 1100 iwdLLLKYRS-----GRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-203 |
7.08e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGnkdnVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSL 80
Cdd:PRK09700 2 ATPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfRKNELGFVFQDFNLLDTLTAYENIALA--LTIKGEASSKID-GKIQAVA----KYLDIEQVLSKYPYQISGGQKQRV 153
Cdd:PRK09700 78 ---AQLGIGIIYQELSVIDELTVLENLYIGrhLTKKVCGVNIIDwREMRVRAammlLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447167138 154 ASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKAtILMVTH 203
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTA-IVYISH 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-203 |
1.00e-14 |
|
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: 70.60 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKskslDKFRKNELGFVFQDfNLLDTLTAYEN 106
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR----DSIARGLLYLGHAP-GIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IALALTIKGEasskiDGKIQAVAKyLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLER 186
Cdd:cd03231 94 LRFWHADHSD-----EQVEEALAR-VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 447167138 187 FESlNKDLKATILMVTH 203
Cdd:cd03231 168 MAG-HCARGGMVVLTTH 183
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-222 |
1.41e-14 |
|
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: 69.98 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIdhvTTGKIIINNSdiTRLKSKSLD 81
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGD--IHYNGIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFR---KNELGFVFQDFNLLDTLTAYENIALALTIKGEASSKidgkiqavakyldieqvlskypyQISGGQKQRVASARA 158
Cdd:cd03233 76 EFAekyPGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVR-----------------------GISGGERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYAR--RILFINDGKI 222
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLfdKVLVLYEGRQ 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-202 |
2.16e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVT----KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlKSKSLDKFRK--------- 85
Cdd:PRK09700 270 NVTsrdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKgmayitesr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 NELGFvFQDFNLldtltaYENIALALTIK--------GEASSKIDGKIQAVAKYL------DIEQVLSkypyQISGGQKQ 151
Cdd:PRK09700 348 RDNGF-FPNFSI------AQNMAISRSLKdggykgamGLFHEVDEQRTAENQRELlalkchSVNQNIT----ELSGGNQQ 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKaTILMVT 202
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVS 466
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-199 |
2.21e-14 |
|
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: 72.74 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKDnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlksKSLDK 82
Cdd:TIGR01257 1936 DILRLNELTKVYSGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKNeLGFVFQDFNLLDTLTAYENIALALTIKGEASSKIDG----KIQAVAKYLDIEQVLSKYpyqiSGGQKQRVASARA 158
Cdd:TIGR01257 2010 VHQN-MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTY----SGGNKRKLSTAIA 2084
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATIL 199
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-219 |
2.23e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDitRLKSKSLdKFRKNELGFVFQDFNLL------- 98
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINL-KWWRSKIGVVSQDPLLFsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 99 --------------------DTLTAYENI------------ALALTIKGEASSKI-----------DGKIQAVAKYLDIE 135
Cdd:PTZ00265 480 ikyslyslkdlealsnyyneDGNDSQENKnkrnscrakcagDLNDMSNTTDSNELiemrknyqtikDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 136 QVLSKYP-----------YQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250
....*....|....*
gi 447167138 205 AFTASYARRILFIND 219
Cdd:PTZ00265 640 LSTIRYANTIFVLSN 654
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-208 |
3.02e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKsksldkfRKNELGFVFQDFNLLDTLTAYEN 106
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKypyQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARlLLER 186
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT-LVNR 178
|
170 180
....*....|....*....|..
gi 447167138 187 FESLNKDLKATILMVTHDAFTA 208
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAA 200
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-222 |
3.26e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinnsditrlksksld 81
Cdd:PRK15064 317 RNALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKN-ELGFVFQD--------FNLLDTLTAYenialaltikgeasSKIDGKIQAVAKYL--------DIEqvlsKYPYQ 144
Cdd:PRK15064 377 KWSENaNIGYYAQDhaydfendLTLFDWMSQW--------------RQEGDDEQAVRGTLgrllfsqdDIK----KSVKV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 145 ISGGQKQRVASARAIVTDPSLVLADEPTGSLDsksarllLERFESLN---KDLKATILMVTHD-AFTASYARRILFINDG 220
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNmalEKYEGTLIFVSHDrEFVSSLATRIIEITPD 511
|
..
gi 447167138 221 KI 222
Cdd:PRK15064 512 GV 513
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-196 |
3.36e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTI-DHVT-TGKIIINNSDitrLKSKSLD 81
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSP---LKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNELGFVFQDFNLLDTLTAYENIALA--LTIKGeasskidGKIQAVAKYLDIEQVL----------SKYPYQISGGQ 149
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGneITLPG-------GRMAYNAMYLRAKNLLrelqldadnvTRPVGDYGGGQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLErfesLNKDLKA 196
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLD----IIRDLKA 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-172 |
3.95e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIekyygnkdNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNsdiTRLKSKSLDKF 83
Cdd:COG1129 256 VLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 RKNELGFVFQD---FNLLDTLTAYENIALALTIKGEASSKID-GKIQAVA---------KYLDIEQVLSkypyQISGGQK 150
Cdd:COG1129 325 IRAGIAYVPEDrkgEGLVLDLSIRENITLASLDRLSRGGLLDrRRERALAeeyikrlriKTPSPEQPVG----NLSGGNQ 400
|
170 180
....*....|....*....|..
