|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-160 |
2.04e-36 |
|
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: 133.04 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPELESKA-KASAA 78
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEiIEAAR 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--TVVLI 156
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIII 666
|
....
gi 2163878594 157 AHNL 160
Cdd:COG2274 667 AHRL 670
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-176 |
6.85e-33 |
|
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: 122.56 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAA 78
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQNPYLFAGTIRENLRLGRPDAsDEELEAALE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLI 156
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILI 528
|
170 180
....*....|....*....|
gi 2163878594 157 AHNLtkEERDLFDREVALRA 176
Cdd:COG4988 529 THRL--ALLAQADRILVLDD 546
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-160 |
4.30e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.27 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDP-----ELESKAKA 75
Cdd:COG1132 373 GPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslRRQIGVVPQDTFLFSGTIRENIRYGRPdatdeEVEEAAKA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SaadaQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKqT 152
Cdd:COG1132 453 A----QAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIqeaLERLMKGR-T 527
|
....*...
gi 2163878594 153 VVLIAHNL 160
Cdd:COG1132 528 TIVIAHRL 535
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-176 |
8.62e-32 |
|
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: 119.49 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAA 78
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlRRRIAVVPQRPHLFDTTLRENLRLARPDAtDEELWAALE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--TVVLI 156
Cdd:COG4987 447 RVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLI 526
|
170 180
....*....|....*....|
gi 2163878594 157 AHNLTkeERDLFDREVALRA 176
Cdd:COG4987 527 THRLA--GLERMDRILVLED 544
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-161 |
1.67e-30 |
|
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: 109.01 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNItmfdpeleskakasaad 79
Cdd:cd03228 34 VGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLFSGTIRENI----------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 aqlseavdswpqgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--TVVLIA 157
Cdd:cd03228 97 ------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVIVIA 152
|
....
gi 2163878594 158 HNLT 161
Cdd:cd03228 153 HRLS 156
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-170 |
8.65e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 8.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRTKIGYLPQQAVL---LPSSVMNNITM-FDPELeskAKASAA 78
Cdd:COG1121 39 GPNGAGKSTLLKAILGLLPPTSGTVRLF---GKPPRRARRRIGYVPQRAEVdwdFPITVRDVVLMgRYGRR---GLFRRP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQS 149
Cdd:COG1121 113 SRADREAVDEA---LER-VGLEDladrpiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALyelLRELRRE 188
|
170 180
....*....|....*....|.
gi 2163878594 150 KQTVVLIAHNLTkEERDLFDR 170
Cdd:COG1121 189 GKTILVVTHDLG-AVREYFDR 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-158 |
1.25e-28 |
|
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: 105.36 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPELESKA-KASAAD 79
Cdd:cd03245 37 GRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERiLRAAEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK--QTVVLIA 157
Cdd:cd03245 117 AGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIIT 196
|
.
gi 2163878594 158 H 158
Cdd:cd03245 197 H 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-161 |
7.22e-28 |
|
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: 103.85 E-value: 7.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAAD 79
Cdd:cd03253 34 GPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVVPQDTVLFNDTIGYNIRYGRPDAtDEEVIEAAKA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQSKQTVVLIA 157
Cdd:cd03253 114 AQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALrdVSKGRTTIVIA 193
|
....
gi 2163878594 158 HNLT 161
Cdd:cd03253 194 HRLS 197
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-161 |
1.64e-27 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 102.69 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKV--KPDRTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAAD 79
Cdd:cd03254 36 GPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKqTVVLI 156
Cdd:cd03254 116 AGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIqeaLEKLMKGR-TSIII 194
|
....*
gi 2163878594 157 AHNLT 161
Cdd:cd03254 195 AHRLS 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-174 |
2.25e-27 |
|
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: 106.99 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAA 78
Cdd:TIGR02857 354 VGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAGTIAENIRLARPDAsDAEIREALE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKqTVVL 155
Cdd:TIGR02857 434 RAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDaetEAEVLEALRALAQGR-TVLL 512
|
170
....*....|....*....
gi 2163878594 156 IAHNLtkEERDLFDREVAL 174
Cdd:TIGR02857 513 VTHRL--ALAALADRIVVL 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-174 |
2.47e-27 |
|
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: 101.84 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRTKIGYLPQQAVL---LPSSVMNNITM-FDPELESKAKASAA 78
Cdd:cd03235 32 GPNGAGKSTLLKAILGLLKPTSGSIRVF---GKPLEKERKRIGYVPQRRSIdrdFPISVRDVVLMgLYGHKGLFRRLSKA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DaqlSEAVDswpQGLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ- 151
Cdd:cd03235 109 D---KAKVD---EALER-VGLSEladrqiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRe 181
|
170 180
....*....|....*....|....*
gi 2163878594 152 --TVVLIAHNLTKEErDLFDREVAL 174
Cdd:cd03235 182 gmTILVVTHDLGLVL-EYFDRVLLL 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-165 |
2.91e-25 |
|
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: 101.35 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPE--LESKAKAS 76
Cdd:TIGR01193 505 IVGMSGSGKSTLAKLLVGFFQARSGEILLngFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEnvSQDEIWAA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK-QTVVL 155
Cdd:TIGR01193 585 CEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIF 664
|
170
....*....|
gi 2163878594 156 IAHNLTKEER 165
Cdd:TIGR01193 665 VAHRLSVAKQ 674
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-160 |
5.76e-25 |
|
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: 96.00 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRTKIGYLPQQAVLLP-SSVMNNItMFDPELeskakASAADAQ 81
Cdd:cd03293 37 GPSGCGKSTLLRIIAGLERPTSGEVLVD---GEPVTGPGPDRGYVFQQDALLPwLTVLDNV-ALGLEL-----QGVPKAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID----QAAGRKILDKLLQSKQ 151
Cdd:cd03293 108 ARERAEEL---LEL-VGLSGfenaypHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGK 183
|
....*....
gi 2163878594 152 TVVLIAHNL 160
Cdd:cd03293 184 TVLLVTHDI 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-161 |
8.13e-25 |
|
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: 96.07 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:cd03249 36 GSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 -QLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID-------QAAgrkiLDKLLQSKqT 152
Cdd:cd03249 116 aNIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaeseklvQEA----LDRAMKGR-T 190
|
....*....
gi 2163878594 153 VVLIAHNLT 161
Cdd:cd03249 191 TIVIAHRLS 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-160 |
2.61e-24 |
|
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: 93.69 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkpdRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADAQ 81
Cdd:cd03250 37 VGPVGSGKSSLLSALLGELEKLSGSVSV-----------PGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK----QTVVLIA 157
Cdd:cd03250 106 LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLllnnKTRILVT 185
|
...
gi 2163878594 158 HNL 160
Cdd:cd03250 186 HQL 188
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-161 |
3.41e-24 |
|
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: 94.22 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAAD 79
Cdd:cd03251 35 GPSGSGKSTLVNLIPRFYDVDSGRILIdgHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGAtREEVEEAARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKqTVVLI 156
Cdd:cd03251 115 ANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVqaaLERLMKNR-TTFVI 193
|
....*
gi 2163878594 157 AHNLT 161
Cdd:cd03251 194 AHRLS 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
3-132 |
1.59e-23 |
|
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: 90.40 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA--GKKVKPDRTKIGYLPQQAVLLP-SSVMNNItmFDPELESKAKASAAD 79
Cdd:pfam00005 18 GPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPrLTVRENL--RLGLLLKGLSKREKD 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 80 AQLSEAVDSWPQG--LETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTS 132
Cdd:pfam00005 96 ARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-160 |
3.21e-23 |
|
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: 91.40 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGAngtGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNItmfDPELE---SKAKAS 76
Cdd:cd03244 39 TGS---GKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlRSRISIIPQDPVLFSGTIRSNL---DPFGEysdEELWQA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILdKLLQSK---QTV 153
Cdd:cd03244 113 LERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQ-KTIREAfkdCTV 191
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:cd03244 192 LTIAHRL 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-176 |
2.86e-22 |
|
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: 88.69 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-RTKIGYLPQQAVLLPS-SVMNNITMFdpelESKAKASAAD 79
Cdd:COG4133 34 TGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGHADGLKPElTVRENLRFW----AALYGLRADR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLL----QSKQTVVL 155
Cdd:COG4133 110 EAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD-AAGVALLAELIaahlARGGAVLL 186
|
170 180
....*....|....*....|.
gi 2163878594 156 IAHNltkEERDLFDREVALRA 176
Cdd:COG4133 187 TTHQ---PLELAAARVLDLGD 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-158 |
3.17e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 92.41 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF---------FDQAGKKvkpdrtkIGYLPQQAVLLPSSVMNNITMFDPELESKA 73
Cdd:TIGR01842 351 GPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdRETFGKH-------IGYLPQDVELFPGTVAENIARFGENADPEK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 K-ASAADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQ---AAGRKILDKLLQS 149
Cdd:TIGR01842 424 IiEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEegeQALANAIKALKAR 503
|
....*....
gi 2163878594 150 KQTVVLIAH 158
Cdd:TIGR01842 504 GITVVVITH 512
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-175 |
3.81e-22 |
|
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: 88.70 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD------RTKIGYLPQQAVLLPS-SVMNNITMfdPELESKAK 74
Cdd:cd03255 36 VGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafrRRHIGFVFQSFNLLPDlTALENVEL--PLLLAGVP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSwpqgletpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL- 147
Cdd:cd03255 114 KKERRERAEELLER--------VGLGDrlnhypSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRe 185
|
170 180 190
....*....|....*....|....*....|.
gi 2163878594 148 ---QSKQTVVLIAHNLTKEERdlFDREVALR 175
Cdd:cd03255 186 lnkEAGTTIVVVTHDPELAEY--ADRIIELR 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-160 |
6.13e-22 |
|
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: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAA 78
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevRRRVSVCAQDAHLFDTTVRENLRLARPDAtDEELWAALE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLI 156
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAalSGRTVVLI 526
|
....
gi 2163878594 157 AHNL 160
Cdd:TIGR02868 527 THHL 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-170 |
8.02e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.20 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD----RTKIGYLPQQAVLLPS-SVMNNITMF-----DPELESK 72
Cdd:COG1131 33 GPNGAGKTTTIRMLLGLLRPTSGEVRVL---GEDVARDpaevRRRIGYVPQEPALYPDlTVRENLRFFarlygLPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASaadaQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ- 151
Cdd:COG1131 110 ERID----ELLELF-----GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAe 180
|
170 180
....*....|....*....|..
gi 2163878594 152 --TVVLIAHNLtkEE-RDLFDR 170
Cdd:COG1131 181 gkTVLLSTHYL--EEaERLCDR 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-176 |
9.52e-22 |
|
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: 86.47 E-value: 9.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ----AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITMfdpeleskakasa 77
Cdd:cd03229 33 GPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdLEDELPPLRRRIGMVFQDFALFPHlTVLENIAL------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 adaqlseavdswpqgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TV 153
Cdd:cd03229 100 -------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTV 154
|
170 180
....*....|....*....|...
gi 2163878594 154 VLIAHNLTKEERdLFDREVALRA 176
Cdd:cd03229 155 VLVTHDLDEAAR-LADRVVVLRD 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-170 |
1.54e-21 |
|
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: 85.91 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNItmfdpeleskakasaada 80
Cdd:cd03230 33 GPNGAGKTTLIKIILGLLKPDSGEIKVLGKdIKKEPEEVKRRIGYLPEEPSLYENlTVRENL------------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 qlseavdswpqgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ---TVVLIA 157
Cdd:cd03230 95 ----------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSS 152
|
170
....*....|...
gi 2163878594 158 HNLTkEERDLFDR 170
Cdd:cd03230 153 HILE-EAERLCDR 164
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-175 |
1.81e-21 |
|
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: 85.37 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQqavllpssvmnnitmfdpeleskakasaad 79
Cdd:cd00267 31 VGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelRRRIGYVPQ------------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 aqlseavdswpqgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSKQTVVLI 156
Cdd:cd00267 81 ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEllrELAEEGRTVIIV 136
|
170
....*....|....*....
gi 2163878594 157 AHNLtKEERDLFDREVALR 175
Cdd:cd00267 137 THDP-ELAELAADRVIVLK 154
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-160 |
2.32e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.22 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGqisffdqagkKVKPDRTkIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADAQL 82
Cdd:PTZ00243 693 GATGSGKSTLLQSLLSQFEISEG----------RVWAERS-IAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQL 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 83 SEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK---QTVVLIAHN 159
Cdd:PTZ00243 762 EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGAlagKTRVLATHQ 841
|
.
gi 2163878594 160 L 160
Cdd:PTZ00243 842 V 842
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-176 |
6.82e-21 |
|
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: 85.04 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQ----AGKKV--KPDRTKIGYLPQQAVLLPS-SVMNNIT-----MFDPE 68
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKInlPPQQRKIGLVFQQYALFPHlNVRENLAfglkrKRNRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 69 LESKAKASAADAQLSEAVDSWPQGLetpvdlagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgRKILDKLLQ 148
Cdd:cd03297 108 DRISVDELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRAL-RLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|...
gi 2163878594 149 S-----KQTVVLIAHNLTKEERdLFDREVALRA 176
Cdd:cd03297 176 QikknlNIPVIFVTHDLSEAEY-LADRIVVMED 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-161 |
8.08e-21 |
|
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: 85.62 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAAda 80
Cdd:cd03252 35 GRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAA-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVD---SWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQSKQTVVL 155
Cdd:cd03252 113 KLAGAHDfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMhdICAGRTVII 192
|
....*.
gi 2163878594 156 IAHNLT 161
Cdd:cd03252 193 IAHRLS 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-160 |
1.19e-20 |
|
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: 84.92 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-----VGEAAASGGQISFFDQAGKKVKPD----RTKIGYLPQQAVLLPSSVMNNITM--------F 65
Cdd:cd03260 33 GPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDvlelRRRVGMVFQKPNPFPGSIYDNVAYglrlhgikL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 66 DPELESKAKASAADAQLSEAVDSwpqgletpvDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDK 145
Cdd:cd03260 113 KEELDERVEEALRKAALWDEVKD---------RLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEEL 183
|
170
....*....|....*..
gi 2163878594 146 LLQSKQ--TVVLIAHNL 160
Cdd:cd03260 184 IAELKKeyTIVIVTHNM 200
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-170 |
1.63e-20 |
|
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: 84.06 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQavllPSS--VMNNIT---MFDPELESKAK 74
Cdd:cd03225 33 VGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQN----PDDqfFGPTVEeevAFGLENLGLPE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAAD--AQLSEAVDSWPQgLETPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQS 149
Cdd:cd03225 109 EEIEErvEEALELVGLEGL-RDRSPF----TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRellELLKKLKAE 183
|
170 180
....*....|....*....|.
gi 2163878594 150 KQTVVLIAHNLtKEERDLFDR 170
Cdd:cd03225 184 GKTIIIVTHDL-DLLLELADR 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-158 |
2.19e-20 |
|
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: 87.11 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDR--TKIGYLPQQAVLLPSSVMNNITMF---DPEleskakASA 77
Cdd:COG4618 365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDGTIAENIARFgdaDPE------KVV 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLS---EAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--- 151
Cdd:COG4618 439 AAAKLAgvhEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArga 518
|
....*..
