|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-245 |
3.42e-124 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 352.85 E-value: 3.42e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQ---GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGY 77
Cdd:COG1116 5 APALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAA--GKIVYALDVDLPKPRTLEMRYEPRFNEL 235
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVDLPRPRDRELRTSPEFAAL 244
|
250
....*....|
gi 1215498689 236 SFHVRQAMEG 245
Cdd:COG1116 245 RAEILDLLRE 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-218 |
1.15e-105 |
|
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: 304.78 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY---QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQ 80
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAA--GKIVYALDVDL 218
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
4.63e-81 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.93 E-value: 4.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-PSS--SIGY 77
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEkrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
1.04e-80 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 242.85 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGL---TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGY 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAA--GKIVYALDVD 217
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLELD 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-211 |
9.39e-78 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 234.17 E-value: 9.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQ---GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:COG1136 5 LELRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDiAEAVYLADRIAVMAAGKIV 211
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-211 |
1.11e-77 |
|
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: 233.57 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGYVFQ 80
Cdd:cd03259 1 LELKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-211 |
4.14e-73 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 224.97 E-value: 4.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK--PSS---SIGYVF 79
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDldPVElrrRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGL--SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
1.31e-72 |
|
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: 220.82 E-value: 1.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGL---TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIaEAVYLADRIAVMAAGKI 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-211 |
8.19e-69 |
|
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: 211.78 E-value: 8.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-----KPSSSIGYV 78
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGL--SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 157 EPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
4.03e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 213.78 E-value: 4.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGY 77
Cdd:COG3839 1 MASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-235 |
6.11e-68 |
|
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: 209.24 E-value: 6.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQAPTLLEWKRVIDNVLLPIS 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 100 --LKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTL 177
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 178 CRLQNTSVLFITHDIAEAVYLADRIAVMAAG---KIVYALDVDLPKPRT-LEMRYEPRFNEL 235
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVPFPRPRDrLEVVEDPSYYDL 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-217 |
2.33e-67 |
|
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: 216.31 E-value: 2.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY----QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPT--LLEWKRVIDNVLLPISL-KRKPAKEDYELAHDLLERVGLSA-YRDHYPAQLSGGQQSRVAMARALI 147
Cdd:COG1123 341 rrrVQMVFQDPYssLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-211 |
8.12e-67 |
|
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: 206.75 E-value: 8.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPIS-LKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-212 |
1.17e-66 |
|
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: 206.03 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlrelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQ-------APTllewkrVIDNVLL-PISLKRkPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRP 150
Cdd:COG1122 81 FQnpddqlfAPT------VEEDVAFgPENLGL-PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 151 ALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-217 |
7.67e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.45 E-value: 7.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----IGYVF 79
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 160 AALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG1131 160 SGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-211 |
1.60e-64 |
|
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: 200.54 E-value: 1.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK---PSSSIGYVFQ 80
Cdd:cd03300 1 IELENVSKFYGG-FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
3.59e-63 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 197.62 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQ 80
Cdd:COG1121 4 MPAIELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLlEWK---RVIDNVLL----PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:COG1121 83 RAEV-DWDfpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-239 |
4.85e-63 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 197.59 E-value: 4.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQAPT 83
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDNVLLPISLKRKPAkedyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 164 AITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVDLPKPRTlemRYEPRFNELSFHV 239
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRR---RGSARLAELEAEV 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-211 |
2.27e-62 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 195.03 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY---QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-------- 72
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 73 SSIGYVFQAP--TLLEWKRVIDNVLLPISLKRKPAKED--YELAHDLLERVGLSAYR-DHYPAQLSGGQQSRVAMARALI 147
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEarKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
2.43e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.66 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrlrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVL--------LPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALI 147
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVF 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-217 |
4.69e-62 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 195.30 E-value: 4.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQAPT 83
Cdd:PRK11248 2 LQISHLYADYGG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 164 AITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMA--AGKIVYALDVD 217
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-211 |
5.50e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 195.37 E-value: 5.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE--KVTKPSSS--IG 76