gi 447167138 151 QRVASARAIVTDPSLVLADEPT 172
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-196 |
5.14e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGnkdnVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTI-DHVT-TGKIIINNSDitrLKSK 78
Cdd:PRK13549 2 MEYLLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEE---LQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 79 SLDKFRKNELGFVFQDFNLLDTLTAYENIALaltikGEASSKiDGKIQAVAKYLDIEQVLSKYPYQIS---------GGQ 149
Cdd:PRK13549 75 NIRDTERAGIAIIHQELALVKELSVLENIFL-----GNEITP-GGIMDYDAMYLRAQKLLAQLKLDINpatpvgnlgLGQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 150 KQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLErfesLNKDLKA 196
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLD----IIRDLKA 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-222 |
6.75e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTID--HVTTGKIIINNSDITRLkskSLDKfRKNE-LGFVFQD------ 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILEL---SPDE-RARAgIFLAFQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 ---FNLLdtLTAYENialaltIKGEASSKID--GKIQAVAKYLDIEQVLSKYPYQI--SGGQKQRVASARAIVTDPSLVL 167
Cdd:COG0396 92 vsvSNFL--RTALNA------RRGEELSAREflKLLKEKMKELGLDEDFLDRYVNEgfSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHdaftasYAR--------RILFINDGKI 222
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH------YQRildyikpdFVHVLVDGRI 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-222 |
2.42e-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: 66.78 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCIstIDH----VTTGKIIINNSDITRLksksldkfrknelgfvfqdfnlld 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHpkyeVTEGEILFKGEDITDL------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 tlTAYENIALALTIKGEASSKIDG-KIQAVAKYLDieqvlskypYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSK 178
Cdd:cd03217 70 --PPEERARLGIFLAFQYPPEIPGvKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447167138 179 SARLLLERFESLnKDLKATILMVTHDAFTASYAR--RILFINDGKI 222
Cdd:cd03217 139 ALRLVAEVINKL-REEGKSVLIITHYQRLLDYIKpdRVHVLYDGRI 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-204 |
6.31e-13 |
|
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: 68.04 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVtkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnSDITrlksksldkf 83
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rkneLGFVFQDFNLLDTLTAYENIALALTIKGEASSKID--------------------GKIQAV---AKYLDIEQVLS- 139
Cdd:TIGR03719 70 ----VGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNeisakyaepdadfdklaaeqAELQEIidaADAWDLDSQLEi 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 140 -----KYP------YQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSArLLLERFEslnKDLKATILMVTHD 204
Cdd:TIGR03719 146 amdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERHL---QEYPGTVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-180 |
7.56e-13 |
|
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: 65.34 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCIS--TIDHVTTGKIIINnsdiTRLKSKSLDKfrknELGFVFQDFNLLDTL 101
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILIN----GRPLDKNFQR----STGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 102 TAYENIalaltikgEASSKIDGkiqavakyldieqvlskypyqISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSA 180
Cdd:cd03232 95 TVREAL--------RFSALLRG---------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
62-219 |
9.34e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 62 TGKIIINNSDITRLKSKSLdkfrKNELGFVFQDfNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYldIEQVLSKY 141
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDL----RNLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEF--IESLPNKY 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 142 -----PY--QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRI 214
Cdd:PTZ00265 1349 dtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKI 1428
|
....*
gi 447167138 215 LFIND 219
Cdd:PTZ00265 1429 VVFNN 1433
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-222 |
2.15e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLN------CISTIDH--VTTGKIIINNSDITRLKSKSLDKFR-----KNELGF 90
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdlTGGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 91 VFQDFNLLdTLTAYENIAlaltiKGEASSKIDGKI--QAVAKyLDIEQVLSKYPYQISGGQKQRVASARAI--------- 159
Cdd:PRK13547 97 AFSAREIV-LLGRYPHAR-----RAGALTHRDGEIawQALAL-AGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 160 VTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHDA-FTASYARRILFINDGKI 222
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-220 |
2.21e-12 |
|
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: 64.27 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNELGFVFQDFNLLDTlTA 103
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALTIKGEASSKIdgkIQAVAKYLDIEQV-------LSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:cd03290 96 EENITFGSPFNKQRYKAV---TDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447167138 177 SK-SARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDG 220
Cdd:cd03290 173 IHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-204 |
4.32e-12 |
|
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: 65.58 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 33 EGEFVGIMGPSGSGKTTLLNCIStidhvttGKIIINNSDITRLKSKS--LDKFRKNELGFVFQDFNLLDTLTAY-----E 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILS-------GELKPNLGDYDEEPSWDevLKRFRGTELQDYFKKLANGEIKVAHkpqyvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIALALtiKGEAS---SKID--GKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSK-- 178
Cdd:COG1245 171 LIPKVF--KGTVRellEKVDerGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqr 248
|
170 180
....*....|....*....|....*...
gi 447167138 179 --SARLLLErfesLNKDLKAtILMVTHD 204
Cdd:COG1245 249 lnVARLIRE----LAEEGKY-VLVVEHD 271
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-203 |
4.64e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItrlksksldKFRKNELGF------VFQDF 95
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFASTTAALaagvaiIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 NLLDTLTAYENIAL-------ALTIKGEASSKIDGKIQAVAKYLDIEQVLsKYpyqISGGQKQRVASARAIVTDPSLVLA 168
Cdd:PRK11288 89 HLVPEMTVAENLYLgqlphkgGIVNRRLLNYEAREQLEHLGVDIDPDTPL-KY---LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190
....*....|....*....|....*....|....*
gi 447167138 169 DEPTGSLDSKSARLLLERFESLNKDLKAtILMVTH 203
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSH 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-221 |
5.11e-12 |
|
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: 63.97 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 21 TKAIDNISFKVDEGEF-----VGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlksksldkFRKNELGFVFQdf 95
Cdd:cd03237 7 KKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 96 nlldtltayenialaLTIKGEASSKIDGK------IQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:cd03237 76 ---------------GTVRDLLSSITKDFythpyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 170 EPTGSLDSKSaRLL----LERFeSLNKdlKATILMVTHDAFTASYARRILFINDGK 221
Cdd:cd03237 141 EPSAYLDVEQ-RLMaskvIRRF-AENN--EKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-221 |
1.07e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCIS-TIDHvtTGKIIINNSDITRLKSKSLDKFRknelGFVFQDFNLLDTLTAYE 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAgLLPG--SGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIALALTiKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIV-TDPS------LVLADEPTGSLD-S 177
Cdd:PRK03695 89 YLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDinpagqLLLLDEPMNSLDvA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 178 KSARL--LLERFESLNkdlkATILMVTHDA-FTASYARRILFINDGK 221
Cdd:PRK03695 168 QQAALdrLLSELCQQG----IAVVMSSHDLnHTLRHADRVWLLKQGK 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-204 |
2.15e-11 |
|
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: 62.00 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 33 EGEFVGIMGPSGSGKTTLLNCIStidhvttGKIIINNSDITRLKS--KSLDKFRKNELGFVFQDFnLLDTLTA-----YE 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILA-------GKLKPNLGKFDDPPDwdEILDEFRGSELQNYFTKL-LEGDVKVivkpqYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIaLALTIKGEAS---SKID--GKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSK-- 178
Cdd:cd03236 97 DL-IPKAVKGKVGellKKKDerGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqr 175
|
170 180
....*....|....*....|....*...