gi 2163878594 152 TVVLIAH 158
Cdd:COG4618 519 TVVVITH 525
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-160 |
7.71e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRTKIGYLPQQAVLLP-SSVMNNItMFDPELESKAKASAADA- 80
Cdd:COG1116 44 GPSGCGKSTLLRLIAGLEKPTSGEVLVD---GKPVTGPGPDRGVVFQEPALLPwLTVLDNV-ALGLELRGVPKAERRERa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 -------QLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLL-----Q 148
Cdd:COG1116 120 rellelvGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALD-ALTRERLQDELlrlwqE 187
|
170
....*....|..
gi 2163878594 149 SKQTVVLIAHNL 160
Cdd:COG1116 188 TGKTVLFVTHDV 199
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-159 |
8.02e-20 |
|
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: 81.49 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNItmfdpeleskakasaad 79
Cdd:cd03246 34 IGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelGDHVGYLPQDDELFSGSIAENI----------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 aqlseavdswpqgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK---QTVVLI 156
Cdd:cd03246 97 ------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVI 152
|
...
gi 2163878594 157 AHN 159
Cdd:cd03246 153 AHR 155
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-175 |
3.02e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD------RTKIGYLPQQAVLLPS-SVMNNITMfdPELESKAK 74
Cdd:COG1136 40 VGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlrRRHIGFVFQFFNLLPElTALENVAL--PLLLAGVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSwpqgletpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL- 147
Cdd:COG1136 118 RKERRERARELLER--------VGLGDrldhrpSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRe 189
|
170 180 190
....*....|....*....|....*....|.
gi 2163878594 148 ---QSKQTVVLIAHNLTKEERdlFDREVALR 175
Cdd:COG1136 190 lnrELGTTIVMVTHDPELAAR--ADRVIRLR 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-160 |
3.44e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.87 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-----RTKIGYLPQQAVLLPS-SVMNNItMFdPeLESKAKA 75
Cdd:COG2884 34 TGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipylRRRIGVVFQDFRLLPDrTVYENV-AL-P-LRVTGKS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSWpqgletpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--L 147
Cdd:COG2884 111 RKEIRRRVREVLDL-------VGLSDkakalpHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLeeI 183
|
170
....*....|....
gi 2163878594 148 QSKQTVVLIA-HNL 160
Cdd:COG2884 184 NRRGTTVLIAtHDL 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-176 |
3.84e-19 |
|
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: 81.08 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA-----GKKVKPDRTKIGYLPQQAVLLP-SSVMNNI-------------- 62
Cdd:cd03256 34 GPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkGKALRQLRRQIGMIFQQFNLIErLSVLENVlsgrlgrrstwrsl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 63 -TMFDPEleskakASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK 141
Cdd:cd03256 114 fGLFPKE------EKQRALAALERV-----GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2163878594 142 ILDKLLQSKQ----TVVLIAHNLtKEERDLFDREVALRA 176
Cdd:cd03256 183 VMDLLKRINReegiTVIVSLHQV-DLAREYADRIVGLKD 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-161 |
3.93e-19 |
|
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: 80.64 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNI-------TMFDPELESKAK 74
Cdd:cd03259 33 GPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYALFPHlTVAENIafglklrGVPKAEIRARVR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQSKQ- 151
Cdd:cd03259 113 ELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELkeLQRELg 181
|
170
....*....|.
gi 2163878594 152 -TVVLIAHNLT 161
Cdd:cd03259 182 iTTIYVTHDQE 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-160 |
6.00e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 82.95 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKASAAD 79
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLFNDTIAYNIAYGRPDAsEEEVEAAARA 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQSKQTVVLIA 157
Cdd:COG5265 471 AQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALreVARGRTTLVIA 550
|
...
gi 2163878594 158 HNL 160
Cdd:COG5265 551 HRL 553
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-165 |
2.59e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.31 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKV--KPDRTKIGYLPQQAVLLPSSVMNNITM---FDPELESKAKAsa 77
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhHYLHRQVALVGQEPVLFSGSVRENIAYgltDTPDEEIMAAA-- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 adaQLSEAVD---SWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQTVV 154
Cdd:TIGR00958 592 ---KAANAHDfimEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVL 668
|
170
....*....|.
gi 2163878594 155 LIAHNLTKEER 165
Cdd:TIGR00958 669 LIAHRLSTVER 679
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-158 |
2.71e-18 |
|
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: 78.78 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF-----FDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNItMFDPELESKAKAS 76
Cdd:cd03258 38 GRSGAGKSTLIRCINGLERPTSGSVLVdgtdlTLLSGKELRKARRRIGMIFQHFNLLSSrTVFENV-ALPLEIAGVPKAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AAD--AQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--- 151
Cdd:cd03258 117 IEErvLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelg 191
|
....*...
gi 2163878594 152 -TVVLIAH 158
Cdd:cd03258 192 lTIVLITH 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-165 |
3.95e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.28 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQIsFFDqaGKKV-----KPDRTKIGYLPQQAVLLPSSVMNNIT--MFDPELESKA 73
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQGGQV-LLD--GKPIsqyehKYLHSKVSLVGQEPVLFARSLQDNIAygLQSCSFECVK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLSeAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQ 151
Cdd:cd03248 122 EAAQKAHAHS-FISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwpERR 200
|
170
....*....|....
gi 2163878594 152 TVVLIAHNLTKEER 165
Cdd:cd03248 201 TVLVIAHRLSTVER 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-160 |
4.34e-18 |
|
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: 77.09 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKP-DRTK-IGYLPQqavllpssVMNNItmfdpeleskakasaada 80
Cdd:cd03214 32 GPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkELARkIAYVPQ--------ALELL------------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 qlseavdswpqGLEtpvDLAG---DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKQ-TV 153
Cdd:cd03214 86 -----------GLA---HLADrpfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahQIELLELLRRLARERGkTV 151
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:cd03214 152 VMVLHDL 158
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-161 |
1.32e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAA 78
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID----QAAGRKIldKLLQSKQTVV 154
Cdd:PRK10790 452 TVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDsgteQAIQQAL--AAVREHTTLV 529
|
....*..
gi 2163878594 155 LIAHNLT 161
Cdd:PRK10790 530 VIAHRLS 536
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-160 |
2.05e-17 |
|
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: 75.91 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNItmfDPELESKAKASAADA 80
Cdd:cd03369 41 GRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdlRSSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAvdswpqgletpvdlaGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgrkilDKLLQ-------SKQTV 153
Cdd:cd03369 118 RVSEG---------------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-----DALIQktireefTNSTI 177
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:cd03369 178 LTIAHRL 184
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-160 |
2.09e-17 |
|
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: 76.00 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTK----IGYLPQQAVLLPS-SVMNNITMFD-----PELESK 72
Cdd:cd03263 35 GHNGAGKTTTLKMLTGELRPTSGTAYI---NGYSIRTDRKAarqsLGYCPQFDALFDElTVREHLRFYArlkglPKSEIK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASAADAQLseavdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ- 151
Cdd:cd03263 112 EEVELLLRVL---------GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKg 182
|
170
....*....|
gi 2163878594 152 -TVVLIAHNL 160
Cdd:cd03263 183 rSIILTTHSM 192
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-170 |
2.38e-17 |
|
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: 76.22 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQ--AGKKVKPDRTKIGYLPQ----QavLLPSSVMNNItMFDPE---LESK 72
Cdd:COG1122 33 IGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKdiTKKNLRELRRKVGLVFQnpddQ--LFAPTVEEDV-AFGPEnlgLPRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 akasaadaQLSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KIL 143
Cdd:COG1122 110 --------EIRERVEEA---LEL-VGLEHladrppHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRellELL 177
|
170 180
....*....|....*....|....*...
gi 2163878594 144 DKLLQSKQTVVLIAHNLtkEE-RDLFDR 170
Cdd:COG1122 178 KRLNKEGKTVIIVTHDL--DLvAELADR 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-166 |
3.86e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITmFDPELESKAKASAADA 80
Cdd:PRK11176 376 GRSGSGKSTIANLLTRFYDIDEGEILLdgHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA-YARTEQYSREQIEEAA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVD---SWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKlLQSKQTVV 154
Cdd:PRK11176 455 RMAYAMDfinKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDE-LQKNRTSL 533
|
170
....*....|...
gi 2163878594 155 LIAHNL-TKEERD 166
Cdd:PRK11176 534 VIAHRLsTIEKAD 546
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-160 |
5.84e-17 |
|
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: 75.23 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-----AGKKVKPDRTKIGYLPQQavllPSSVMN----------------N 61
Cdd:cd03257 38 GESGSGKSTLARAILGLLKPTSGSIIFDGKdllklSRRLRKIRRKEIQMVFQD----PMSSLNprmtigeqiaeplrihG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 62 ITMFDPELESKAKASAADAQLSEAV-DSWPQGLetpvdlagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR 140
Cdd:cd03257 114 KLSKKEARKEAVLLLLVGVGLPEEVlNRYPHEL-----------SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
170 180
....*....|....*....|....
gi 2163878594 141 KILDKLLQSKQ----TVVLIAHNL 160
Cdd:cd03257 183 QILDLLKKLQEelglTLLFITHDL 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-160 |
7.18e-17 |
|
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: 74.85 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-----AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNI--------TMFDPE 68
Cdd:cd03261 33 GPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglSEAELYRLRRRMGMLFQSGALFDSlTVFENVafplrehtRLSEEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 69 LESKAKASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ 148
Cdd:cd03261 113 IREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRS 181
|
170
....*....|....*.
gi 2163878594 149 SKQ----TVVLIAHNL 160
Cdd:cd03261 182 LKKelglTSIMVTHDL 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-161 |
7.19e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPE-LESKAKASAAD 79
Cdd:PRK10789 348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSDTVANNIALGRPDaTQQEIEHVARL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLIA 157
Cdd:PRK10789 428 ASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQwgEGRTVIISA 507
|
....
gi 2163878594 158 HNLT 161
Cdd:PRK10789 508 HRLS 511
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-160 |
7.42e-17 |
|
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: 75.08 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKP-DR-TKIGYLPQQAVL-LPSSV-----------MNNITMFDPE 68
Cdd:COG1120 34 GPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELaRRIAYVPQEPPApFGLTVrelvalgryphLGLFGRPSAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 69 LEskakasaadaqlsEAVDswpQGLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAG 139
Cdd:COG1120 114 DR-------------EAVE---EALER-TGLEHladrpvDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahQLEV 176
|
170 180
....*....|....*....|..
gi 2163878594 140 RKILDKLLQSKQ-TVVLIAHNL 160
Cdd:COG1120 177 LELLRRLARERGrTVVMVLHDL 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-158 |
1.11e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISffdqagkkvKPDRTKIGYLPQQAVLLPS-SVMNNITMFDPEL-----------E 70
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDSGEVS---------IPKGLRIGYLPQEPPLDDDlTVLDTVLDGDAELraleaeleeleA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 71 SKAKASAADAQLS------EAVDSW----------------PQGLETPVdlagDNLSGGQKQKVVLARAEVRDSQLLLVD 128
Cdd:COG0488 102 KLAEPDEDLERLAelqeefEALGGWeaearaeeilsglgfpEEDLDRPV----SELSGGWRRRVALARALLSEPDLLLLD 177
|
170 180 190
....*....|....*....|....*....|.
gi 2163878594 129 EGTSAIDqAAGRKILDKLLQS-KQTVVLIAH 158
Cdd:COG0488 178 EPTNHLD-LESIEWLEEFLKNyPGTVLVVSH 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-160 |
4.34e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASG-----GQ-ISFFDQAGKkvkpdRTKIGYLPQQAVLLPSSVMNNITMFDPEL-ESKAKA 75
Cdd:PRK11174 383 GPSGAGKTSLLNALLGFLPYQGslkinGIeLRELDPESW-----RKHLSWVGQNPQLPHGTLRDNVLLGNPDAsDEQLQQ 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTV 153
Cdd:PRK11174 458 ALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTT 537
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:PRK11174 538 LMVTHQL 544
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-161 |
5.20e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.98 E-value: 5.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkpdRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:TIGR00957 669 VVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK-----QTVVL 155
Cdd:TIGR00957 738 ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlknKTRIL 817
|
....*.
gi 2163878594 156 IAHNLT 161
Cdd:TIGR00957 818 VTHGIS 823
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-175 |
7.36e-16 |
|
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: 72.06 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQA-----GKKVKPDRTKIGYLPQQAVLLPS-SVMNNItMFDPELeSKAK 74
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAIPYLRRKIGVVFQDFRLLPDrNVYENV-AFALEV-TGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--- 151
Cdd:cd03292 110 PREIRKRVPAALEL--VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagt 187
|
170 180
....*....|....*....|....*...
gi 2163878594 152 TVVLIAHNltkeeRDLFD----REVALR 175
Cdd:cd03292 188 TVVVATHA-----KELVDttrhRVIALE 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1-160 |
1.10e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 71.59 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISF------FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAK 74
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAI-----DQAAGRKILDKLLQS 149
Cdd:cd03290 112 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALdihlsDHLMQEGILKFLQDD 191
|
170
....*....|.
gi 2163878594 150 KQTVVLIAHNL 160
Cdd:cd03290 192 KRTLVLVTHKL 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-175 |
1.28e-15 |
|
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: 73.40 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVG---EAAASGGQISFFDQAGKKVKPD--RTKIGYLPQ--QAVLLPSSVMNNItMFDPELESKAKA 75
Cdd:COG1123 39 GESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAlrGRRIGMVFQdpMTQLNPVTVGDQI-AEALENLGLSRA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAAD--AQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ-- 151
Cdd:COG1123 118 EARArvLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRer 192
|
170 180
....*....|....*....|....*.
gi 2163878594 152 --TVVLIAHNLTkEERDLFDREVALR 175
Cdd:COG1123 193 gtTVLLITHDLG-VVAEIADRVVVMD 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-160 |
1.52e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.44 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKST----LFKLLvgEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKAS 76
Cdd:TIGR00957 1317 IVGRTGAGKSSltlgLFRIN--ESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWA 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgrkilDKLLQSKQ----- 151
Cdd:TIGR00957 1395 LELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET-----DNLIQSTIrtqfe 1469
|
170
....*....|.
gi 2163878594 152 --TVVLIAHNL 160
Cdd:TIGR00957 1470 dcTVLTIAHRL 1480
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-162 |
2.13e-15 |
|
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: 70.93 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD---RTKIGYLPQQAVLLPS-SVMNNITMfdpeLESKAKASAA 78
Cdd:cd03224 33 GRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraRAGIGYVPEGRRIFPElTVEENLLL----GAYARRRAKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGT-----SAIDQAAgrKILDKLLQSKQTV 153
Cdd:cd03224 109 KARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSeglapKIVEEIF--EAIRELRDEGVTI 185
|
....*....
gi 2163878594 154 VLIAHNLTK 162
Cdd:cd03224 186 LLVEQNARF 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-160 |
2.14e-15 |
|
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: 70.36 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKP-DRTK-IGYLPQ--QAVLLPSSVMNNITMFDPELESKAKASA 77
Cdd:cd03226 32 TGKNGAGKTTLAKILAGLIKESSGSILL---NGKPIKAkERRKsIGYVMQdvDYQLFTDSVREELLLGLKELDAGNEQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQ---LSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID----QAAGRKILDKLLQSK 150
Cdd:cd03226 109 TVLKdldLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknmERVGELIRELAAQGK 177
|
170
....*....|
gi 2163878594 151 qTVVLIAHNL 160
Cdd:cd03226 178 -AVIVITHDY 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-175 |
2.87e-15 |
|
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: 70.25 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ----AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT--------MFDPEL 69
Cdd:cd03262 33 GPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltdDKKNINELRQKVGMVFQQFNLFPHlTVLENITlapikvkgMSKAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KL 146
Cdd:cd03262 113 EERALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDvmkDL 181
|
170 180
....*....|....*....|....*....