Cdd:COG1118 1 MS-IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPPRErrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 157 EPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-213 |
9.41e-61 |
|
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: 191.80 E-value: 9.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYV 78
Cdd:COG1120 2 LEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLL---P-ISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-211 |
1.42e-60 |
|
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: 190.79 E-value: 1.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPISLKRK-PAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-217 |
2.22e-60 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 190.40 E-value: 2.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGL---TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-----SI 75
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTL-LEWKRVIDNVLL-PISLKRKPAKEDYelAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:COG1124 82 QMVFQDPYAsLHPRHTVDRILAePLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-209 |
4.22e-60 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 188.44 E-value: 4.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-----SIGYV 78
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPtllEW----KRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:cd03225 81 FQNP---DDqffgPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-211 |
1.16e-59 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 187.46 E-value: 1.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGYVFQ 80
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-211 |
1.87e-59 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 191.40 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGY 77
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQkrdYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-211 |
9.45e-59 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 187.08 E-value: 9.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---------IGYVFQAPTLL 85
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAI 165
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 166 TREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-209 |
2.80e-58 |
|
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: 182.77 E-value: 2.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-------SSIG 76
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpplrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLLPislkrkpakedyelahdllervglsayrdhypaqLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 157 EPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-210 |
8.13e-58 |
|
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: 183.69 E-value: 8.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS---SSIGY 77
Cdd:cd03296 1 MS-IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqeRNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLK----RKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLC-RLQNTSVlFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHdELHVTTV-FVTHDQEEALEVADRVVVMNKGRI 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
4.04e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 189.73 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD---EGAVYLRGEKVTKPS-----SS 74
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSealrgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAP-TLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:COG1123 85 IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD--LPKPRTLE 225
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEeiLAAPQALA 238
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-211 |
5.12e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 181.02 E-value: 5.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipylrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 156 DEPFAALDAITREELqADLL-TLCRLqNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG2884 162 DEPTGNLDPETSWEI-MELLeEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-211 |
5.43e-57 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 181.73 E-value: 5.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSI-------G 76
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 156 DEPFAALDAitreELQADLL-TLCRL--QNTSVLFITHDI--AEAVylADRIAVMAAGKIV 211
Cdd:COG1126 161 DEPTSALDP----ELVGEVLdVMRDLakEGMTMVVVTHEMgfAREV--ADRVVFMDGGRIV 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-210 |
1.27e-56 |
|
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: 179.65 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQApTL 84
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQR-RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LEWK---RVIDNVLL----PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03235 79 IDRDfpiSVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-232 |
3.39e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 179.67 E-value: 3.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS----SSIGYVF 79
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPrearRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 160 AALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVDLPKPRTLEMRYEPRF 232
Cdd:COG4555 161 NGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-217 |
7.83e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 178.41 E-value: 7.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDgvsWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK------PSSSIgy 77
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppaerPVSML-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 vFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG3840 77 -FQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
8.79e-56 |
|
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: 178.40 E-value: 8.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG----LTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS------- 72
Cdd:COG4181 9 IELRGLTKTVGTgageLT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 73 --SSIGYVFQA----PTL--LEwkrvidNVLLPISLKRkpAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMAR 144
Cdd:COG4181 88 raRHVGFVFQSfqllPTLtaLE------NVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 145 ALIQRPALLFLDEPFAALDAITREELqADLL-TLCRLQNTSVLFITHDIAeavyLA---DRIAVMAAGKIV 211
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQI-IDLLfELNRERGTTLVLVTHDPA----LAarcDRVLRLRAGRLV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-210 |
8.99e-56 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.84 E-value: 8.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGY 77
Cdd:PRK09452 12 SPLVELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-211 |
2.75e-55 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 181.20 E-value: 2.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS---------SSIGYVFQAPTLL 85
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelrevrrKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAI 165
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 166 TREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIV 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-212 |
6.07e-55 |
|
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: 176.60 E-value: 6.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPiSLKRKPA---------KEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG-RLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-211 |
1.14e-54 |
|