gi 447167138 179 --SARLLLErfesLNKDLKAtILMVTHD 204
Cdd:cd03236 176 lnAARLIRE----LAEDDNY-VLVVEHD 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-203 |
3.95e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDkfrknelgfvfqdfnllDTLT 102
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN-----------------GQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARL 182
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|.
gi 447167138 183 LLERFESLNKDLKaTILMVTH 203
Cdd:PRK13545 182 CLDKMNEFKEQGK-TIFFISH 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-241 |
1.09e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 20 VTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIinnsditrlksksldkfRKNELGFVFQdFNLLD 99
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------------HSGRISFSSQ-FSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIALALTIKgeasskiDGKIQAVAKYLDIEQVLSKYPYQ-----------ISGGQKQRVASARAIVTDPSLVLA 168
Cdd:cd03291 111 PGTIKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 169 DEPTGSLDSKSARlllERFESLNKDLKA--TILMVTHDAFTASYARRILFINDGK-----IFIELvrgNDSRKEFFTKII 241
Cdd:cd03291 184 DSPFGYLDVFTEK---EIFESCVCKLMAnkTRILVTSKMEHLKKADKILILHEGSsyfygTFSEL---QSLRPDFSSKLM 257
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-180 |
1.34e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCIStiDHVTTGKIiinNSDITRLKSKSLDKFRKNELGFVFQDFNLLDTLTA 103
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVI---TGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALTIKGEASSKIDGKIQAVAKYLDIEQvLSKYPYQISG--------GQKQRVASARAIVTDP-SLVLADEPTGS 174
Cdd:TIGR00956 854 RESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLE-MESYADAVVGvpgeglnvEQRKRLTIGVELVAKPkLLLFLDEPTSG 932
|
....*.
gi 447167138 175 LDSKSA 180
Cdd:TIGR00956 933 LDSQTA 938
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-223 |
1.53e-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: 60.72 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 3 NILSVEKIEKYYGNKdnvtKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSditrLKSKSLDK 82
Cdd:TIGR03719 321 KVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET----VKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 83 FRKnelgfvfqdfNLLDTLTAYENIALALTI----KGEASSK-------IDGKIQavakyldieqvlSKYPYQISGGQKQ 151
Cdd:TIGR03719 393 SRD----------ALDPNKTVWEEISGGLDIiklgKREIPSRayvgrfnFKGSDQ------------QKKVGQLSGGERN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFEslnkDLKATILMVTHDA-FTASYARRIL-FINDGKIF 223
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISHDRwFLDRIATHILaFEGDSHVE 520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-203 |
2.13e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSK-SLDkfrkNELGFVFQDFNLLDT 100
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALE----NGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 101 LTAYENIALA-LTIKGE--ASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDS 177
Cdd:PRK10982 88 RSVMDNMWLGrYPTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180
....*....|....*....|....*.
gi 447167138 178 KSARLLLERFESLnKDLKATILMVTH 203
Cdd:PRK10982 168 KEVNHLFTIIRKL-KERGCGIVYISH 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-204 |
3.33e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 33 EGEFVGIMGPSGSGKTTLLNCIStidhvttGKIIINNSDITRLKSKS--LDKFRKNELGFVFQDFNLLDTLTAY-----E 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILS-------GELIPNLGDYEEEPSWDevLKRFRGTELQNYFKKLYNGEIKVVHkpqyvD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIALALTIK-GEASSKID--GKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD----SK 178
Cdd:PRK13409 171 LIPKVFKGKvRELLKKVDerGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLN 250
|
170 180
....*....|....*....|....*.