gi 2163878594 147 LQSKQTVVLIAHNLTkeerdlFDREVALR 175
Cdd:cd03262 182 AEEGMTMVVVTHEMG------FAREVADR 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-161 |
3.82e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPE-LESKAKASAAD 79
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIdgTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAER 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQTVVlI 156
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVkaaLDELMKGRTTFI-I 526
|
....*
gi 2163878594 157 AHNLT 161
Cdd:PRK13657 527 AHRLS 531
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-176 |
4.25e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFD-QAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITMFDPELeskakaSAADA 80
Cdd:PRK13536 74 GPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGVVPQFDNLDLEfTVRENLLVFGRYF------GMSTR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWPQ--GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQTVVL 155
Cdd:PRK13536 148 EIEAVIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIwerLRSLLARGKTILL 227
|
170 180
....*....|....*....|.
gi 2163878594 156 IAHNLTKEERdLFDREVALRA 176
Cdd:PRK13536 228 TTHFMEEAER-LCDRLCVLEA 247
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-158 |
6.68e-15 |
|
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: 69.14 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-AGKKVKPDRTKIGYLPQQAVLLPS----------SVMNNITmfDPELES 71
Cdd:cd03264 32 GPNGAGKTTLMRILATLTPPSSGTIRIDGQdVLKQPQKLRRRIGYLPQEFGVYPNftvrefldyiAWLKGIP--SKEVKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 KAKASAADAQLSEAVDSWPQGletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQA---AGRKILDKLLQ 148
Cdd:cd03264 110 RVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEeriRFRNLLSELGE 178
|
170
....*....|
gi 2163878594 149 SKqTVVLIAH 158
Cdd:cd03264 179 DR-IVILSTH 187
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-175 |
1.81e-14 |
|
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: 67.07 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRtkigylPQQAVLLPssvmnnITMFdpeleskakasaadaql 82
Cdd:cd03216 33 GENGAGKSTLMKILSGLYKPDSGEILV---DGKEVSFAS------PRDARRAG------IAMV----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 83 seavdswPQgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSKQTVVLIAHN 159
Cdd:cd03216 81 -------YQ------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVErlfKVIRRLRAQGVAVIFISHR 141
|
170
....*....|....*.
gi 2163878594 160 LtKEERDLFDREVALR 175
Cdd:cd03216 142 L-DEVFEIADRVTVLR 156
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-170 |
1.93e-14 |
|
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: 67.34 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-RTKIGYLPQQAVLLPSSVMNNItmfdpeleskakasaadaq 81
Cdd:cd03247 35 GRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAlSSLISVLNQRPYLFDTTLRNNL------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 lseavdswpqgletpvdlaGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLIAHN 159
Cdd:cd03247 96 -------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvlKDKTLIWITHH 156
|
170
....*....|.
gi 2163878594 160 LTKEERdlFDR 170
Cdd:cd03247 157 LTGIEH--MDK 165
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-160 |
3.91e-14 |
|
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: 67.91 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA--GKKVKPDRTKIGYLPQQavllPSSVMN---NI--TMFDP-ELESKAK 74
Cdd:COG1124 38 GESGSGKSTLLRALAGLERPWSGEVTFDGRPvtRRRRKAFRRRVQMVFQD----PYASLHprhTVdrILAEPlRIHGLPD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVdswpqGLetPVDLAG---DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAagrKILDKLLQ 148
Cdd:COG1124 114 REERIAELLEQV-----GL--PPSFLDrypHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvQA---EILNLLKD 183
|
170
....*....|....*.
gi 2163878594 149 SKQ----TVVLIAHNL 160
Cdd:COG1124 184 LREerglTYLFVSHDL 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-155 |
4.31e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 68.34 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISffdQAGKkvkpdrtkIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:cd03291 68 ITGSTGSGKTSLLMLILGELEPSEGKIK---HSGR--------ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKAC 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 81 QLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD----KLLQSKQTVVL 155
Cdd:cd03291 137 QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscvcKLMANKTRILV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-176 |
5.66e-14 |
|
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: 66.92 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKP-DRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKAsaadaQ 81
Cdd:cd03269 33 GPNGAGKTTTIRMILGIILPDSGEVLFD---GKPLDIaARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKE-----E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ---T 152
Cdd:cd03269 105 ARRRIDEW---LER-LELSEyankrvEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkT 180
|
170 180
....*....|....*....|....
gi 2163878594 153 VVLIAHNLTKEERdLFDREVALRA 176
Cdd:cd03269 181 VILSTHQMELVEE-LCDRVLLLNK 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-161 |
7.35e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDR--TKIGYLPQQAVL-LPSSVMNNITMfdpELESKAKASAAD 79
Cdd:COG4559 34 GPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLaFPFTVEEVVAL---GRAPHGSSAAQD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVdswpqgLETpVDLAG------DNLSGGQKQKVVLARA-------EVRDSQLLLVDEGTSAID---QAAGRKIL 143
Cdd:COG4559 111 RQIVREA------LAL-VGLAHlagrsyQTLSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTSALDlahQHAVLRLA 183
|
170 180
....*....|....*....|
gi 2163878594 144 DKLLQSKQTVVLIAH--NLT 161
Cdd:COG4559 184 RQLARRGGGVVAVLHdlNLA 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-156 |
9.33e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTK------IGYLP----QQAVLLPSSVMNNITMfdPELE 70
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRL---DGKPVRIRSPRdairagIAYVPedrkGEGLVLDLSIRENITL--ASLD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 71 SKAKASA-ADAQLSEAVDSW-------PQGLETPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR-- 140
Cdd:COG1129 358 RLSRGGLlDRRRERALAEEYikrlrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAei 433
|
170
....*....|....*..
gi 2163878594 141 -KILDKLLQSKQTVVLI 156
Cdd:COG1129 434 yRLIRELAAEGKAVIVI 450
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-160 |
9.63e-14 |
|
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: 66.69 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTK---IGYLPQQAVLLPS-SVMNNITM----FDPELESKAK 74
Cdd:cd03219 33 GPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRTFQIPRLFPElTVLENVMVaaqaRTGSGLLLAR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDE---GTSAIDQAAGRKILDK 145
Cdd:cd03219 113 ARREEREARERAEEL---LER-VGLADladrpaGELSYGQQRRLEIARALATDPKLLLLDEpaaGLNPEETEELAELIRE 188
|
170
....*....|....*
gi 2163878594 146 LLQSKQTVVLIAHNL 160
Cdd:cd03219 189 LRERGITVLLVEHDM 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-160 |
1.17e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITM-FDPELESKAKASAADA 80
Cdd:PRK10771 32 GPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLgLNPGLKLNAAQREKLH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKIL---DKLLQSKQ-TVVLI 156
Cdd:PRK10771 112 AIARQM-----GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLtlvSQVCQERQlTLLMV 186
|
....
gi 2163878594 157 AHNL 160
Cdd:PRK10771 187 SHSL 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-160 |
1.56e-13 |
|
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: 67.24 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-----AGKKVKPDRTKIGYLPQQavllPSSvmnnitMFDP------ELES 71
Cdd:COG1123 298 GESGSGKSTLARLLLGLLRPTSGSILFDGKdltklSRRSLRELRRRVQMVFQD----PYS------SLNPrmtvgdIIAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 --KAKASAADAQLSEAVDSWpqgLETpVDLAGD-------NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI 142
Cdd:COG1123 368 plRLHGLLSRAERRERVAEL---LER-VGLPPDladryphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI 443
|
170 180
....*....|....*....|..
gi 2163878594 143 LDKL--LQSKQ--TVVLIAHNL 160
Cdd:COG1123 444 LNLLrdLQRELglTYLFISHDL 465
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-160 |
2.02e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAA 78
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIddCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAagrkiLDKLLQ-------SKQ 151
Cdd:PLN03232 1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR-----TDSLIQrtireefKSC 1421
|
....*....
gi 2163878594 152 TVVLIAHNL 160
Cdd:PLN03232 1422 TMLVIAHRL 1430
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-158 |
3.03e-13 |
|
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: 65.70 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNItmfDPE---LESKAKASA 77
Cdd:cd03288 54 GRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEckcTDDRLWEAL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgRKILDKLLQS---KQTVV 154
Cdd:cd03288 131 EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVVMTafaDRTVV 209
|
....
gi 2163878594 155 LIAH 158
Cdd:cd03288 210 TIAH 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-158 |
3.88e-13 |
|
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: 64.58 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT-------MFDPELESKAK 74
Cdd:cd03301 33 GPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHmTVYDNIAfglklrkVPKDEIDERVR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQS-K 150
Cdd:cd03301 113 EVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklRVQMRAELKRLQQRlG 181
|
....*...
gi 2163878594 151 QTVVLIAH 158
Cdd:cd03301 182 TTTIYVTH 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-160 |
4.04e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.34 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTL---FKLLV----GEAAASGGQISFFDqagkkVKPDRTKIGYLPQQAVLLPSSVMNNItmfDPELESKAKA 75
Cdd:PTZ00243 1343 GRTGSGKSTLlltFMRMVevcgGEIRVNGREIGAYG-----LRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAE 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQL---SEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEV-RDSQLLLVDEGTSAIDQAAGRKILDKLLQ--S 149
Cdd:PTZ00243 1415 VWAALELvglRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSafS 1494
|
170
....*....|.
gi 2163878594 150 KQTVVLIAHNL 160
Cdd:PTZ00243 1495 AYTVITIAHRL 1505
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-170 |
4.45e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPEleskakasAADA 80
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVVSQRVHLFSATLRDNLLLAAPN--------ASDE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVD--------SWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ- 151
Cdd:PRK11160 445 ALIEVLQqvglekllEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQn 524
|
170 180
....*....|....*....|
gi 2163878594 152 -TVVLIAHNLTKEERdlFDR 170
Cdd:PRK11160 525 kTVLMITHRLTGLEQ--FDR 542
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-160 |
4.59e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGE-AAASGGQISFfdqagkkvkpdRTKIGYLPQQAVLLPSSVMNNITM---FDPElesKAKASAA 78
Cdd:PLN03130 650 GSTGEGKTSLISAMLGElPPRSDASVVI-----------RGTVAYVPQVSWIFNATVRDNILFgspFDPE---RYERAID 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ---SKQTVVL 155
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKdelRGKTRVL 795
|
....*
gi 2163878594 156 IAHNL 160
Cdd:PLN03130 796 VTNQL 800
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-174 |
6.69e-13 |
|
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: 64.05 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITM-FDPELESKAkasaada 80
Cdd:cd03298 31 GPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHlTVEQNVGLgLSPGLKLTA------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDswpqGLETPVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL----QSK 150
Cdd:cd03298 104 EDRQAIE----VALARVGLAGlekrlpGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlhaETK 179
|
170 180
....*....|....*....|....
gi 2163878594 151 QTVVLIAHNLTKEERdLFDREVAL 174
Cdd:cd03298 180 MTVLMVTHQPEDAKR-LAQRVVFL 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-155 |
7.05e-13 |
|
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: 65.70 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISffdQAGKkvkpdrtkIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:TIGR01271 457 VAGSTGSGKSSLLMMIMGELEPSEGKIK---HSGR--------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKAC 525
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 81 QLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD----KLLQSKQTVVL 155
Cdd:TIGR01271 526 QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEsclcKLMSNKTRILV 604
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-175 |
7.20e-13 |
|
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: 64.28 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNI-------TMFDPELESKAK 74
Cdd:cd03299 32 GPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHmTVYKNIayglkkrKVDKKEIERKVL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL----QSK 150
Cdd:cd03299 112 EIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFG 180
|
170 180
....*....|....*....|....*
gi 2163878594 151 QTVVLIAHNLTkEERDLFDREVALR 175
Cdd:cd03299 181 VTVLHVTHDFE-EAWALADKVAIML 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-170 |
1.17e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.24 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD-----RTKIGYLPQ----QAVllPSSVMNNIT------MFDP 67
Cdd:PRK13632 42 GHNGSGKSTISKILTGLLKPQSGEIKID---GITISKEnlkeiRKKIGIIFQnpdnQFI--GATVEDDIAfglenkKVPP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 -ELESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL 146
Cdd:PRK13632 117 kKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIM 185
|
170 180
....*....|....*....|....*...
gi 2163878594 147 L----QSKQTVVLIAHNLtkEERDLFDR 170
Cdd:PRK13632 186 VdlrkTRKKTLISITHDM--DEAILADK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-160 |
1.62e-12 |
|
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: 63.82 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD------RTKIGYLPQQAVLLPS-SVMNNITmFDPEL--ESKA 73
Cdd:cd03294 57 GLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrRKKISMVFQSFALLPHrTVLENVA-FGLEVqgVPRA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ----S 149
Cdd:cd03294 136 EREERAAEALELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqaeL 210
|
170
....*....|.
gi 2163878594 150 KQTVVLIAHNL 160
Cdd:cd03294 211 QKTIVFITHDL 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-160 |
1.67e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.24 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITM-FDPELESKAKASAADA 80
Cdd:COG3840 32 GPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHlTVAQNIGLgLRPGLKLTAEQRAQVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSKQ-TVVLI 156
Cdd:COG3840 112 QALERV-----GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDlvdELCRERGlTVLMV 186
|
....
gi 2163878594 157 AHNL 160
Cdd:COG3840 187 THDP 190
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-160 |
1.73e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKL------LVGEAAASGgQISFFDQ--AGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITmFDPELesk 72
Cdd:COG1117 44 GPSGCGKSTLLRClnrmndLIPGARVEG-EILLDGEdiYDPDVDVVelRRRVGMVFQKPNPFPKSIYDNVA-YGLRL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 aKASAADAQLSEAVDS-------WPQ---GLETPvdlaGDNLSGGQKQKVVLARA-----EVrdsqlLLVDEGTSAIDQA 137
Cdd:COG1117 119 -HGIKSKSELDEIVEEslrkaalWDEvkdRLKKS----ALGLSGGQQQRLCIARAlavepEV-----LLMDEPTSALDPI 188
|
170 180
....*....|....*....|....*
gi 2163878594 138 AGRKILDKLLQSKQ--TVVLIAHNL 160
Cdd:COG1117 189 STAKIEELILELKKdyTIVIVTHNM 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-165 |
1.74e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgRKILDKLL-----QSKQTVVLI 156
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEKTIvdikdKADKTIITI 1415
|
....*....
gi 2163878594 157 AHNLTKEER 165
Cdd:PTZ00265 1416 AHRIASIKR 1424
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-156 |
1.94e-12 |
|
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: 62.06 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRT------KIGYLP----QQAVLLPSSVMNNITMfdpeles 71
Cdd:cd03215 32 AGLVGNGQTELAEALFGLRPPASGEITL---DGKPVTRRSPrdairaGIAYVPedrkREGLVLDLSVAENIAL------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 kakasaadaqlseavdswpqgletpvdlaGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ 151
Cdd:cd03215 102 -----------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
....*...
gi 2163878594 152 ---TVVLI 156
Cdd:cd03215 153 agkAVLLI 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-165 |
1.97e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASG-----GQISFFDQAgkkVKPDRTKIGYLPQQAV-------LLPSSVMNNITM---- 64
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQN---IYERRVNLNRLRRQVSmvhpkpnLFPMSVYDNVAYgvki 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 65 --FDPELESKAKASAADaqlsEAVDSWPQgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK- 141
Cdd:PRK14258 115 vgWRPKLEIDDIVESAL----KDADLWDE-IKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKv 189
|
170 180
....*....|....*....|....*..