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: 178.32 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 8 RVTYR-YQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQP---DEGAVYLRGEKVTKPSSS--------- 74
Cdd:COG0444 8 KVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrkirgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQA------PTLlewkRVIDNVLLPISLKRK-PAKEDYELAHDLLERVGLSAYRDH---YPAQLSGGQQSRVAMAR 144
Cdd:COG0444 88 IQMIFQDpmtslnPVM----TVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 145 ALIQRPALLFLDEPFAALDAITreelQADLLTLCR-LQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTI----QAQILNLLKdLQrelGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
1.23e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.62 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:COG4619 1 LELEGLSFRVGG-KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNVLLPISLKRKPAkeDYELAHDLLERVGLSA-YRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKF--DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-211 |
5.55e-54 |
|
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: 173.54 E-value: 5.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 6 LDRVTYRYQ---GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS--------SS 74
Cdd:cd03258 4 LKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrkarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIaEAVY-LADRIAVMAAGKIV 211
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEM-EVVKrICDRVAVMEKGEVV 220
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-210 |
7.93e-54 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 173.45 E-value: 7.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS---SSIGYVFQ 80
Cdd:TIGR00968 1 IEIANISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHardRKIGFVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:TIGR00968 80 HYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:TIGR00968 160 ALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-210 |
1.54e-52 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 169.25 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-------SSIGYVFQAPTLLEWKRVI 91
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninelrQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 92 DNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREEL 170
Cdd:cd03262 95 ENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1215498689 171 QADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:cd03262 175 LDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-210 |
3.14e-51 |
|
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: 164.49 E-value: 3.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----IGYVF 79
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVllpislkrkpakedyelahdllervglsayrdhypaQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 160 AALDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:cd03230 124 SGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-211 |
9.54e-51 |
|
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: 165.59 E-value: 9.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KPSS-SIGYVFQAPTLLEWKRVIDNVL 95
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlPPEKrDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 96 LPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLL 175
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1215498689 176 TLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-211 |
1.81e-50 |
|
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: 165.60 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLEWKRVIDNVLLPISLK---------------RKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSR 139
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARlgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 140 VAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIaEAVY-LADRIAVMAAGKIV 211
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVMgLADRIVVLDFGRVI 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-212 |
1.90e-50 |
|
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: 165.68 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS------SSIG 76
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPtllewkrviDNVLLPISL----------KRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:TIGR04520 81 MVFQNP---------DNQFVGATVeddvafglenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVyLADRIAVMAAGKIVY 212
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVA 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-211 |
2.44e-50 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 164.53 E-value: 2.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiarlgIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLK----------RKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALI 147
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARtgsglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 148 QRPALLFLDEPFAALDAITREELqADLLTLCRLQNTSVLFITHDIaEAVY-LADRIAVMAAGKIV 211
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDM-DVVMsLADRVTVLDQGRVI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-213 |
8.82e-50 |
|
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: 162.46 E-value: 8.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 29 EGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG-------EKVTKPSS--SIGYVFQAPTLLEWKRVIDNVLLpiS 99
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQqrKIGLVFQQYALFPHLNVRENLAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 100 LKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCR 179
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....
gi 1215498689 180 LQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-212 |
1.19e-49 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 162.85 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS--------SSI 75
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPiSLKRKPA---------KEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHG-RLGYKPTwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVF 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-211 |
2.36e-48 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 162.28 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS---SIGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYEL 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPhlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 112 AHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHD 191
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|
gi 1215498689 192 IAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIA 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-213 |
4.39e-48 |
|
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: 159.09 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGA-VYLRGEKVTKPS-----SS 74
Cdd:COG1119 1 DPLLELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDvwelrKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVfqAPTLLEWKRVIDNVL-LPIS-------LKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:COG1119 80 IGLV--SPALQLRFPRDETVLdVVLSgffdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-212 |
6.15e-48 |
|
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: 157.67 E-value: 6.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT----KPSSSIGYV 78
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdrkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 159 FAALDAITREELQADLLTLcrLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-211 |