gi 447167138 179 SARLLLERFEslnkdlKATILMVTHD 204
Cdd:PRK13409 251 VARLIRELAE------GKYVLVVEHD 270
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-222 |
4.27e-10 |
|
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: 59.57 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDFNL-------- 97
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLfsgslrmn 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTLTAY--ENIALALTIkgeasSKIDGKIQAVAKYLDIEqvLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:TIGR00957 1380 LDPFSQYsdEEVWWALEL-----AHLKTFVSALPDKLDHE--CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 176 DSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-237 |
4.69e-10 |
|
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: 59.57 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCI-STIDHVTtGKIIInnsditrlksksldkfrKNELGFVFQDfNLLDTLT 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVE-GHVHM-----------------KGSVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSKIdgkIQAVAKYLDIEQVLSKYPYQI-------SGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:TIGR00957 715 LRENILFGKALNEKYYQQV---LEACALLPDLEILPSGDRTEIgekgvnlSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 176 DSKSARLLLERFESLNKDLK-ATILMVTHDAFTASYARRILFINDGKI-----FIELVRGNDSRKEFF 237
Cdd:TIGR00957 792 DAHVGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQVDVIIVMSGGKIsemgsYQELLQRDGAFAEFL 859
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-220 |
5.02e-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: 59.54 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 20 VTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIinnsditrlksksldkfRKNELGFVFQdFNLLD 99
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------------HSGRISFSPQ-TSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIALALTIKgeasskiDGKIQAVAKYLDIEQVLSKYPYQ-----------ISGGQKQRVASARAIVTDPSLVLA 168
Cdd:TIGR01271 500 PGTIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447167138 169 DEPTGSLDSKSARlllERFESLNKDLKA--TILMVTHDAFTASYARRILFINDG 220
Cdd:TIGR01271 573 DSPFTHLDVVTEK---EIFESCLCKLMSnkTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-220 |
5.75e-10 |
|
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: 56.95 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNcistidhvttgkIIINNSDITRLkSKSLDKFRKNELGFVFQdfnlLDTLt 102
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------EGLYASGKARL-ISFLPKFSRNKLIFIDQ----LQFL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 ayenIALALTikgeasskidgkiqavakYLDIEQVLSkypyQISGGQKQRVASARAIV--TDPSLVLADEPTGSLDSKSA 180
Cdd:cd03238 72 ----IDVGLG------------------YLTLGQKLS----TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 181 RLLLERFESLnKDLKATILMVTHDAFTASYARRILFINDG 220
Cdd:cd03238 126 NQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-222 |
5.81e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNC-ISTIDHVTTGKIIINNSditrlksksldkfrkneLGFVFQ---DFNLldtl 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGT-----------------VAYVPQvswIFNA---- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 102 TAYENIALALTIKGEASSK-IDgkIQAVAKYLDI-----EQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PLN03130 694 TVRDNILFGSPFDPERYERaID--VTALQHDLDLlpggdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447167138 176 DSKSARlllERFESLNKD--LKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PLN03130 772 DAHVGR---QVFDKCIKDelRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-197 |
6.03e-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: 59.15 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHvTTGKIIInnsDITRLKSKSLDKFRKnELGFVFQDFNLLD---- 99
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI---DGVSWNSVTLQTWRK-AFGVIPQKVFIFSgtfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 -TLTAYENIAlaltikgeasskiDGKIQAVAKYLDIEQVLSKYP-----------YQISGGQKQRVASARAIVTDPSLVL 167
Cdd:TIGR01271 1310 kNLDPYEQWS-------------DEEIWKVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190
....*....|....*....|....*....|
gi 447167138 168 ADEPTGSLDSKSarlllerFESLNKDLKAT 197
Cdd:TIGR01271 1377 LDEPSAHLDPVT-------LQIIRKTLKQS 1399
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-204 |
8.23e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIInnsditrLKSKSLDKFRKNELGFVFQD------FN 96
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-------LGQPTRQALQKNLVAYVPQSeevdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LL--DTLTA--YENIALALTIKGEASSKIDGKIQAVakylDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK15056 95 VLveDVVMMgrYGHMGWLRRAKKRDRQIVTAALARV----DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|..
gi 447167138 173 GSLDSKSARLLLERFESLnKDLKATILMVTHD 204
Cdd:PRK15056 171 TGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-242 |
9.57e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNC-ISTIDHVTTGKIIINNSditrlksksldkfrkneLGFVFQdFNLLDTLT 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS-----------------VAYVPQ-VSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIALALTIKGEASSK-IDgkIQAVAKYLDI-----EQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PLN03232 695 VRENILFGSDFESERYWRaID--VTALQHDLDLlpgrdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 177 SKSARlllERFESLNKD-LKA-TILMVTHDAFTASYARRILFINDGKI-----FIELVRGNdsrkEFFTKIIE 242
Cdd:PLN03232 773 AHVAH---QVFDSCMKDeLKGkTRVLVTNQLHFLPLMDRIILVSEGMIkeegtFAELSKSG----SLFKKLME 838
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-222 |
9.96e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHvTTGKIIInnsDITRLKSKSLDKFRKnELGFVFQDFNLLdTLTA 103
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI---DGVSWNSVPLQKWRK-AFGVIPQKVFIF-SGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENialaLTIKGEASskiDGKIQAVAKYLDIEQVLSKYP-----------YQISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:cd03289 94 RKN----LDPYGKWS---DEEIWKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 173 GSLDSKSarlllerFESLNKDLK-----ATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03289 167 AHLDPIT-------YQVIRKTLKqafadCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-222 |
1.12e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQDFNLL-DTLtaY 104
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLaDTF--L 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 105 ENIALALTIKGEASSKIDGKIQ--AVAKYLD--IEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSA 180
Cdd:PRK10790 433 ANVTLGRDISEEQVWQALETVQlaELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447167138 181 RLLLERFESLNKdlKATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PRK10790 513 QAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-176 |
1.76e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDI-TRLKSKSLDkfrkNELGFVFQDFN---LLD 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLA----NGIVYISEDRKrdgLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIAL-ALTIKGEASSKIDGK--IQAVAKYLDIEQVLSKYPYQI----SGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK10762 344 GMSVKENMSLtALRYFSRAGGSLKHAdeQQAVSDFIRLFNIKTPSMEQAigllSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
....