gi 2163878594 142 ---ILDKLLQSKQTVVLIAHNLTKEER 165
Cdd:PRK14258 190 eslIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-160 |
2.00e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIdgCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERA 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgrkilDKLLQS-------KQTV 153
Cdd:PLN03130 1352 HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQKtireefkSCTM 1426
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:PLN03130 1427 LIIAHRL 1433
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-158 |
3.49e-12 |
|
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: 60.54 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISffdqagkkvKPDRTKIGYLPQqavllpssvmnnitmfdpeleskakasaadaq 81
Cdd:cd03221 32 VGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVKIGYFEQ-------------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163878594 82 lseavdswpqgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQTVVLIAH 158
Cdd:cd03221 71 ----------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSH 125
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-164 |
4.14e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.86 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-AGKKVKPDRTKIGYLPQQAVLLP-SSVMNNItMFDPEleskaKASAADA 80
Cdd:COG1118 35 GPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRERRVGFVFQHYALFPhMTVAENI-AFGLR-----VRPPSKA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLL-----QS 149
Cdd:COG1118 109 EIRARVEEL---LEL-VQLEGladrypSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVRKELRRWLrrlhdEL 183
|
170
....*....|....*
gi 2163878594 150 KQTVVLIAHNLtkEE 164
Cdd:COG1118 184 GGTTVFVTHDQ--EE 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-165 |
4.30e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA-GKKVKPDRTKIGYLPQQAVLLPS-SVMNNITMFDPELeskakaSAADA 80
Cdd:PRK13537 40 GPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSRARHARQRVGVVPQFDNLDPDfTVRENLLVFGRYF------GLSAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWPQ--GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQTVVL 155
Cdd:PRK13537 114 AARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMwerLRSLLARGKTILL 193
|
170
....*....|
gi 2163878594 156 IAHNLTKEER 165
Cdd:PRK13537 194 TTHFMEEAER 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-158 |
4.71e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-VGEAAASGgQIS----FFDQAG----KKVKPDRTKIGYLPQQAVLLPS-SVMNNIT--------M 64
Cdd:PRK11124 35 GPSGAGKSSLLRVLnLLEMPRSG-TLNiagnHFDFSKtpsdKAIRELRRNVGMVFQQYNLWPHlTVQQNLIeapcrvlgL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 65 FDPELESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRK 141
Cdd:PRK11124 114 SKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVS 182
|
170
....*....|....*..
gi 2163878594 142 ILDKLLQSKQTVVLIAH 158
Cdd:PRK11124 183 IIRELAETGITQVIVTH 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-176 |
6.00e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQ--AGKKVKPDRTKIGYLPQQavlLPSSVmnniTMFDPELEskakasaa 78
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplESWSSKAFARKVAYLPQQ---LPAAE----GMTVRELV-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 daqlseAVDSWP-------------QGLETPVDLAG---------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQ 136
Cdd:PRK10575 107 ------AIGRYPwhgalgrfgaadrEKVEEAISLVGlkplahrlvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2163878594 137 AAGRKILdKLLQ--SKQ---TVVLIAHNLTKEERdLFDREVALRA 176
Cdd:PRK10575 181 AHQVDVL-ALVHrlSQErglTVIAVLHDINMAAR-YCDYLVALRG 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
3-144 |
8.49e-12 |
|
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: 62.04 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF-----FD-QAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNitmfdpeLE---SK 72
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLggevlQDsARGIFLPPHRRRIGYVFQEARLFPHlSVRGN-------LLygrKR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163878594 73 AKASAADAQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD 144
Cdd:COG4148 105 APRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-160 |
8.87e-12 |
|
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: 61.15 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ-----AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNItMFdPELESKAKAS 76
Cdd:COG1127 38 GGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglSEKELYELRRRIGMLFQGGALFDSlTVFENV-AF-PLREHTDLSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVdswpqgLETpVDLAGDN------LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKIlDKLLQS- 149
Cdd:COG1127 116 AEIRELVLEK------LEL-VGLPGAAdkmpseLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVI-DELIREl 187
|
170
....*....|....*
gi 2163878594 150 ----KQTVVLIAHNL 160
Cdd:COG1127 188 rdelGLTSVVVTHDL 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-160 |
9.19e-12 |
|
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: 61.16 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPS-SVMNNITMFdPELE--SKAKASA 77
Cdd:cd03295 34 GPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelRRKIGYVIQQIGLFPHmTVEENIALV-PKLLkwPKEKIRE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLSEAVDSWPQGLetpVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TV 153
Cdd:cd03295 113 RADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelgkTI 189
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:cd03295 190 VFVTHDI 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-158 |
1.04e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqaGKKVkpdrtKIGYLPQ-QAVLLPS-SVMNNITMFDPELEskakaSAADA 80
Cdd:COG0488 348 GPNGAGKSTLLKLLAGELEPDSGTVKL----GETV-----KIGYFDQhQEELDPDkTVLDELRDGAPGGT-----EQEVR 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 81 QLSEAVDSWPQGLETPVdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgRKILDKLLQS-KQTVVLIAH 158
Cdd:COG0488 414 GYLGRFLFSGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEALEEALDDfPGTVLLVSH 487
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-161 |
1.16e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsffdQAGKKVKPD-RTKIGYLPQQAVLLP-SSVMNNITmfdpeLESKAKASAADA 80
Cdd:PRK11247 45 GRSGCGKSTLLRLLAGLETPSAGEL----LAGTAPLAEaREDTRLMFQDARLLPwKKVIDNVG-----LGLKGQWRDAAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVdswpqGLEtpvDLAGD---NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQS--KQ---T 152
Cdd:PRK11247 116 QALAAV-----GLA---DRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALD-ALTRIEMQDLIESlwQQhgfT 186
|
....*....
gi 2163878594 153 VVLIAHNLT 161
Cdd:PRK11247 187 VLLVTHDVS 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-164 |
1.24e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDR--TKIGYLPQQAVL-LPSSVMNNITM-FDPELESKAKASAA 78
Cdd:PRK13548 35 GPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFPFTVEEVVAMgRAPHGLSRAEDDAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWpqgletpvDLAGDN---LSGGQKQKVVLARA------EVRDSQLLLVDEGTSAIDqaagrkildklLQS 149
Cdd:PRK13548 115 VAAALAQVDLA--------HLAGRDypqLSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSALD-----------LAH 175
|
170
....*....|....*
gi 2163878594 150 KQTVVLIAHNLTKEE 164
Cdd:PRK13548 176 QHHVLRLARQLAHER 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-172 |
2.07e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.87 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQ-AVLLPSSVMNNI----TMFdP--------EL 69
Cdd:PRK10851 35 GPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHyALFRHMTVFDNIafglTVL-PrrerpnaaAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQS 149
Cdd:PRK10851 114 KAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGALD-AQVRKELRRWLRQ 181
|
170 180
....*....|....*....|....*...
gi 2163878594 150 -----KQTVVLIAHNlTKEERDLFDREV 172
Cdd:PRK10851 182 lheelKFTSVFVTHD-QEEAMEVADRVV 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-158 |
2.11e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.09 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISffdqagkkvKPDRTKIGYLPQQAVLLPSSvmnnitmfdpeleskakasaada 80
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIG---------MPEGEDLLFLPQRPYLPLGT----------------------- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 81 qLSEAVD-SWpqgletpvdlaGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQTVVLIAH 158
Cdd:cd03223 80 -LREQLIyPW-----------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-170 |
2.77e-11 |
|
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: 59.86 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD---RTKIGYLPQQAVLLPS-SVMNNITMFdpeLESKAKASAA 78
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkraRLGIGYLPQEASIFRKlTVEENILAV---LEIRGLSKKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSwPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI--LDKLLQSKQTVVLI 156
Cdd:cd03218 110 REEKLEELLE-EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIqkIIKILKDRGIGVLI 188
|
170
....*....|....*
gi 2163878594 157 A-HNLtKEERDLFDR 170
Cdd:cd03218 189 TdHNV-RETLSITDR 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-174 |
3.02e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPD----RTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAA 78
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLV---GGKDIETNldavRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSwpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLI 156
Cdd:TIGR01257 1040 LEMEAMLEDT---GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKyrSGRTIIMS 1116
|
170
....*....|....*...
gi 2163878594 157 AHNLtkEERDLFDREVAL 174
Cdd:TIGR01257 1117 THHM--DEADLLGDRIAI 1132
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-135 |
8.76e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 59.34 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNItMFDPELESKAKAsaadaQ 81
Cdd:COG3842 38 GPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHlTVAENV-AFGLRMRGVPKA-----E 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:COG3842 112 IRARVAEL---LEL-VGLEGladrypHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-165 |
1.05e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-----RTKIGYLPQ-QAVLLPSSVMNNITMfdPELESKAK 74
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflRRQIGMIFQdHHLLMDRTVYDNVAI--PLIIAGAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKIL---DKLLQSKQ 151
Cdd:PRK10908 111 GDDIRRRVSAALDK--VGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILrlfEEFNRVGV 188
|
170
....*....|....
gi 2163878594 152 TVVLIAHNLTKEER 165
Cdd:PRK10908 189 TVLMATHDIGLISR 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-176 |
1.21e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkPDRTKIGYLPQ----------QAVLLPSSVmnniTMFDPEles 71
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrpylplgtlrEALLYPATA----EAFSDA--- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 kakasaadaQLSEA-----VDSWPQGLETPVDLaGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL 146
Cdd:COG4178 459 ---------ELREAleavgLGHLAERLDEEADW-DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL 528
|
170 180 190
....*....|....*....|....*....|..
gi 2163878594 147 LQSKQ--TVVLIAHNLTKEerDLFDREVALRA 176
Cdd:COG4178 529 REELPgtTVISVGHRSTLA--AFHDRVLELTG 558
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
3-174 |
1.25e-10 |
|
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: 57.86 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGylpQQAVLLP-SSVMNNI---------TMFDPELESK 72
Cdd:TIGR01184 18 GHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---QNYSLLPwLTVRENIalavdrvlpDLSKSERRAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ---- 148
Cdd:TIGR01184 95 VEEHIALVGLTEAADKRP-----------GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQiwee 163
|
170 180
....*....|....*....|....*.
gi 2163878594 149 SKQTVVLIAHNLtKEERDLFDREVAL 174
Cdd:TIGR01184 164 HRVTVLMVTHDV-DEALLLSDRVVML 188
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
103-158 |
1.60e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.27 E-value: 1.60e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDkLLQSKQ-----TVVLIAH 158
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-LLKDINrelglTIVLITH 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-176 |
2.24e-10 |
|
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: 57.44 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQ--------AGKKVKPDRtkIGYLPQQAVLLPS-SVMNNITMfdP-ELES 71
Cdd:COG4181 44 VGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedARARLRARH--VGFVFQSFQLLPTlTALENVML--PlELAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 KAKASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDkLL---- 147
Cdd:COG4181 120 RRDARARARALLERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID-LLfeln 193
|
170 180 190
....*....|....*....|....*....|
gi 2163878594 148 -QSKQTVVLIAHNLTKEERdlFDREVALRA 176
Cdd:COG4181 194 rERGTTLVLVTHDPALAAR--CDRVLRLRA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-175 |
2.54e-10 |
|
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: 57.35 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNI---------TMFDPELESK 72
Cdd:cd03296 35 GPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHmTVFDNVafglrvkprSERPPEAEIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASA--ADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQSK 150
Cdd:cd03296 115 AKVHEllKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALD-AKVRKELRRWLRRL 182
|
170 180 190
....*....|....*....|....*....|
gi 2163878594 151 Q-----TVVLIAHNlTKEERDLFDREVALR 175
Cdd:cd03296 183 HdelhvTTVFVTHD-QEEALEVADRVVVMN 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-135 |
2.77e-10 |
|
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: 56.86 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT-------MFDPELESKAK 74
Cdd:cd03300 33 GPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHlTVFENIAfglrlkkLPKAEIKERVA 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 75 ASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:cd03300 113 EALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-162 |
2.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA--GKKVKPDRTKIGYLPQQAvllPSSVMNNITMFD------------PE 68
Cdd:PRK13648 42 GHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitDDNFEKLRKHIGIVFQNP---DNQFVGSIVKYDvafglenhavpyDE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 69 LESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ 148
Cdd:PRK13648 119 MHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
170
....*....|....*...
gi 2163878594 149 SKQ----TVVLIAHNLTK 162
Cdd:PRK13648 188 VKSehniTIISITHDLSE 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
97-158 |
3.10e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 3.10e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163878594 97 VDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TVVLIAH 158
Cdd:COG1135 128 VGLSDkadaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelglTIVLITH 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-165 |
3.78e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQI--------SFFDQAGKKVKpdRTKIGYLPQQAVLLPSSVMNNITMFDPELesk 72
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVR--RKKIAMVFQSFALMPHMTVLDNTAFGMEL--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 aKASAADAQLSEAVDSWPQ-GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQS 149
Cdd:PRK10070 134 -AGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvkLQA 212
|
170
....*....|....*...
gi 2163878594 150 K--QTVVLIAHNLTKEER 165
Cdd:PRK10070 213 KhqRTIVFISHDLDEAMR 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-170 |
4.03e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfDQAGKKVKP----DRTKIGYLPQQAVLLPS-SVMNNItMFDPELESKAKA 75
Cdd:PRK10895 34 LLGPNGAGKTTTFYMVVGIVPRDAGNIII-DDEDISLLPlharARRGIGYLPQEASIFRRlSVYDNL-MAVLQIRDDLSA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAG---RKILDKLLQSKQT 152
Cdd:PRK10895 112 EQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLG 189
|
170
....*....|....*...
gi 2163878594 153 VVLIAHNLtKEERDLFDR 170
Cdd:PRK10895 190 VLITDHNV-RETLAVCER 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-164 |
4.09e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT-------MFDPELESKAK 74
Cdd:PRK11607 52 GASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHmTVEQNIAfglkqdkLPKAEIASRVN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK----ILDKLLQSK 150
Cdd:PRK11607 132 EMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRmqleVVDILERVG 200
|
170
....*....|....
gi 2163878594 151 QTVVLIAHNltKEE 164
Cdd:PRK11607 201 VTCVMVTHD--QEE 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-175 |
5.14e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.36 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ------AGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITMfdPELESKAKA 75
Cdd:PRK11629 42 GSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklsSAAKAELRNQKLGFIYQFHHLLPDfTALENVAM--PLLIGKKKP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQT 152
Cdd:PRK11629 120 AEINSRALEMLAA--VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRLQGT 197
|
170 180
....*....|....*....|....
gi 2163878594 153 VVL-IAHNLTKEERdlFDREVALR 175
Cdd:PRK11629 198 AFLvVTHDLQLAKR--MSRQLEMR 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-160 |
7.09e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEaaasggqISFFDQAGKKVkpdRTKIGYLPQQAVLLPSSVMNNItMFDPELESKAK-ASAAD 79
Cdd:PLN03232 648 IVGGTGEGKTSLISAMLGE-------LSHAETSSVVI---RGSVAYVPQVSWIFNATVRENI-LFGSDFESERYwRAIDV 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK---QTVVLI 156
Cdd:PLN03232 717 TALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElkgKTRVLV 796
|
....