gi 447167138 173 GSLD 176
Cdd:PRK10762 424 RGVD 427
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-223 |
2.19e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFRKnELGFVFQDfNLLDTLTAYEN 106
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRR-VLSIIPQS-PVLFSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IalaltikGEASSKIDGKIQAVAKYLDIEQVLSKYPY-----------QISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PLN03232 1330 I-------DPFSEHNDADLWEALERAHIKDVIDRNPFgldaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 176 DSKS----ARLLLERFESlnkdlkATILMVTHDAFTASYARRILFINDGKIF 223
Cdd:PLN03232 1403 DVRTdsliQRTIREEFKS------CTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-227 |
3.56e-09 |
|
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: 56.76 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCI-STIDHVTTGKIIINNSDI-TRLKSKSLdkfrKNELGFVFQD---FN 96
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVdIRNPAQAI----RAGIAMVPEDrkrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDTLTAYENIALALTIKGEASSKID--GKIQAVAKYLDIEQVLSKYPY----QISGGQKQRVASARAIVTDPSLVLADE 170
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSFCFKMRIDaaAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 171 PTGSLDSKSARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIFIELV 227
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFV 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-204 |
4.11e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYYGNKDNVtkaIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnSDITrlksksldkf 83
Cdd:PRK11819 6 IYTMNRVSKVVPPKKQI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 84 rkneLGFVFQDFNLLDTLTAYENIALALtikGEASSKID-----------------------GKIQAV---AKYLDIEQV 137
Cdd:PRK11819 72 ----VGYLPQEPQLDPEKTVRENVEEGV---AEVKAALDrfneiyaayaepdadfdalaaeqGELQEIidaADAWDLDSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 138 LS------KYP------YQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSArLLLERFesLnKDLKATILMVTHD 204
Cdd:PRK11819 145 LEiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQF--L-HDYPGTVVAVTHD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-203 |
4.82e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNKdNVTKAIDnisFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKsl 80
Cdd:PRK15439 8 APPLLCARSISKQYSGV-EVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkfRKNELG--FVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSkypyQISGGQKQRVASARA 158
Cdd:PRK15439 82 ---KAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTH 203
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISH 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-226 |
5.80e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkSKSLDKFRKnELGFVFQDFNLLDTLtayen 106
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRK-LFSAVFTDFHLFDQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 ialaLTIKGEASSKidgkiQAVAKYLDIEQVLSKYPY--------QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSK 178
Cdd:PRK10522 413 ----LGPEGKPANP-----ALVEKWLERLKMAHKLELedgrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447167138 179 SARLLLERFESLNKDLKATILMVTHDAFTASYARRILFINDGKIfIEL 226
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL-SEL 530
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-203 |
6.59e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDItrlkSKSLDKFRKnELGFVFQDFNLLDTLTA 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 104 YENIALALtikgeASSKIDGKIQAVAKYLDIEQVLSkYPYQ-ISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARL 182
Cdd:PRK13540 92 RENCLYDI-----HFSPGAVGITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 447167138 183 LLERFESLNKDLKAtILMVTH 203
Cdd:PRK13540 166 IITKIQEHRAKGGA-VLLTSH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-204 |
6.69e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAIDNISFKV-------------DEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKfrk 85
Cdd:PRK10575 9 DTTFALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 86 nELGFVFQDFNLLDTLTAYENIAL-------ALTIKGEAS-SKIDGKIQAVakylDIEQVLSKYPYQISGGQKQRVASAR 157
Cdd:PRK10575 86 -KVAYLPQQLPAAEGMTVRELVAIgrypwhgALGRFGAADrEKVEEAISLV----GLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDLKATILMVTHD 204
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-176 |
1.64e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 4 ILSVEKIEKYygNKDNVT-KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDH-VTTGKIIINNSditRLKSKSLD 81
Cdd:PRK13549 259 ILEVRNLTAW--DPVNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGK---PVKIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNELGFVFQD---FNLLDTLTAYENIALALTIKGEASSKIDG--KIQAVAKYLDIEQVLSKYPYQ----ISGGQKQR 152
Cdd:PRK13549 334 QAIAQGIAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGGSRIDDaaELKTILESIQRLKVKTASPELaiarLSGGNQQK 413
|
170 180
....*....|....*....|....
gi 447167138 153 VASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-228 |
3.48e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSldkfrKNELGFVF-----QDFNL-LD 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLyLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 100 TLTAYENIALA-----LTIKGEASSKI-DGKIQAVA-KYLDIEQVLSKypyqISGGQKQRVASARAIVTDPSLVLADEPT 172
Cdd:PRK15439 356 APLAWNVCALThnrrgFWIKPARENAVlERYRRALNiKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 173 GSLDSkSARL-LLERFESLNKDLKAtILMVTHD-AFTASYARRILFINDGKIFIELVR 228
Cdd:PRK15439 432 RGVDV-SARNdIYQLIRSIAAQNVA-VLFISSDlEEIEQMADRVLVMHQGEISGALTG 487
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-192 |
5.02e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDniSFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLDKFRKNElgfvFQDFN- 96
Cdd:PRK10938 15 DTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 -LL-----DT-LTAYENIALaltikgeaSSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:PRK10938 89 dMLspgedDTgRTTAEIIQD--------EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180
....*....|....*....|...
gi 447167138 170 EPTGSLDSKSARLLLERFESLNK 192
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQ 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-176 |
1.04e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.55 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 38 GIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKsKSLDKFRKnELGFVFQD------FNLLDTltayeNIALAL 111
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQ-QVATVFQDpeqqifYTDIDS-----DIAFSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447167138 112 TIKGEASSKIDGKIQAVAKYLDiEQVLSKYPYQ-ISGGQKQRVASARAIVTDPSLVLADEPTGSLD 176
Cdd:PRK13638 104 RNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-187 |
1.17e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 15 GNK----DNVTKA------IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSditrLKSKSLDKFR 84
Cdd:PRK11819 321 GDKvieaENLSKSfgdrllIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET----VKLAYVDQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 85 KnelgfvfqdfNLLDTLTAYENIAlaltikgeasskiDGkiqavakyLDIEQV----------LSKYPY----------Q 144
Cdd:PRK11819 397 D----------ALDPNKTVWEEIS-------------GG--------LDIIKVgnreipsrayVGRFNFkggdqqkkvgV 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447167138 145 ISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLL---LERF 187
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALeeaLLEF 491
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-182 |
1.39e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSl 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 dkFRKNELGFVFQDFNLLDTLTAYENIALaltikGEASSKIDGKIQAVAKYLDIEQVLSKY--PY-------QISGGQKQ 151
Cdd:PRK10762 76 --SQEAGIGIIHQELNLIPQLTIAENIFL-----GREFVNRFGRIDWKKMYAEADKLLARLnlRFssdklvgELSIGEQQ 148
|
170 180 190
....*....|....*....|....*....|..
gi 447167138 152 RVASARAIVTDPSLVLADEPTGSL-DSKSARL 182
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTETESL 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-222 |
1.41e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLkskSLDKFRKNeLGFVFQD---------FNl 97
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKV-LGIIPQApvlfsgtvrFN- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 98 LDTLTAYENIALaltikGEASSKIDGK--IQAVAKYLDIEqvLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PLN03130 1333 LDPFNEHNDADL-----WESLERAHLKdvIRRNSLGLDAE--VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447167138 176 DSKSARLLL----ERFESlnkdlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:PLN03130 1406 DVRTDALIQktirEEFKS------CTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-222 |
2.26e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 15 GNKDNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIinnsditrlksksldkfRKNELGFVFQD 94
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 FNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGS 174
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447167138 175 LDSKSARLLLERFESLnKDLKATILMVTHD-AFTASYARRILFINDGKI 222
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKL 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-222 |
4.26e-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: 49.52 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRLKSKSLdkfrKNELGFVFQD--- 94
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQDpil 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 ------FNLLDTLTAYEN-IALALTIkgeasSKIDGKIQAVAKYLDieQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:cd03288 107 fsgsirFNLDPECKCTDDrLWEALEI-----AQLKNMVKSLPGGLD--AVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447167138 168 ADEPTGSLDSKSARLLLERFESLNKDlkATILMVTHDAFTASYARRILFINDGKI 222
Cdd:cd03288 180 MDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-220 |
4.27e-07 |
|
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: 48.14 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 34 GEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksksldkfrknelgfvfqdfnlldtltayenialalti 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL--------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 114 kgeasskidgkiqAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKD 193
Cdd:smart00382 43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 447167138 194 LKA-----TILMVTH------DAFTASYARRILFINDG 220
Cdd:smart00382 110 LLKseknlTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-222 |
4.61e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINnsdiTRLKSKSLDKFRKNelgfvfqdfnlLD-TLT 102
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRAE-----------LDpEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 103 AYENIAlaltiKGEASSKIDGKIQAVAKYLdieQVLSKYPYQ-------ISGGQKQRVASARAIVTDPSLVLADEPTGSL 175
Cdd:PRK11147 400 VMDNLA-----EGKQEVMVNGRPRHVLGYL---QDFLFHPKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447167138 176 DSKSarllLERFESLNKDLKATILMVTHD-AF-----TASYarriLFINDGKI 222
Cdd:PRK11147 472 DVET----LELLEELLDSYQGTVLLVSHDrQFvdntvTECW----IFEGNGKI 516
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-237 |
4.71e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 23 AIDNISFKVDEGEFVGIMGPSGSGKTT-------LLNcistidhVTTGKI-----IINNSDI-TRLKsksldkfrkneLG 89
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLP-------ASEGEAwlfgqPVDAGDIaTRRR-----------VG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 90 FVFQDFNLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVLAD 169
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 170 EPTGSLDSkSAR-----LLLErfesLNKDLKATILMVTHdaFTASYAR--RILFINDGKIFI-----ELV--RGNDSRKE 235
Cdd:NF033858 423 EPTSGVDP-VARdmfwrLLIE----LSREDGVTIFISTH--FMNEAERcdRISLMHAGRVLAsdtpaALVaaRGAATLEE 495
|
..
gi 447167138 236 FF 237
Cdd:NF033858 496 AF 497
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-204 |
5.01e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIinnsditRLKSKSLDKFRKNEL-GFVFQDFNLLDTLTAY 104
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMAVFSQHHVdGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 105 ENIAlaltikgeasskiDGKIQAVAKYLDIEQVLSKYP-YQISGGQKQRVASARAIVTDPSLVLADEPTGSLDsksarll 183
Cdd:PLN03073 600 PGVP-------------EQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD------- 659
|
170 180
....*....|....*....|....
gi 447167138 184 LERFESLNKDL---KATILMVTHD 204
Cdd:PLN03073 660 LDAVEALIQGLvlfQGGVLMVSHD 683
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-223 |
5.63e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCIsTIDH-------VT-------TGKIIInnsDItrlksksldkfrKNELG 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHpqgysndLTlfgrrrgSGETIW---DI------------KKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 90 FVFQDFNL-LDTLTAYENIALaltikgeaSSKID--GKIQAVA--------KYLDI---EQVLSKYPYQ-ISGGQKQRVA 154
Cdd:PRK10938 340 YVSSSLHLdYRVSTSVRNVIL--------SGFFDsiGIYQAVSdrqqklaqQWLDIlgiDKRTADAPFHsLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447167138 155 SARAIVTDPSLVLADEPTGSLDSKSaRLLLERF-ESLNKDLKATILMVTHDAFTA--SYARRILFINDGKIF 223
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFvDVLISEGETQLLFVSHHAEDApaCITHRLEFVPDGDIY 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-208 |
9.94e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkSKSLDKFRKnELGFVFQDFNLLDTlTAYEN 106
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLRELRR-QFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 107 IALALtikgEASSK----------IDGKIQAVAKYLDiEQVL---SKYpyqiSGGQKQRVASARAIVTDPS-LVLADEPT 172
Cdd:PTZ00243 1404 VDPFL----EASSAevwaalelvgLRERVASESEGID-SRVLeggSNY----SVGQRQLMCMARALLKKGSgFILMDEAT 1474
|
170 180 190
....*....|....*....|....*....|....*.
gi 447167138 173 GSLDSksarlllerfeSLNKDLKATILmvthDAFTA 208
Cdd:PTZ00243 1475 ANIDP-----------ALDRQIQATVM----SAFSA 1495
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-203 |
1.47e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCIStiDH----VTTGKIIINNSDITrlkskSLDKFRKNELGfVFQD 94
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHpaykILEGDILFKGESIL-----DLEPEERAHLG-IFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 FNLLDTLTAYENI---ALALTIKGEASSK-----------IDGKIQAVakylDIEQV-LSKYPYQ-ISGGQKQRVASARA 158
Cdd:CHL00131 90 FQYPIEIPGVSNAdflRLAYNSKRKFQGLpeldplefleiINEKLKLV----GMDPSfLSRNVNEgFSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447167138 159 IVTDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTH 203
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-176 |
3.36e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCI--STIDHVTTGKIIINNSDITrlkSKSLDKFRKNELGFVFQD----- 94
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVD---VSTVSDAIDAGLAYVTEDrkgyg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 95 FNLLDTLTayENIALAlTIKGEASSKI--DGKIQAVA---------KYLDIEQVLSKypyqISGGQKQRVASARAIVTDP 163
Cdd:NF040905 351 LNLIDDIK--RNITLA-NLGKVSRRGVidENEEIKVAeeyrkkmniKTPSVFQKVGN----LSGGNQQKVVLSKWLFTDP 423
|
170
....*....|...