gi 2163878594 157 AHNL 160
Cdd:PLN03232 797 TNQL 800
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-160 |
7.33e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.25 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTKIGYLPQQAVLLP-SSVMNNITMfdpELESKAKASAADAQ 81
Cdd:PRK11248 34 GPSGCGKTTLLNLIAGFVPYQHGSITL---DGKPVEGPGAERGVVFQNEGLLPwRNVQDNVAF---GLQLAGVEKMQRLE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSeavdswpQGLETPVDLAGD------NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLL-----QSK 150
Cdd:PRK11248 108 IA-------HQMLKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTREQMQTLLlklwqETG 179
|
170
....*....|
gi 2163878594 151 QTVVLIAHNL 160
Cdd:PRK11248 180 KQVLLITHDI 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-175 |
1.10e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRT-KIG-YL-PQQAVLLPS-SVMNNITMFDP-ELESKAKASA 77
Cdd:PRK15439 44 GGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhQLGiYLvPQEPLLFPNlSVKENILFGLPkRQASMQKMKQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLSEAVDswpqgletpVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQTVV 154
Cdd:PRK15439 124 LLAALGCQLD---------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIV 194
|
170 180
....*....|....*....|.
gi 2163878594 155 LIAHNLtKEERDLFDREVALR 175
Cdd:PRK15439 195 FISHKL-PEIRQLADRISVMR 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-174 |
1.54e-09 |
|
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: 54.68 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDqAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITMFdpelesKAKASAAD 79
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPDAGFATVdgFD-VVKEPAEARRRLGFVSDSTGLYDRlTARENLEYF------AGLYGLKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVDSWPQ--GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK---QTVV 154
Cdd:cd03266 111 DELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCIL 190
|
170 180
....*....|....*....|
gi 2163878594 155 LIAHNLTKEERdLFDREVAL 174
Cdd:cd03266 191 FSTHIMQEVER-LCDRVVVL 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-138 |
2.00e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.49 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPdRTKIGYLPQQAVLLPS-SVMNNITMFdpelesKAKASAADA 80
Cdd:PRK13539 34 TGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-AEACHYLGHRNAMKPAlTVAENLEFW------AAFLGGEEL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163878594 81 QLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAA 138
Cdd:PRK13539 107 DIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-161 |
2.16e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKK---VKPDRTKIGYLPQQAVLLPSSVMNNI-----TMFDPE-LESKA 73
Cdd:PTZ00265 418 GESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinLKWWRSKIGVVSQDPLLFSNSIKNNIkyslySLKDLEaLSNYY 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQL----------------------------------------SEAVD------------SWPQGLETPVDLAG 101
Cdd:PTZ00265 498 NEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDvskkvlihdfvsALPDKYETLVGSNA 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163878594 102 DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAG---RKILDKLLQSKQTV-VLIAHNLT 161
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRItIIIAHRLS 641
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-159 |
2.52e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD------RTKIGYLPQQAVLLPS-SVMNNItmfdpELESKAKA 75
Cdd:PRK10535 41 GASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlrREHFGFIFQRYHLLSHlTAAQNV-----EVPAVYAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSWPQ-GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK---ILDKLLQSKQ 151
Cdd:PRK10535 116 LERKQRLLRAQELLQRlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEvmaILHQLRDRGH 195
|
....*...
gi 2163878594 152 TVVLIAHN 159
Cdd:PRK10535 196 TVIIVTHD 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-160 |
2.82e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKpDRTKIGYLPQQ-------AVLLPSSVM-------------- 59
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQSeevdwsfPVLVEDVVMmgryghmgwlrrak 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 60 -NNITMFDPELESKAKASAADAQLSEavdswpqgletpvdlagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAA 138
Cdd:PRK15056 117 kRDRQIVTAALARVDMVEFRHRQIGE-------------------LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*
gi 2163878594 139 GRKILDKLLQSK---QTVVLIAHNL 160
Cdd:PRK15056 178 EARIISLLRELRdegKTMLVSTHNL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-175 |
2.86e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTK------IGYLPQQAVLLPS-SVMNNITMFDPELESKAKA 75
Cdd:COG1129 37 GENGAGKSTLMKILSGVYQPDSGEILL---DGEPVRFRSPRdaqaagIAIIHQELNLVPNlSVAENIFLGREPRRGGLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAV-DSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQA-AGR--KILDKLLQSKQ 151
Cdd:COG1129 114 WRAMRRRARELlARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERlfRIIRRLKAQGV 191
|
170 180
....*....|....*....|....*
gi 2163878594 152 TVVLIAHNLtkEE-RDLFDREVALR 175
Cdd:COG1129 192 AIIYISHRL--DEvFEIADRVTVLR 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-165 |
3.32e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.40 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-----VGEAAASGGQISFFDQA--GKKVKPD--RTKIGYLPQQAVLLPSSVMNNITmFDPELESKA 73
Cdd:PRK14243 43 GPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNlyAPDVDPVevRRRIGMVFQKPNPFPKSIYDNIA-YGARINGYK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQ--LSEAVdSWPQgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI--LDKLLQS 149
Cdd:PRK14243 122 GDMDELVErsLRQAA-LWDE-VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIeeLMHELKE 199
|
170
....*....|....*.
gi 2163878594 150 KQTVVLIAHNLTKEER 165
Cdd:PRK14243 200 QYTIIIVTHNMQQAAR 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-158 |
4.83e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGG--------QISFFDQAGKKVKPDRTkigylpqqavllpssVMNNITMFDPELESKAK 74
Cdd:PRK11147 352 GPNGCGKTTLLKLMLGQLQADSGrihcgtklEVAYFDQHRAELDPEKT---------------VMDNLAEGKQEVMVNGR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAVDSwPQGLETPVDLagdnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQSKQ-TV 153
Cdd:PRK11147 417 PRHVLGYLQDFLFH-PKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD-VETLELLEELLDSYQgTV 490
|
....*
gi 2163878594 154 VLIAH 158
Cdd:PRK11147 491 LLVSH 495
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-160 |
4.90e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsffdqagkkVKPDRTKIGYLPQQAVL---LPSSVmNNITMFDPELESKAKASAAD 79
Cdd:PRK09544 37 GPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQKLYLdttLPLTV-NRFLRLRPGTKKEDILPALK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVdswpqgLETPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKQTVVL- 155
Cdd:PRK09544 107 RVQAGHL------IDAPMQ----KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVALYDLIDQLRRELDCAVLm 176
|
....*
gi 2163878594 156 IAHNL 160
Cdd:PRK09544 177 VSHDL 181
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-165 |
6.01e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVL--LPSSV-------------MNNITMFDP 67
Cdd:PRK10419 45 GRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFqdSISAVnprktvreiirepLRHLLSLDK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 EleskaKASAADAQLSEAVDSWPQGLetpvDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILD 144
Cdd:PRK10419 125 A-----ERLARASEMLRAVDLDDSVL----DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLK 195
|
170 180
....*....|....*....|..
gi 2163878594 145 KLLQSKQTV-VLIAHNLTKEER 165
Cdd:PRK10419 196 KLQQQFGTAcLFITHDLRLVER 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-164 |
6.56e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTKI----GYLPQqavllpSSVMNNITMFDPELESKAKAS 76
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATV---AGKSILTNISDVhqnmGYCPQ------FDAIDDLLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSW---PQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSK 150
Cdd:TIGR01257 2041 GVPAEEIEKVANWsiqSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtivSIIREG 2120
|
170
....*....|....
gi 2163878594 151 QTVVLIAHNLTKEE 164
Cdd:TIGR01257 2121 RAVVLTSHSMEECE 2134
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
3-160 |
7.07e-09 |
|
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: 53.52 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQ----------ISFFdqAG-------KKVKPDRTKIGYLPQQAVLLPSSVMNNItmf 65
Cdd:cd03236 33 GPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEF--RGselqnyfTKLLEGDVKVIVKPQYVDLIPKAVKGKV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 66 dpelESKAKASAADAQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID-----QAAgr 140
Cdd:cd03236 108 ----GELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqrlNAA-- 179
|
170 180
....*....|....*....|
gi 2163878594 141 KILDKLLQSKQTVVLIAHNL 160
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHDL 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-159 |
7.30e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-----RTK-IGYLPQQAVLLPS-SVMNNITMfdPEL---E 70
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklRAKhVGFVFQSFMLIPTlNALENVEL--PALlrgE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 71 SKAKASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK 150
Cdd:PRK10584 119 SSRQSRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
|
170
....*....|...
gi 2163878594 151 Q----TVVLIAHN 159
Cdd:PRK10584 194 RehgtTLILVTHD 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-135 |
7.61e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.54 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT-------MFDPELEskak 74
Cdd:COG3839 36 GPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQSYALYPHmTVYENIAfplklrkVPKAEID---- 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163878594 75 asaadaqlsEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:COG3839 112 ---------RRVREA---AEL-LGLEDlldrkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-165 |
7.72e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-----VGEAAASGGQISFfdqAGKKVKPDRT-------KIGYLPQQAVLLPSSVMNNItMFDPELE 70
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmndLNPEVTITGSIVY---NGHNIYSPRTdtvdlrkEIGMVFQQPNPFPMSIYENV-VYGLRLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 71 SKAKASAadaqLSEAVDSWPQGL---ETPVDLAGDN---LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD 144
Cdd:PRK14239 114 GIKDKQV----LDEAVEKSLKGAsiwDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEE 189
|
170 180
....*....|....*....|...
gi 2163878594 145 KL--LQSKQTVVLIAHNLTKEER 165
Cdd:PRK14239 190 TLlgLKDDYTMLLVTRSMQQASR 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
104-160 |
8.21e-09 |
|
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: 53.52 E-value: 8.21e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAagrKILDKL--LQSKQ--TVVLIAHNL 160
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiQA---QILNLLkdLQRELglAILFITHDL 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-129 |
9.09e-09 |
|
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: 52.68 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD---RTKIGYLPQQAVLLPS-SVMNNITMFdpeLESKAKASAA 78
Cdd:COG0410 36 GRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriaRLGIGYVPEGRRIFPSlTVEENLLLG---AYARRDRAEV 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 79 DAQLSEAVDSWPQgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDE 129
Cdd:COG0410 113 RADLERVYELFPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-164 |
1.03e-08 |
|
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: 52.78 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEA-AASGGQISFFDQagKKVKPD----RTKIGYL-P--QQAVLLPSSVMN--------NITMFD 66
Cdd:COG1119 36 GPNGAGKSTLLSLITGDLpPTYGNDVRLFGE--RRGGEDvwelRKRIGLVsPalQLRFPRDETVLDvvlsgffdSIGLYR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 pelESKAKASAADAQLSEAVdswpqGLEtpvDLAG---DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAG---R 140
Cdd:COG1119 114 ---EPTDEQRERARELLELL-----GLA---HLADrpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARellL 182
|
170 180
....*....|....*....|....*
gi 2163878594 141 KILDKLLQSKQ-TVVLIAHNLtkEE 164
Cdd:COG1119 183 ALLDKLAAEGApTLVLVTHHV--EE 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-158 |
1.07e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRT----KIGYLPQQAVLLPSSVMNNITMFDPELESKAKAS 76
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFE---RQSIKKDLCtyqkQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEavdswpqgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ---TV 153
Cdd:PRK13540 109 TELCRLFS--------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAkggAV 180
|
....*
gi 2163878594 154 VLIAH 158
Cdd:PRK13540 181 LLTSH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-170 |
1.10e-08 |
|
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: 52.66 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVG---EAAASGGQISFFdqaGKKVKPDRTK--IGYLPQQAVLLPS-SVMNNITmFDPELESKAKAS 76
Cdd:cd03234 40 GSSGSGKTTLLDAISGrveGGGTTSGQILFN---GQPRKPDQFQkcVAYVRQDDILLPGlTVRETLT-YTAILRLPRKSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQGLETPVdlAGD---NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSK 150
Cdd:cd03234 116 DAIRKKRVEDVLLRDLALTRI--GGNlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALnlvSTLSQLARRN 193
|
170 180
....*....|....*....|
gi 2163878594 151 QTVVLIAHNLTKEERDLFDR 170
Cdd:cd03234 194 RIVILTIHQPRSDLFRLFDR 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-165 |
1.20e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 1.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--TVVLIAHNLTKEER 165
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAAR 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-158 |
1.26e-08 |
|
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: 53.02 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-------VGEAAASGGqisffdqagkkvkpdrTKIGYLPQQAVLLPS-----SVM----------- 59
Cdd:TIGR03719 38 GLNGAGKSTLLRIMagvdkdfNGEARPQPG----------------IKVGYLPQEPQLDPTktvreNVEegvaeikdald 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 60 --NNITMF----DPELESKAKASAADAQLSEAVDSWpqGLETPVDLAGD------------NLSGGQKQKVVLARAEVRD 121
Cdd:TIGR03719 102 rfNEISAKyaepDADFDKLAAEQAELQEIIDAADAW--DLDSQLEIAMDalrcppwdadvtKLSGGERRRVALCRLLLSK 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 2163878594 122 SQLLLVDEGTSAIDqAAGRKILDKLLQS-KQTVVLIAH 158
Cdd:TIGR03719 180 PDMLLLDEPTNHLD-AESVAWLERHLQEyPGTVVAVTH 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-175 |
1.32e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQ-----ISFFDQAgKKVKPDRTKIGYLPQQAVLLPS-SVMNNItMFDP--------- 67
Cdd:PRK09493 34 GPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPK-VDERLIRQEAGMVFQQFYLFPHlTALENV-MFGPlrvrgaske 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 ELESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILdKLL 147
Cdd:PRK09493 112 EAEKQARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL-KVM 179
|
170 180 190
....*....|....*....|....*....|..
gi 2163878594 148 QS----KQTVVLIAHNLTkeerdlFDREVALR 175
Cdd:PRK09493 180 QDlaeeGMTMVIVTHEIG------FAEKVASR 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-176 |
1.36e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFD----------QAGKKVKPDRTKIGYLPQQAVLLP-SSVMNNItMFDPEL-- 69
Cdd:PRK11264 36 GPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsQQKGLIRQLRQHVGFVFQNFNLFPhRTVLENI-IEGPVIvk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 -ESKAKASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---K 145
Cdd:PRK11264 115 gEPKEEATARARELLAKV-----GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNtirQ 189
|
170 180 190
....*....|....*....|....*....|.
gi 2163878594 146 LLQSKQTVVLIAHNLTkeerdlFDREVALRA 176
Cdd:PRK11264 190 LAQEKRTMVIVTHEMS------FARDVADRA 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-155 |
1.50e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.02 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPSSVMNNItMFDPELEskakasAA 78
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEiyRQQVSYCAQTPTLFGDTVYDNL-IFPWQIR------NQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSWPQ-GL-ETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK---ILDKLLQSKQTV 153
Cdd:PRK10247 111 QPDPAIFLDDLERfALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNvneIIHRYVREQNIA 190
|
..
gi 2163878594 154 VL 155
Cdd:PRK10247 191 VL 192
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-165 |
1.83e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLL------VGEAAASG----GQISFFDQagKKVKPDRTKIGYLPQQAVLLPSSVMNNITM------ 64
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLnrmndkVSGYRYSGdvllGGRSIFNY--RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAgvrahk 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 65 FDPELESKAKASAadaQLSEaVDSWpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD 144
Cdd:PRK14271 130 LVPRKEFRGVAQA---RLTE-VGLW-DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180
....*....|....*....|...