gi 447167138 164 SLVLADEPTGSLD 176
Cdd:NF040905 424 DVLILDEPTRGID 436
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-203 |
3.67e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 15 GNKDNVTKAIDNISFkvdeGEFVGIMGPSGSGKTTLL-------------NCisTIDHV--------TTGKIIINNSDIT 73
Cdd:PLN03073 188 GGRDLIVDASVTLAF----GRHYGLVGRNGTGKTTFLrymamhaidgipkNC--QILHVeqevvgddTTALQCVLNTDIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 74 RLKsksldkFRKNELGFVFQDFNL-LDTLTAYENIALALTIKGEASSK-----------IDGkIQAVAKYLDIEQVLSKY 141
Cdd:PLN03073 262 RTQ------LLEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQrleeiykrlelIDA-YTAEARAASILAGLSFT 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 142 P-------YQISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKsARLLLERFesLNKDLKaTILMVTH 203
Cdd:PLN03073 335 PemqvkatKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH-AVLWLETY--LLKWPK-TFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-223 |
6.22e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 24 IDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIIN--------NSDITRLKSKSLD-------KFRKNEL 88
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvNQETPALPQPALEyvidgdrEYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 89 GFVF----QDFNLLDTLTAYENIALALTIKGEASSKIDGkiqavakyLDIEQVLSKYPYQ-ISGGQKQRVASARAIVTDP 163
Cdd:PRK10636 97 QLHDanerNDGHAIATIHGKLDAIDAWTIRSRAASLLHG--------LGFSNEQLERPVSdFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 164 SLVLADEPTGSLDsKSARLLLERFEslnKDLKATILMVTHDA-FTASYARRILFINDGKIF 223
Cdd:PRK10636 169 DLLLLDEPTNHLD-LDAVIWLEKWL---KSYQGTLILISHDRdFLDPIVDKIIHIEQQSLF 225
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-221 |
6.69e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 6.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 145 ISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSaRLLLER-FESLNKDLKATILMVTHDAFTASYARRILFINDGK 221
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ-RLNAARaIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-225 |
2.27e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 2 RNILSVEKIEKYYGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSG--KTTLLNCISTIDHVTTGKIIINNSDITRLKSKS 79
Cdd:NF000106 11 RNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 80 LDKFRKNELGfvfqdfnLLDTLTAYENiaLALTIKGEASSKIDGKIQA--VAKYLDIEQVLSKYPYQISGGQKQRVASAR 157
Cdd:NF000106 87 IG*HRPVR*G-------RRESFSGREN--LYMIGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 158 AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNKDlKATILMVTHDAFTA-SYARRILFINDGKIFIE 225
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeQLAHELTVIDRGRVIAD 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-204 |
2.47e-05 |
|
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: 45.16 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 18 DNVTKAIDNISFKVD-----EGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinNSDIT------RLKSKSldkfrkn 86
Cdd:COG1245 345 PDLTKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKisykpqYISPDY------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 87 elgfvfqdfnlldTLTAYENIalaltiKGEASSKIDGKI--QAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPS 164
Cdd:COG1245 415 -------------DGTVEEFL------RSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447167138 165 LVLADEPTGSLDSkSARLLLERF-ESLNKDLKATILMVTHD 204
Cdd:COG1245 476 LYLLDEPSAHLDV-EQRLAVAKAiRRFAENRGKTAMVVDHD 515
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-204 |
2.90e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.14 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLN-----CISTIDHVTTGK----------------IIINNSDITRLK-------S 77
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQpgnhdrieglehidkvIVIDQSPIGRTPrsnpatyT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 78 KSLDKFRKnelgfVFQD------FN--LLDTLTAYENIA--LALTIKG-----EASSKIDGKIQAVAK----YLDIEQVL 138
Cdd:cd03271 93 GVFDEIRE-----LFCEvckgkrYNreTLEVRYKGKSIAdvLDMTVEEaleffENIPKIARKLQTLCDvglgYIKLGQPA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447167138 139 SkypyQISGGQKQRVASARAI---VTDPSLVLADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHD 204
Cdd:cd03271 168 T----TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHN 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-204 |
3.78e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 19 NVTKAIDNISFKVD-----EGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIiinNSDIT------RLKSKSldkfrkne 87
Cdd:PRK13409 345 DLTKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisykpqYIKPDY-------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 88 lgfvfqdfnlldTLTAYENIAlaltikgEASSKIDGKI--QAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSL 165
Cdd:PRK13409 414 ------------DGTVEDLLR-------SITDDLGSSYykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447167138 166 VLADEPTGSLDSkSARLLLERF-ESLNKDLKATILMVTHD 204
Cdd:PRK13409 475 YLLDEPSAHLDV-EQRLAVAKAiRRIAEEREATALVVDHD 513
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-172 |
1.01e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 14 YGNkdnvTKAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITrlkskslDKFRKNELG---- 89
Cdd:NF033858 11 YGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-------DARHRRAVCpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 90 FVFQDF--NLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQISGGQKQRVASARAIVTDPSLVL 167
Cdd:NF033858 80 YMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
....*
gi 447167138 168 ADEPT 172
Cdd:NF033858 160 LDEPT 164
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1-204 |
2.13e-04 |
|
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: 41.05 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 1 MRNILSVEKIEKyygnkdnvtkaidnISFkvDEGEFVgIMGPSGSGKTTLLNCIStidHVTTGKIIINNSDITRLKsksl 80
Cdd:cd03240 6 IRNIRSFHERSE--------------IEF--FSPLTL-IVGQNGAGKTTIIEALK---YALTGELPPNSKGGAHDP---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 81 DKFRKNE-LGFVFQDFNLL--DTLTAYENIAL---ALTIKGEASSKIdgkiqavakyldieqvLSKYPYQISGGQKQ--- 151
Cdd:cd03240 62 KLIREGEvRAQVKLAFENAngKKYTITRSLAIlenVIFCHQGESNWP----------------LLDMRGRCSGGEKVlas 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447167138 152 ---RVASARAIVTDPSLVLADEPTGSLDSKSARL-LLERFESLNKDLKATILMVTHD 204
Cdd:cd03240 126 liiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-221 |
4.66e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 22 KAIDNISFKVDEGEFVGIMGPSGSGKTTLLNCISTI-DHVT-TGKIIINNsDITRLKSksldkFRKNE-LGFVF--QDFN 96
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyPHGSyEGEILFDG-EVCRFKD-----IRDSEaLGIVIihQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 97 LLDTLTAYENIALAltikGEASSK--ID-GKIQAVAKYLdIEQV-LSKYPY----QISGGQKQRVASARAIVTDPSLVLA 168
Cdd:NF040905 89 LIPYLSIAENIFLG----NERAKRgvIDwNETNRRAREL-LAKVgLDESPDtlvtDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447167138 169 DEPTGSL-DSKSARLLlerfeSLNKDLKA---TILMVTHDAFTASY-ARRILFINDGK 221
Cdd:NF040905 164 DEPTAALnEEDSAALL-----DLLLELKAqgiTSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-222 |
9.35e-04 |
|
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: 40.17 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 27 ISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSDITRlksKSLDKFRKNelgF--VFQDFNLLDTLtay 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAYRQL---FsaVFSDFHLFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 105 enialaLTIKGEASskiDGKIQAVAKYLDIEQVLSkypYQ--------ISGGQKQRVASARAIVTD-PSLVLaDE----- 170
Cdd:COG4615 422 ------LGLDGEAD---PARARELLERLELDHKVS---VEdgrfsttdLSQGQRKRLALLVALLEDrPILVF-DEwaadq 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447167138 171 -PTgsldsksarlllerF-----ESLNKDLKA---TILMVTHD--AFtaSYARRILFINDGKI 222
Cdd:COG4615 489 dPE--------------FrrvfyTELLPELKArgkTVIAISHDdrYF--DLADRVLKMDYGKL 535
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-239 |
9.72e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 131 YLDIEQVLSKypyqISGGQKQRVASARAIVTDPSLV--LADEPTGSLDSKSARLLLERFESLnKDLKATILMVTHDAFTA 208
Cdd:PRK00635 467 YLTPERALAT----LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMI 541
|
90 100 110
....*....|....*....|....*....|..
gi 447167138 209 SYARRILFINDGK-IFIELVRGNDSRKEFFTK 239
Cdd:PRK00635 542 SLADRIIDIGPGAgIFGGEVLFNGSPREFLAK 573
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-205 |
9.89e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 39 IMGPSGSGKTTLLNCISTI---DHVTTGKI---IINNSD-----------------ITRLKSKSLDKFRKN--ELGFVFQ 93
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYAlygKARSRSKLrsdLINVGSeeasvelefehggkryrIERRQGEFAEFLEAKpsERKEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 94 DfnLLDTLTAYENIALALTIKGEASSKIDGKIQAVAKYLDIEQVLSKY--PYQISGGQKQRVASARAIvtdpSLVLaDep 171
Cdd:COG0419 108 R--LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLdpIETLSGGERLRLALADLL----SLIL-D-- 178
|
170 180 190
....*....|....*....|....*....|....
gi 447167138 172 TGSLDSKSARLLLERFESLNkdlkatilMVTHDA 205
Cdd:COG0419 179 FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-215 |
1.61e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 32 DEGEFVGIMGPSGSGKTTLLNCISTIdhvTTGKIiinnsdiTRLKSKSLDKFRKNElgfvfqdfnlldtltAYENIALAL 111
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIGLA---LGGAQ-------SATRRRSGVKAGCIV---------------AAVSAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 112 TIKgeasskidgkiqavakyldieqvlskypyQISGGQKQRVASARAI----VTDPSLVLADEPTGSLDSKSARLLLERF 187
Cdd:cd03227 74 TRL-----------------------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170 180
....*....|....*....|....*...
gi 447167138 188 ESLNkDLKATILMVTHDAFTASYARRIL 215
Cdd:cd03227 125 LEHL-VKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
144-204 |
1.64e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447167138 144 QISGGQKQRVASARAIVTDPSLVLADEPTGSLDSKSARLLlerfESLNKDLKATILMVTHD 204
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWL----EDVLNERNSTMIIISHD 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-222 |
2.38e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 26 NISFKVDEGEFVGIMGPSGSGKTTLLNCISTIDHVTTGKIIINNSditrlksksldkfrkneLGFVFQDFNLLDTlTAYE 105
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-----------------IAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 106 NIalaLTIKGEASSKIDGKIQAVAKYLDIEQVLSKYPYQI-------SGGQKQRVASARAIVTDPSLVLADEPTGSLDSK 178
Cdd:PTZ00243 740 NI---LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIgekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447167138 179 SARLLLErfESLNKDLKA-TILMVTHDAFTASYARRILFINDGKI 222
Cdd:PTZ00243 817 VGERVVE--ECFLGALAGkTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
82-204 |
6.34e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447167138 82 KFRKNELGFVFQDFNLLDTL--TAYENIALALTikgeaSSKIDGKIQAVA----KYLDIEQVLskypYQISGGQKQRVAS 155
Cdd:PRK00635 750 RFLPQVLEVRYKGKNIADILemTAYEAEKFFLD-----EPSIHEKIHALCslglDYLPLGRPL----SSLSGGEIQRLKL 820
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 447167138 156 AR---AIVTDPSLVLADEPTGSLDSKSARLLLERFESLNkDLKATILMVTHD 204
Cdd:PRK00635 821 AYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHN 871
|
|
| |