gi 2163878594 145 --KLLQSKQTVVLIAHNLTKEER 165
Cdd:PRK14271 205 fiRSLADRLTVIIVTHNLAQAAR 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-135 |
1.87e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 51.92 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF----FDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNIT--------MFDPEL 69
Cdd:COG1126 34 GPSGSGKSTLLRCINLLEEPDSGTITVdgedLTDSKKDINKLRRKVGMVFQQFNLFPHlTVLENVTlapikvkkMSKAEA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:COG1126 114 EERAMELLERVGLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-170 |
2.02e-08 |
|
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: 52.05 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQagKKVKPD-----RTKIGYLPQ----QAVllPSSV-------MNNITMFD 66
Cdd:TIGR04520 35 GHNGSGKSTLAKLLNGLLLPTSGKVTVDGL--DTLDEEnlweiRKKVGMVFQnpdnQFV--GATVeddvafgLENLGVPR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 PELESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL 146
Cdd:TIGR04520 111 EEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETI 179
|
170 180
....*....|....*....|....*...
gi 2163878594 147 LQSKQ----TVVLIAHNLtkEERDLFDR 170
Cdd:TIGR04520 180 RKLNKeegiTVISITHDM--EEAVLADR 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-135 |
2.40e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPssvmnNITMFD-------------PEL 69
Cdd:PRK09452 47 GPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFP-----HMTVFEnvafglrmqktpaAEI 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:PRK09452 122 TPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-165 |
2.45e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.94 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDR--TKIGYLPQQAVllpssVMNNITMFD-------PELESKA 73
Cdd:PRK11231 35 GPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHL-----TPEGITVRElvaygrsPWLSLWG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLseaVDSWPQ--GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQ 148
Cdd:PRK11231 110 RLSAEDNAR---VNQAMEqtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhQVELMRLMRELNT 186
|
170
....*....|....*..
gi 2163878594 149 SKQTVVLIAHNLTKEER 165
Cdd:PRK11231 187 QGKTVVTVLHDLNQASR 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-135 |
2.52e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.57 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQagkkvkpDRTK----------IGYLPQQavllPS-----SVMNNITMFdp 67
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-------DITHlpmhkrarlgIGYLPQE----ASifrklTVEDNILAV-- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163878594 68 eLESKAKASAADAQLSEAVdswpqgLE----TPV-DLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:COG1137 103 -LELRKLSKKEREERLEEL------LEefgiTHLrKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-158 |
3.13e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.66 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFD------QAGKKVKPDRTKIGYLPQ--QAVLLPSSVMNNITmFDP----- 67
Cdd:PRK13643 37 LIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVA-FGPqnfgi 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 ---ELESKAKASAADAQLSEavDSWPQgleTPVDLagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAG---RK 141
Cdd:PRK13643 116 pkeKAEKIAAEKLEMVGLAD--EFWEK---SPFEL-----SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARiemMQ 185
|
170
....*....|....*..
gi 2163878594 142 ILDKLLQSKQTVVLIAH 158
Cdd:PRK13643 186 LFESIHQSGQTVVLVTH 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-158 |
3.72e-08 |
|
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: 50.82 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTK-IGYLPQQAVLLPS-SVMNNITMFDPELeskAKASAAD 79
Cdd:TIGR01189 32 TGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnILYLGHLPGLKPElSALENLHFWAAIH---GGAQRTI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 80 AQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK---ILDKLLQSKQTVVLI 156
Cdd:TIGR01189 109 EDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALlagLLRAHLARGGIVLLT 183
|
..
gi 2163878594 157 AH 158
Cdd:TIGR01189 184 TH 185
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-160 |
3.86e-08 |
|
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: 51.19 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ--AGKKVkPDRTKIG----YlpQQAVLLPS-SVMNNITM---------FD 66
Cdd:COG0411 37 GPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPP-HRIARLGiartF--QNPRLFPElTVLENVLVaaharlgrgLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 PELESKAKASAADAQLSEAVDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDE---GTSAIDQA 137
Cdd:COG0411 114 AALLRLPRARREEREARERAEEL---LER-VGLADradepaGNLSYGQQRRLEIARALATEPKLLLLDEpaaGLNPEETE 189
|
170 180
....*....|....*....|....
gi 2163878594 138 AGRKILDKLLQSKQ-TVVLIAHNL 160
Cdd:COG0411 190 ELAELIRRLRDERGiTILLIEHDM 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-158 |
3.96e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.40 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRtkiGYLPQQAVLLP-SSVMNNITmFDPELeskakASAADAQ 81
Cdd:COG4525 40 GASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---GVVFQKDALLPwLNVLDNVA-FGLRL-----RGVPKAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQ--GLEtpvDLAGDN---LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLL-----QSKQ 151
Cdd:COG4525 111 RRARAEELLAlvGLA---DFARRRiwqLSGGMRQRVGIARALAADPRFLLMDEPFGALD-ALTREQMQELLldvwqRTGK 186
|
....*..
gi 2163878594 152 TVVLIAH 158
Cdd:COG4525 187 GVFLITH 193
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-175 |
4.52e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFK----LLVGEAAAS------GGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNI---TMFD 66
Cdd:PRK09984 35 LLGPSGSGKSTLLRhlsgLITGDKSAGshiellGRTVQREGRLARDIRKSRANTGYIFQQFNLVNRlSVLENVligALGS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 PELESKAKASAADAQLSEAVDSWPQ-GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDK 145
Cdd:PRK09984 115 TPFWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDT 194
|
170 180 190
....*....|....*....|....*....|....
gi 2163878594 146 LLQSKQ----TVVLIAHNLTKEERdLFDREVALR 175
Cdd:PRK09984 195 LRDINQndgiTVVVTLHQVDYALR-YCERIVALR 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-158 |
4.62e-08 |
|
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: 50.57 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTK----IGYLPQQAVLLpsSVMNNITMFDPeleskakaS 76
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARgllyLGHAPGIKTTL--SVLENLRFWHA--------D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ---TV 153
Cdd:cd03231 101 HSDEQVEEALAR--VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCArggMV 178
|
....*
gi 2163878594 154 VLIAH 158
Cdd:cd03231 179 VLTTH 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-176 |
4.86e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD------RTKIGYLPQQAVLLPS-SVMNNITMFDPELESKAKA 75
Cdd:COG3845 38 GENGAGKSTLMKILYGLYQPDSGEILID---GKPVRIRsprdaiALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQ----LSE----AVDswpqgLETPVdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAI-DQAAGR--KILD 144
Cdd:COG3845 115 RKAARArireLSEryglDVD-----PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADElfEILR 185
|
170 180 190
....*....|....*....|....*....|..
gi 2163878594 145 KLLQSKQTVVLIAHNLtKEERDLFDREVALRA 176
Cdd:COG3845 186 RLAAEGKSIIFITHKL-REVMAIADRVTVLRR 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-159 |
7.85e-08 |
|
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: 50.48 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkpDRTKIGYLPQQavLLPSSVMnniTMFDPELESKAKASAADA 80
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEI----------ELDTVSYKPQY--IKADYEG---TVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDswPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQ----AAGRKILDKLLQSKQTVVLI 156
Cdd:cd03237 95 FKTEIAK--PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAENNEKTAFVV 172
|
...
gi 2163878594 157 AHN 159
Cdd:cd03237 173 EHD 175
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-160 |
9.48e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.11 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKP-DRTKIGYLPQQAVLLPS-SVMNNITMFdpeleskakasaadA 80
Cdd:COG4152 34 GPNGAGKTTTIRIILGILAPDSGEVLWD---GEPLDPeDRRRIGYLPEERGLYPKmKVGEQLVYL--------------A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QL-----SEA---VDSWpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL 146
Cdd:COG4152 97 RLkglskAEAkrrADEW---LER-LGLGDrankkvEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170
....*....|....*..
gi 2163878594 147 LQSKQ---TVVLIAHNL 160
Cdd:COG4152 173 RELAAkgtTVIFSSHQM 189
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-159 |
1.18e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQA---GKKVKPDRTKIGYLPQ-QAVLLPSSVMNNITM--FDPELEskak 74
Cdd:PRK11614 36 LIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdWQTAKIMREAVAIVPEgRRVFSRMTVEENLAMggFFAERD---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 asAADAQLSEAVDSWPQGLETPVDLAGdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--- 151
Cdd:PRK11614 112 --QFQERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREqgm 188
|
....*...
gi 2163878594 152 TVVLIAHN 159
Cdd:PRK11614 189 TIFLVEQN 196
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-160 |
1.89e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.41 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVG-----EAAASGGQISFFDQAGKKVKPDRTKIGYLPQQavllPSSVMNNITMFD--------- 66
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGlllpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQN----PDNQFVGATVGDdvafglenr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 ----PELESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI 142
Cdd:PRK13640 114 avprPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
170 180
....*....|....*....|..
gi 2163878594 143 LD---KLLQSKQ-TVVLIAHNL 160
Cdd:PRK13640 183 LKlirKLKKKNNlTVISITHDI 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-135 |
3.64e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqagkKVkpdrtKIGYLPQ----------QAVLlpSSVMNNI--TMFDPELE 70
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDP------EL-----KISYKPQyikpdydgtvEDLL--RSITDDLgsSYYKSEII 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 71 SkakasaadaqlseavdswPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:PRK13409 439 K------------------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-160 |
4.05e-07 |
|
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: 48.65 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISF-------------FDQAGKKVKpdrtKIGYLPQQAVLLP-SSVMNNITmfd 66
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgPDGRGRAKR----YIGILHQEYDLYPhRTVLDNLT--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 peleskakasaadaqlsEAVdswpqGLETPVDLA-------------------------GDNLSGGQKQKVVLARAEVRD 121
Cdd:TIGR03269 388 -----------------EAI-----GLELPDELArmkavitlkmvgfdeekaeeildkyPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2163878594 122 SQLLLVDEGTSAIDQAAGRKILDKLLQSK----QTVVLIAHNL 160
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSILKAReemeQTFIIVSHDM 488
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-174 |
4.46e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.44 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQ--ISFFDQAG-KKVKPDRTKIGYLPQ--QAVLLPSSVMNNITmFDPE---LESK 72
Cdd:PRK13644 33 IIGKNGSGKSTLALHLNGLLRPQKGKvlVSGIDTGDfSKLQGIRKLVGIVFQnpETQFVGRTVEEDLA-FGPEnlcLPPI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASAADAQLSEAvdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQS 149
Cdd:PRK13644 112 EIRKRVDRALAEI------GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLErikKLHEK 185
|
170 180
....*....|....*....|....*
gi 2163878594 150 KQTVVLIAHNLtkEERDLFDREVAL 174
Cdd:PRK13644 186 GKTIVYITHNL--EELHDADRIIVM 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-151 |
5.17e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsFFDqaGKKVKPDRTK---IGYLPQQAVLLPS-SVMNNI----TMfdpeleSKAK 74
Cdd:PRK11432 39 GPSGCGKTTVLRLVAGLEKPTEGQI-FID--GEDVTHRSIQqrdICMVFQSYALFPHmSLGENVgyglKM------LGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 ASAADAQLSEAvdswpqgLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ 148
Cdd:PRK11432 110 KEERKQRVKEA-------LEL-VDLAGfedryvDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
...
gi 2163878594 149 SKQ 151
Cdd:PRK11432 182 LQQ 184
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-158 |
5.85e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.82 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQA------GKKVKPDRTKIGYLPQ--QAVLLPSSVMNNITmFDP------- 67
Cdd:PRK13649 40 GHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDVA-FGPqnfgvsq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 -ELESKAKASAADAQLSEavdswpqgletpvDLAGDN---LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRK-- 141
Cdd:PRK13649 119 eEAEALAREKLALVGISE-------------SLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLD-PKGRKel 184
|
170
....*....|....*....
gi 2163878594 142 --ILDKLLQSKQTVVLIAH 158
Cdd:PRK13649 185 mtLFKKLHQSGMTIVLVTH 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-172 |
5.98e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsFFDqaGKKVKPDRtkigylPQQAVLLPSSVMNNITMFDPELESKAKASAadaql 82
Cdd:PRK10522 356 GGNGSGKSTLAMLLTGLYQPQSGEI-LLD--GKPVTAEQ------PEDYRKLFSAVFTDFHLFDQLLGPEGKPAN----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 83 SEAVDSWPQ--GLETPVDLAGD-----NLSGGQKQKV--VLARAEVRDsqLLLVDEGtsAIDQAAG------RKILDKLL 147
Cdd:PRK10522 422 PALVEKWLErlKMAHKLELEDGrisnlKLSKGQKKRLalLLALAEERD--ILLLDEW--AADQDPHfrrefyQVLLPLLQ 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2163878594 148 QSKQTVVLIAHN--------------------LTKEERDLFDREV 172
Cdd:PRK10522 498 EMGKTIFAISHDdhyfihadrllemrngqlseLTGEERDAASRDA 542
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-160 |
6.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 6.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSKQTVVLIAHNL 160
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEifdNLNKQGKTIILVTHDL 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-160 |
7.59e-07 |
|
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: 47.33 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDqagkkVKPDRTKIGYLPQQAVL----------LPS----SVMNNITMFDPE 68
Cdd:cd03267 54 GPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKFLRRIGVVfgqktqlwwdLPVidsfYLLAAIYDLPPA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 69 leskaKASAADAQLSEAVDSWPQgLETPVdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDK 145
Cdd:cd03267 129 -----RFKKRLDELSELLDLEEL-LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaQENIRNFLKE 198
|
170
....*....|....*.
gi 2163878594 146 LLQSKQ-TVVLIAHNL 160
Cdd:cd03267 199 YNRERGtTVLLTSHYM 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-165 |
7.65e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLL------VGEAAASGGQISFFDQAGKKVKPD--RTKIGYLPQQAVLLPS-SVMNNIT--MFDPEL 69
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQIDAIklRKEVGMVFQQPNPFPHlSIYDNIAypLKSHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQgLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKIlDKL--- 146
Cdd:PRK14246 121 KEKREIKKIVEECLRKVGLWKE-VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI-EKLite 198
|
170
....*....|....*....
gi 2163878594 147 LQSKQTVVLIAHNLTKEER 165
Cdd:PRK14246 199 LKNEIAIVIVSHNPQQVAR 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-160 |
1.13e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 47.27 E-value: 1.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID-QAAGR--KILDKLLQSKQTVVLIAHNL 160
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpELVGEvlRIMQQLAEEGKTMVVVTHEM 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-174 |
1.33e-06 |
|
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: 46.39 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASG--GQIsFFDqaGKKVKPD--RTKIGYLPQQAVLLPSSVMNNITMFDPELeskakasaa 78
Cdd:cd03213 42 GPSGAGKSTLLNALAGRRTGLGvsGEV-LIN--GRPLDKRsfRKIIGYVPQDDILHPTLTVRETLMFAAKL--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 daqlseavdswpQGLetpvdlagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSKQTVVL 155
Cdd:cd03213 110 ------------RGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALqvmSLLRRLADTGRTIIC 166
|
170
....*....|....*....
gi 2163878594 156 IAHNLTKEERDLFDREVAL 174
Cdd:cd03213 167 SIHQPSSEIFELFDKLLLL 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-160 |
1.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.75 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQ------AGKKVKPDRTKIGYLPQ--QAVLLPSSVMNNItMFDPelesk 72
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetGNKNLKKLRKKVSLVFQfpEAQLFENTVLKDV-EFGP----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASAADAQLSEAVDSWPQGLETPVDLAGDN---LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQS 149
Cdd:PRK13641 112 KNFGFSEDEAKEKALKWLKKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-PEGRKEMMQLFKD 190
|
170
....*....|....*
gi 2163878594 150 KQ----TVVLIAHNL 160
Cdd:PRK13641 191 YQkaghTVILVTHNM 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-169 |
1.59e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELES-KAKASAADAQ 81
Cdd:PLN03211 101 GPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRLpKSLTKQEKIL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQGLETPVDLAGDN----LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKI---LDKLLQSKQTVV 154
Cdd:PLN03211 181 VAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLvltLGSLAQKGKTIV 260
|
170
....*....|....*
gi 2163878594 155 LIAHNLTKEERDLFD 169
Cdd:PLN03211 261 TSMHQPSSRVYQMFD 275
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-169 |
2.12e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQLAWVNQETPALPQPALEYVIDGDREYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLS------------EAVDSWP----------------QGLETPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTS 132
Cdd:PRK10636 103 ERNdghaiatihgklDAIDAWTirsraasllhglgfsnEQLERPVS----DFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 2163878594 133 AIDQAAgRKILDKLLQSKQ-TVVLIAHnltkeERDLFD 169
Cdd:PRK10636 179 HLDLDA-VIWLEKWLKSYQgTLILISH-----DRDFLD 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-160 |
2.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.17 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFD---QAGKK---VKPDRTKIGYLPQ--QAVLLPSSVMNNITmFDP------- 67
Cdd:PRK13634 40 GHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKnkkLKPLRKKVGIVFQfpEHQLFEETVEKDIC-FGPmnfgvse 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 68 -ELESKAKASAADAQLSEAVDSwpqglETPVDLagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD-- 144
Cdd:PRK13634 119 eDAKQKAREMIELVGLPEELLA-----RSPFEL-----SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmf 188
|
170
....*....|....*...
gi 2163878594 145 -KLLQSKQ-TVVLIAHNL 160
Cdd:PRK13634 189 yKLHKEKGlTTVLVTHSM 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-175 |
2.46e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD---RTKIGYLPQQ-AVLLPSSVMNNitMFDPELESKAKASAA 78
Cdd:PRK09700 38 GENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaQLGIGIIYQElSVIDELTVLEN--LYIGRHLTKKVCGVN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSE-----AVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRK---ILDKLLQSK 150
Cdd:PRK09700 116 IIDWREmrvraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYlflIMNQLRKEG 195
|
170 180
....*....|....*....|....*
gi 2163878594 151 QTVVLIAHNLtKEERDLFDREVALR 175
Cdd:PRK09700 196 TAIVYISHKL-AEIRRICDRYTVMK 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-170 |
2.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.88 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsFFDqaGKKVKPD-----RTKIGYLPQQavllPSSVMNNITMFDPELESKAKASA 77
Cdd:PRK13650 40 GHNGSGKSTTVRLIDGLLEAESGQI-IID--GDLLTEEnvwdiRHKIGMVFQN----PDNQFVGATVEDDVAFGLENKGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLSEAVDSWPQ--GLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRKILDKLLQS-----K 150
Cdd:PRK13650 113 PHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD-PEGRLELIKTIKGirddyQ 191
|
170 180
....*....|....*....|
gi 2163878594 151 QTVVLIAHNLtkEERDLFDR 170
Cdd:PRK13650 192 MTVISITHDL--DEVALSDR 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-160 |
2.75e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 46.16 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD-----RTKIGYLPQ----QAVllPSSV-------MNNITMFD 66
Cdd:PRK13635 40 GHNGSGKSTLAKLLNGLLLPEAGTITVG---GMVLSEEtvwdvRRQVGMVFQnpdnQFV--GATVqddvafgLENIGVPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 67 PELeskakasaaDAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL 146
Cdd:PRK13635 115 EEM---------VERVDQALRQ--VGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETV 183
|
170
....*....|....*...
gi 2163878594 147 LQSKQ----TVVLIAHNL 160
Cdd:PRK13635 184 RQLKEqkgiTVLSITHDL 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
3-160 |
2.89e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASgGQISFFDQA-----GKKVKPDRtkiGYLPQQAVLLPS-SVMNNITMFDPELESKAKAS 76
Cdd:PRK03695 29 GPNGAGKSTLLARMAGLLPGS-GSIQFAGQPleawsAAELARHR---AYLSQQQTPPFAmPVFQYLTLHQPDKTRTEAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQgLETPVdlagDNLSGGQKQKVVLARAEVR-------DSQLLLVDEGTSAID---QAAGRKILDKL 146
Cdd:PRK03695 105 SALNEVAEALGLDDK-LGRSV----NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDvaqQAALDRLLSEL 179
|
170
....*....|....
gi 2163878594 147 LQSKQTVVLIAHNL 160
Cdd:PRK03695 180 CQQGIAVVMSSHDL 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
104-160 |
3.20e-06 |
|
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: 46.22 E-value: 3.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAagrKILDKL--LQSKQ--TVVLIAHNL 160
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvQA---QILDLLrdLQREHglAYLFISHDL 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-160 |
4.27e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.59 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVG--EAAASGGQISFfdqAGKKVKP------DRTKIGYLPQQAVLLPS-SVMNNI--------- 62
Cdd:TIGR02633 32 LCGENGAGKSTLMKILSGvyPHGTWDGEIYW---SGSPLKAsnirdtERAGIVIIHQELTLVPElSVAENIflgneitlp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 63 --TMFDPELESKAKASAADAQLSEAVDSWPQGletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR 140
Cdd:TIGR02633 109 ggRMAYNAMYLRAKNLLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETE 178
|
170 180
....*....|....*....|...
gi 2163878594 141 KILDKLLQSKQ---TVVLIAHNL 160
Cdd:TIGR02633 179 ILLDIIRDLKAhgvACVYISHKL 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-161 |
4.62e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQ----------ISFFdqAG-------KKVKPDRTKIGYLPQQAVLLPSSVMNNITmf 65
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPNLGDydeepswdevLKRF--RGtelqdyfKKLANGEIKVAHKPQYVDLIPKVFKGTVR-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 66 dpELESKAKASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID-----QAAgr 140
Cdd:COG1245 182 --ELLEKVDERGKLDELAEKL-----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlNVA-- 252
|
170 180
....*....|....*....|.
gi 2163878594 141 KILDKLLQSKQTVVLIAHNLT 161
Cdd:COG1245 253 RLIRELAEEGKYVLVVEHDLA 273
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-160 |
4.85e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 45.21 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIsFFDqaGKKVKP----DRTK-IGYLPQQavllPSSVMN---NI-----------T 63
Cdd:COG4167 46 GENGSGKSTLAKMLAGIIEPTSGEI-LIN--GHKLEYgdykYRCKhIRMIFQD----PNTSLNprlNIgqileeplrlnT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 64 MFDPElESKAKASAADAQ---LSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR 140
Cdd:COG4167 119 DLTAE-EREERIFATLRLvglLPEHANFYPH-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRS 186
|
170 180
....*....|....*....|....
gi 2163878594 141 KILDKLL--QSKQTV--VLIAHNL 160
Cdd:COG4167 187 QIINLMLelQEKLGIsyIYVSQHL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
105-160 |
6.67e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 6.67e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 105 SGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD--KLLQSKQTV--VLIAHNL 160
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILAllKSLQQKHQLayLFISHDL 486
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-176 |
6.69e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPDRTKIGYLPQQAVLLPS-SVMNNITmF--------DPELESKA 73
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHlSVAENMS-FglklagakKEEINQRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLSEAVDSWPQGLetpvdlagdnlSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGR---KI----LDKL 146
Cdd:PRK11000 115 NQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD-AALRvqmRIeisrLHKR 182
|
170 180 190
....*....|....*....|....*....|
gi 2163878594 147 LQSkqTVVLIAHNLTkEERDLFDREVALRA 176
Cdd:PRK11000 183 LGR--TMIYVTHDQV-EAMTLADKIVVLDA 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-160 |
7.06e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.08 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFF-----DQAGKKVKPDRTKIGYLPQQ--AVLLPSSVMNNIT-----MFDPEL- 69
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKATDGEVAWLgkdllGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIaeplrTYHPKLs 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 -----ESKAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD 144
Cdd:PRK15079 134 rqevkDRVKAMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVN 202
|
170 180
....*....|....*....|.
gi 2163878594 145 kLLQSKQ-----TVVLIAHNL 160
Cdd:PRK15079 203 -LLQQLQremglSLIFIAHDL 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-158 |
7.26e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.52 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKL------LVGEAAASG-----GQISFfdqagkkvKPDRTKIGYLPQQAVLLPSSV----------- 58
Cdd:PRK14247 34 LMGPSGSGKSTLLRVfnrlieLYPEARVSGevyldGQDIF--------KMDVIELRRRVQMVFQIPNPIpnlsifenval 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 59 ---MNNITMFDPELESKAKASAADAQLSEAVdswpqglETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:PRK14247 106 glkLNRLVKSKKELQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180
....*....|....*....|....*
gi 2163878594 136 QAAGRKILDKLLQSKQ--TVVLIAH 158
Cdd:PRK14247 179 PENTAKIESLFLELKKdmTIVLVTH 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
104-162 |
1.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSK---QTVVLIAHNLTK 162
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKannKTVFVITHTMEH 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-160 |
1.15e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVG--EAAASGGQISFfdqAGKKVKP------DRTKIGYLPQQAVLLPS-SVMNNI----------T 63
Cdd:PRK13549 38 GENGAGKSTLMKVLSGvyPHGTYEGEIIF---EGEELQAsnirdtERAGIAIIHQELALVKElSVLENIflgneitpggI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 64 MFDPELESKAKASAADAQLSEAVDswpqgleTPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKIL 143
Cdd:PRK13549 115 MDYDAMYLRAQKLLAQLKLDINPA-------TPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
|
170 180
....*....|....*....|
gi 2163878594 144 D--KLLQSKQ-TVVLIAHNL 160
Cdd:PRK13549 184 DiiRDLKAHGiACIYISHKL 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-158 |
1.19e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGG-QISFFDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADAQ 81
Cdd:TIGR01271 1252 GRTGSGKSTLLSALLRLLSTEGEiQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVG 1331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 82 LSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ--SKQTVVLIAH 158
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfSNCTVILSEH 1410
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-158 |
1.23e-05 |
|
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: 44.41 E-value: 1.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ----SKQTVVLIAH 158
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkaSGISMVLTSH 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-174 |
1.33e-05 |
|
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: 43.90 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQ--ISFFDqAGKKVKPDRTKIGYLPQQAvllpsSVMNNITMFDPELESKAKASAADA 80
Cdd:cd03265 33 GPNGAGKTTTIKMLTTLLKPTSGRatVAGHD-VVREPREVRRRIGIVFQDL-----SVDDELTGWENLYIHARLYGVPGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDswpQGLETpVDL--AGDNL----SGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--- 151
Cdd:cd03265 107 ERRERID---ELLDF-VGLleAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefg 182
|
170 180
....*....|....*....|....
gi 2163878594 152 -TVVLIAHNLtkEERDLFDREVAL 174
Cdd:cd03265 183 mTILLTTHYM--EEAEQLCDRVAI 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
104-160 |
1.66e-05 |
|
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: 43.90 E-value: 1.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAagrKILDkLLQSKQT-----VVLIAHNL 160
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQA---QILD-LLKDLQRelgmaLLLITHDL 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-156 |
1.80e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ----AGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAA 78
Cdd:PRK15112 46 GENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 DAQLSEAVDSwpqgletpVDLAGDN-------LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL--LQS 149
Cdd:PRK15112 126 EKQIIETLRQ--------VGLLPDHasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMleLQE 197
|
....*..
gi 2163878594 150 KQTVVLI 156
Cdd:PRK15112 198 KQGISYI 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-160 |
1.82e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADA 80
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLW---QGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 QLSEAVDSWPQGLeTPVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqAAGRK----ILDKLLQSK 150
Cdd:PRK13638 109 PEAEITRRVDEAL-TLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD-PAGRTqmiaIIRRIVAQG 186
|
170
....*....|
gi 2163878594 151 QTVVLIAHNL 160
Cdd:PRK13638 187 NHVIISSHDI 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-135 |
1.88e-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: 44.00 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISffdqagKKVkpdrtKIGYLPQ----------QAVLlpSSVmnNITMFDpelesk 72
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEGEVD------EDL-----KISYKPQyispdydgtvEEFL--RSA--NTDDFG------ 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 akasaadaqlseavDSW-------PQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:COG1245 432 --------------SSYykteiikPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-161 |
1.88e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQ----------ISFFdqAG-------KKVKPDRTKIGYLPQQAVLLPSSVMNNITmf 65
Cdd:PRK13409 106 GPNGIGKTTAVKILSGELIPNLGDyeeepswdevLKRF--RGtelqnyfKKLYNGEIKVVHKPQYVDLIPKVFKGKVR-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 66 dpELESKAKASAADAQLSEAVdswpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID--Q--AAGRK 141
Cdd:PRK13409 182 --ELLKKVDERGKLDEVVERL-----GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirQrlNVARL 254
|
170 180
....*....|....*....|
gi 2163878594 142 ILDklLQSKQTVVLIAHNLT 161
Cdd:PRK13409 255 IRE--LAEGKYVLVVEHDLA 272
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-160 |
2.46e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 43.30 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF----FDQAGKKVKPDRTKIGYLPQQA--VLLPSSVMNNIT-----MFDPELES 71
Cdd:PRK13636 39 GGNGAGKSTLFQNLNGILKPSSGRILFdgkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVYQDVSfgavnLKLPEDEV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 KAKASAADAQlseavdswpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ 151
Cdd:PRK13636 119 RKRVDNALKR---------TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQK 189
|
170
....*....|...
gi 2163878594 152 ----TVVLIAHNL 160
Cdd:PRK13636 190 elglTIIIATHDI 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-160 |
2.56e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 6 GTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRtkigylPQQA-----VLLP-----------SSVMNNITMFDPEL 69
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLD---GKPIDIRS------PRDAiragiMLCPedrkaegiipvHSVADNINISARRH 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQGL--ETP-VDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD-- 144
Cdd:PRK11288 360 HLRAGCLINNRWEAENADRFIRSLniKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNvi 439
|
170
....*....|....*..
gi 2163878594 145 -KLLQSKQTVVLIAHNL 160
Cdd:PRK11288 440 yELAAQGVAVLFVSSDL 456
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
104-160 |
2.78e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 43.18 E-value: 2.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAagrKILDkLLQSKQ-----TVVLIAHNL 160
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiQA---QVLN-LLEDLQdelglTYLFISHDL 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-160 |
2.99e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAG-------KKVKPDRTKIGYLPQ--QAVLLPSSVMNNITmFDPeLESKA 73
Cdd:PRK13645 44 GTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkiKEVKRLRKEIGLVFQfpEYQLFQETIEKDIA-FGP-VNLGE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLSEAVDSwpqgLETPVDLAGDN---LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL--- 147
Cdd:PRK13645 122 NKQEAYKKVPELLKL----VQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErln 197
|
170
....*....|....
gi 2163878594 148 -QSKQTVVLIAHNL 160
Cdd:PRK13645 198 kEYKKRIIMVTHNM 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-138 |
3.92e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD----RTKIGYLpQQAVLLPS--SVMNNITM----FD-PELES 71
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLF---GQPVDAGdiatRRRVGYM-SQAFSLYGelTVRQNLELharlFHlPAAEI 374
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 72 KAKASAADAQ--LSEAVDSWPqgletpvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAA 138
Cdd:NF033858 375 AARVAEMLERfdLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-156 |
4.58e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 6 GTGKSTLFKLLVGEAAASGGQISFFDQA--GKKVKpDRTK--IGYLPQ----QAVLLPSSVMNNITM---FDPELES--- 71
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDitGLSPR-ERRRlgVAYIPEdrlgRGLVPDMSVAENLILgryRRPPFSRggf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 72 --KAKASAADAQLSEAVDSWPQGLETPVDlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQS 149
Cdd:COG3845 373 ldRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
170
....*....|
gi 2163878594 150 KQ---TVVLI 156
Cdd:COG3845 449 RDagaAVLLI 458
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-158 |
4.65e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLL-------VGEAAASGGqisffdqagkkvkpdrTKIGYLPQQAVLLPS-----SVM----------- 59
Cdd:PRK11819 40 GLNGAGKSTLLRIMagvdkefEGEARPAPG----------------IKVGYLPQEPQLDPEktvreNVEegvaevkaald 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 60 --NNITM-FDPELESKAKASAADAQLSE---AVDSWpqGLETPVDLAGD------------NLSGGQKQKVVLARAEVRD 121
Cdd:PRK11819 104 rfNEIYAaYAEPDADFDALAAEQGELQEiidAADAW--DLDSQLEIAMDalrcppwdakvtKLSGGERRRVALCRLLLEK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 2163878594 122 SQLLLVDEGTSAIDqAAGRKILDKLLQS-KQTVVLIAH 158
Cdd:PRK11819 182 PDMLLLDEPTNHLD-AESVAWLEQFLHDyPGTVVAVTH 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1-160 |
5.14e-05 |
|
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: 41.79 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFfdqagkkvkpDRTKIGYLPQQAvllpssvmnnitmfdpeleskakasaada 80
Cdd:cd03222 30 IVGPNGTGKTTAVKILAGQLIPNGDNDEW----------DGITPVYKPQYI----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 81 qlseavdswpqgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQ----AAGRKILDKLLQSKQTVVLI 156
Cdd:cd03222 71 ----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVV 128
|
....
gi 2163878594 157 AHNL 160
Cdd:cd03222 129 EHDL 132
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
3-135 |
5.39e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQIS-----FFDQAGK-KVKPDRTKIGYLPQQAVLLPS-SVMNN----ITMFDPEles 71
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVlngrvLFDAEKGiCLPPEKRRIGYVFQDARLFPHyKVRGNlrygMAKSMVA--- 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163878594 72 kakasaadaQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:PRK11144 108 ---------QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
104-160 |
5.64e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 5.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TVVLIAHNL 160
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNL 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
104-160 |
5.99e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 5.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TVVLIAHNL 160
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDL 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-160 |
6.58e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.03 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPD-----RTKIGYLPQQA--VLLPSSVMNNITmFDPeLESKAKA 75
Cdd:PRK13647 38 GPNGAGKSTLLLHLNGIYLPQRGRVKVM---GREVNAEnekwvRSKVGLVFQDPddQVFSSTVWDDVA-FGP-VNMGLDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 76 SAADAQLSEAVDSwpQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKQT 152
Cdd:PRK13647 113 DEVERRVEEALKA--VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKT 190
|
....*...
gi 2163878594 153 VVLIAHNL 160
Cdd:PRK13647 191 VIVATHDV 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
105-160 |
6.97e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 6.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 105 SGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TVVLIAHNL 160
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelglSYVFISHDL 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
97-160 |
7.63e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 42.14 E-value: 7.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163878594 97 VDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKQTVVLIAHNL 160
Cdd:PRK09536 133 ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhQVRTLELVRRLVDDGKTAVAAIHDL 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-132 |
8.43e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqAGKKVKPDRTK------IGYLPQQAVLLPS-SVMNNITMFD-PE----LE 70
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILI---DGQEMRFASTTaalaagVAIIYQELHLVPEmTVAENLYLGQlPHkggiVN 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163878594 71 SKAKASAADAQLSE-AVDSWPQgleTPVdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTS 132
Cdd:PRK11288 114 RRLLNYEAREQLEHlGVDIDPD---TPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
98-160 |
8.91e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 8.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163878594 98 DLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSKQTVVLIAHNL 160
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQQGVAIIVISSEL 465
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-160 |
1.02e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.33 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQ--AGKKVKPDRTKIGYL---PQQAVLLPSsVMNNITmFDPeLESKAKASA 77
Cdd:PRK13652 37 GPNGAGKSTLFRHFNGILKPTSGSVLIRGEpiTKENIREVRKFVGLVfqnPDDQIFSPT-VEQDIA-FGP-INLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 78 ADAQLSEAVDSWpqGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKL----LQSKQTV 153
Cdd:PRK13652 114 VAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLndlpETYGMTV 191
|
....*..
gi 2163878594 154 VLIAHNL 160
Cdd:PRK13652 192 IFSTHQL 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-158 |
1.55e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISffdqagkkVKPDrTKIGYLPQ-QAVLLPSSVMNNITMFDPELESKAKASAADAQ 81
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVS--------LDPN-ERLGKLRQdQFAFEEFTVLDTVIMGHTELWEVKQERDRIYA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSwpQG-----LE---------TPVDLAGDNLSG-----------------GQKQKVVLARAEVRDSQLLLVDEG 130
Cdd:PRK15064 105 LPEMSEE--DGmkvadLEvkfaemdgyTAEARAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDILLLDEP 182
|
170 180
....*....|....*....|....*...
gi 2163878594 131 TSAIDQAAGRKILDKLLQSKQTVVLIAH 158
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNSTMIIISH 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-158 |
1.65e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 40.71 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQiSFFDQAGKKVKPDRTKIGYLPQ-----QAVLLPSSVmnnitmfdpeleskakas 76
Cdd:COG2401 62 VGASGSGKSTLLRLLAGALKGTPVA-GCVDVPDNQFGREASLIDAIGRkgdfkDAVELLNAV------------------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 aadaQLSEAVdSWpqgLETPvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID----QAAGRKILDKLLQSKQT 152
Cdd:COG2401 123 ----GLSDAV-LW---LRRF-----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGIT 189
|
....*.
gi 2163878594 153 VVLIAH 158
Cdd:COG2401 190 LVVATH 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-49 |
2.09e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 2.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFDQAgkkvkpdrtKIGYLPQ 49
Cdd:PRK15064 352 GENGVGKTTLLRTLVGELEPDSGTVKWSENA---------NIGYYAQ 389
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-170 |
2.43e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKP-DRTKIG--YLP---QQAVL-LPSSVMNNITMFdpeLESKA 73
Cdd:PRK15439 294 LAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGlvYLPedrQSSGLyLDAPLAWNVCAL---THNRR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 KASAADAQLSEAVDSWPQGLE---TPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAgRKILDKLLQS- 149
Cdd:PRK15439 371 GFWIKPARENAVLERYRRALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA-RNDIYQLIRSi 449
|
170 180
....*....|....*....|....
gi 2163878594 150 -KQTV--VLIAHNLTKEERdLFDR 170
Cdd:PRK15439 450 aAQNVavLFISSDLEEIEQ-MADR 472
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
104-174 |
2.57e-04 |
|
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: 39.65 E-value: 2.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163878594 104 LSGGQKQKV----VLARAEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSKQTVVLIAHNLtkeerDLFDREVAL 174
Cdd:cd03227 78 LSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEailEHLVKGAQVIVITHLP-----ELAELADKL 150
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-160 |
3.12e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 40.03 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISF--FDQAGKKVKPD--RTKIGYLPQ--QAVLLPSSVMNNITmFDPElESKAKAS 76
Cdd:PRK13637 40 GHTGSGKSTLIQHLNGLLKPTSGKIIIdgVDITDKKVKLSdiRKKVGLVFQypEYQLFEETIEKDIA-FGPI-NLGLSEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 77 AADAQLSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLL----QSKQT 152
Cdd:PRK13637 118 EIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelhkEYNMT 197
|
....*...
gi 2163878594 153 VVLIAHNL 160
Cdd:PRK13637 198 IILVSHSM 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-159 |
3.34e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFfdqaGKKVkpdrtKIGYLPQ-QAVLLPS--SVMNNITMFDP-ELEskakasaa 78
Cdd:PRK10636 345 GRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-----KLGYFAQhQLEFLRAdeSPLQHLARLAPqELE-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 79 dAQLSEAVDSWP-QGleTPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQTVVLIA 157
Cdd:PRK10636 408 -QKLRDYLGGFGfQG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVS 484
|
..
gi 2163878594 158 HN 159
Cdd:PRK10636 485 HD 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
98-160 |
3.53e-04 |
|
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: 40.19 E-value: 3.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163878594 98 DLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSKQTVVLIAHNL 160
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYeiyKLINQLAQEGVAIIVVSSEL 463
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-42 |
3.62e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 3.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGG--------QISFFDQAGKKVKPDRT 42
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGtikigetvKLAYVDQSRDALDPNKT 404
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-176 |
4.28e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFD-QAGKKVKPDRTKIGYlpQQAVLLPSSVMNNITMFdpeleskakasaadAQ 81
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNcNINNIAKPYCTYIGH--NLGLKLEMTVFENLKFW--------------SE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQG-----LETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEgtsaidqaagrkildkllqskqtvvlI 156
Cdd:PRK13541 97 IYNSAETLYAAihyfkLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE--------------------------V 150
|
170 180
....*....|....*....|
gi 2163878594 157 AHNLTKEERDLFDREVALRA 176
Cdd:PRK13541 151 ETNLSKENRDLLNNLIVMKA 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-151 |
4.47e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFdqaGKKVKPDRTK------IGYLPQQ----AVLLPSSVMNNITMFDPELESK 72
Cdd:PRK10762 285 GLMGAGRTELMKVLYGALPRTSGYVTLD---GHEVVTRSPQdglangIVYISEDrkrdGLVLGMSVKENMSLTALRYFSR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 73 AKASAADAQLSEAVDSWPQ--GLETP-VDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQS 149
Cdd:PRK10762 362 AGGSLKHADEQQAVSDFIRlfNIKTPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF 441
|
..
gi 2163878594 150 KQ 151
Cdd:PRK10762 442 KA 443
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-160 |
4.56e-04 |
|
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: 39.45 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGG-QISFFDQAGKKVKPDRTKIGYLPQQAVLLPSSVMNNITMFDPELESKAKASAADAQ 81
Cdd:cd03289 37 GRTGSGKSTLLSAFLRLLNTEGDiQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 82 LSEAVDSWPQGLETPVDLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ--TVVLIAHN 159
Cdd:cd03289 117 LKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAdcTVILSEHR 196
|
.
gi 2163878594 160 L 160
Cdd:cd03289 197 I 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-138 |
5.44e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.02 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 2 TGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKPD-RTKIGYLPQQAVLlpssvmnnitmfDPEL---ESKAKASA 77
Cdd:PRK13538 33 EGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDLLYLGHQPGI------------KTELtalENLRFYQR 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163878594 78 ADAQLSEAvDSWpQGLETpVDLAG------DNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAA 138
Cdd:PRK13538 101 LHGPGDDE-ALW-EALAQ-VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-135 |
8.97e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 38.67 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQAGKKVKP-DRtKIGYLPQQAVLLPS-SVMNNIT-------MFDPELES 71
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDR-DIAMVFQNYALYPHmSVRENMAyglkirgMPKAEIEE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163878594 72 KAKASAADAQLSEAVDSWPQgletpvdlagdNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAID 135
Cdd:PRK11650 114 RVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
103-156 |
1.06e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 103 NLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDqaAGRK-----ILDKLLQSKQTVVLI 156
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGAKyeiytIINELAAEGKGVIVI 460
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
104-158 |
1.24e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 38.39 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQTVVLIAH 158
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISH 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
105-160 |
1.46e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 38.17 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 105 SGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQSKQT-VVLIAHNL 160
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvQAQIMTLLNELKREFNTaIIMITHDL 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-42 |
1.47e-03 |
|
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: 38.38 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGG--------QISFFDQAGKKVKPDRT 42
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGtieigetvKLAYVDQSRDALDPNKT 402
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-156 |
1.49e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAG---RKILDKLLQSKQTVVLI 156
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRqqlAELLASLHQSGITLVLV 191
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-29 |
1.77e-03 |
|
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: 37.86 E-value: 1.77e-03
10 20
....*....|....*....|....*....
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISF 29
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-165 |
1.78e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 37.91 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 1 MTGANGTGKSTLFKLLVGEAAASGGQISFFDQ-----AGKKVKPDRTKIGYLPQQ--AVLLPSSVMNNITMfDP----EL 69
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIM-EPlrvhGL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 70 ESKAKASAADAQLSEAVDSWPQ-GLETPvdlagDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQ 148
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEhAWRYP-----HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180
....*....|....*....|.
gi 2163878594 149 SKQTV----VLIAHNLTKEER 165
Cdd:PRK10261 509 LQRDFgiayLFISHDMAVVER 529
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
104-161 |
2.77e-03 |
|
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: 36.53 E-value: 2.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163878594 104 LSGGQKQKVVLAR--AEVRDSQLLLVDEGTSAIDQAAGRKILD---KLLQSKQTVVLIAHNLT 161
Cdd:cd03238 88 LSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEvikGLIDLGNTVILIEHNLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
104-160 |
2.85e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 37.09 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAID---QAAGRKILDKLLQ-SKQTVVLIAHNL 160
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEpttQAQIFRLLTRLNQnNNTTILLISHDL 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
104-160 |
4.35e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 36.69 E-value: 4.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR---KILDKLLQSKQTVVLIAHNL 160
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAeiyKVMRQLADDGKVILMVSSEL 469
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
104-176 |
5.20e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 36.61 E-value: 5.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILDKLLQSKQ----TVVLIAHNLtkEERDLFDREVALRA 176
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHDL--DEAASSDRILVMKA 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-160 |
5.54e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 36.30 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVGEAAASGGQISFFD------QAGKKVKPDRTKIGYLPQ--QAVLLPSSVMNNItMFDPEleskak 74
Cdd:PRK13646 40 GQTGSGKSTLIQNINALLKPTTGTVTVDDitithkTKDKYIRPVRKRIGMVFQfpESQLFEDTVEREI-IFGPK------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 75 asAADAQLSEAVDSWPQ-----GLETPV-DLAGDNLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD--KL 146
Cdd:PRK13646 113 --NFKMNLDEVKNYAHRllmdlGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRllKS 190
|
170
....*....|....*.
gi 2163878594 147 LQSKQ--TVVLIAHNL 160
Cdd:PRK13646 191 LQTDEnkTIILVSHDM 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
104-158 |
6.53e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 36.22 E-value: 6.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2163878594 104 LSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGRKILD--KLLQSKQ--TVVLIAH 158
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNtiKELNKKYgiTIILITH 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-160 |
9.57e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 35.92 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 3 GANGTGKSTLFKLLVG--EAAASGGQIsFFDqaGKKVK------PDRTKIGYLPQQAVLLPS-SVMNNITMFDPeleska 73
Cdd:NF040905 34 GENGAGKSTLMKVLSGvyPHGSYEGEI-LFD--GEVCRfkdirdSEALGIVIIHQELALIPYlSIAENIFLGNE------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163878594 74 kasaadaQLSEAVDSWPQ------------GL-ETPVDLAGDnLSGGQKQKVVLARAEVRDSQLLLVDEGTSAIDQAAGR 140
Cdd:NF040905 105 -------RAKRGVIDWNEtnrrarellakvGLdESPDTLVTD-IGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSA 176
|
170 180
....*....|....*....|...
gi 2163878594 141 KILDKLLQSKQ---TVVLIAHNL 160
Cdd:NF040905 177 ALLDLLLELKAqgiTSIIISHKL 199
|
|
| |