6.74e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 161.40 E-value: 6.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQ---GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:COG1135 2 IELENLSKTFPtkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 --IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:COG1135 82 rkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 153 LFLDEPFAALD-AITREELqaDLLTlcRLQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1135 162 LLCDEATSALDpETTRSIL--DLLK--DINrelGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-212 |
8.10e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 159.15 E-value: 8.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG--------EKVTKP 71
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 SSSIGYVFQAP--TLLEwKRVIDNVLL-PISLKrKPAKEDYELAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARALI 147
Cdd:TIGR04521 81 RKKVGLVFQFPehQLFE-ETVYKDIAFgPKNLG-LSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVL 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-211 |
1.48e-47 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 160.65 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 8 RVTYRYQGLTpvIDgVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-------KVTKPSS--SIGYV 78
Cdd:COG4148 6 DFRLRRGGFT--LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsarGIFLPPHrrRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLpiSLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:COG4148 83 FQEARLFPHLSVRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 159 FAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-210 |
2.02e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 160.25 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTyRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS---SIGY 77
Cdd:PRK10851 1 MS-IEIANIK-KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHArdrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISL----KRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLCR-LQNTSVlFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEeLKFTSV-FVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-211 |
3.00e-47 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 155.97 E-value: 3.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG---LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:TIGR02211 2 LKCENLGKRYQEgklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLaDRIAVMAAGKIV 211
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-211 |
8.64e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 158.73 E-value: 8.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 2 SFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS---SSIGYV 78
Cdd:PRK11432 5 NFVVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 159 FAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-209 |
1.88e-46 |
|
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: 152.15 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGY 77
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNVLlpislkrkpakedyelahdllervglsayrdhypaqlSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03228 81 VPQDPFLFS-GTIRENIL-------------------------------------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 158 PFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGK 209
Cdd:cd03228 123 ATSALDPETEALILEALRAL--AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-211 |
2.93e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.82 E-value: 2.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 21 DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------IGYVFQAP--TLLEWKRV 90
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrplrrrMQMVFQDPyaSLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDNVLLPISL-KRKPAKEDYELAHDLLERVGLSA-YRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAitre 168
Cdd:COG4608 115 GDIIAEPLRIhGLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV---- 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1215498689 169 ELQADLLTL-CRLQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4608 191 SIQAQVLNLlEDLQdelGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-209 |
9.71e-46 |
|
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: 150.09 E-value: 9.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYVF 79
Cdd:cd00267 1 EIENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelrrrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QaptllewkrvidnvllpislkrkpakedyelahdllervglsayrdhypaqLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 160 AALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:cd00267 109 SGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-211 |
9.87e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 161.93 E-value: 9.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG---EKVTKPS--SSIGY 77
Cdd:COG2274 474 IELENVSFRYPGDSpPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNvllpISLKRKPAkeDYELAHDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARAL 146
Cdd:COG2274 554 VLQDVFLFS-GTIREN----ITLGDPDA--TDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHDiAEAVYLADRIAVMAAGKIV 211
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHR-LSTIRLADRIIVLDKGRIV 688
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
1.76e-45 |
|
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: 150.28 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYVF 79
Cdd:cd03214 1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKelarkIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAptllewkrvidnvllpislkrkpakedyelahdlLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03214 80 QA----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 160 AALDaITReelQADLL----TLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:cd03214 126 SHLD-IAH---QIELLellrRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
4-211 |
3.21e-45 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 155.15 E-value: 3.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD--EGAVYLRGEKVTKP---SSSIGYV 78
Cdd:TIGR03258 6 IRIDHLRVAYGANT-VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHApphKRGLALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:TIGR03258 85 FQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 159 FAALDAITREELQADLLTLC-RLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR03258 165 LSALDANIRANMREEIAALHeELPELTILCVTHDQDDALTLADKAGIMKDGRLA 218
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
19-211 |
5.64e-45 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 150.17 E-value: 5.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG--------EKVTKPSSSIGYVFQAPTLLEWKRV 90
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGqelhgaskKQLVQLRRRIGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDNVLLPISLKRK-PAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREE 169
Cdd:TIGR02982 100 RQNVQMALELQPNlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1215498689 170 LQADLLTLCRLQNTSVLFITHD--IAEavyLADRIAVMAAGKIV 211
Cdd:TIGR02982 180 VVELMQKLAKEQGCTILMVTHDnrILD---VADRILQMEDGKLL 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-211 |
7.61e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 153.42 E-value: 7.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTPVI---DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-------- 73
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 74 SIGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 154 FLDEPFAALD-AITREELqaDLLT-LCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11153 163 LCDEATSALDpATTRSIL--ELLKdINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
1.96e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 148.87 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLL-----QPDEGAVYLRGEKVTKPSS----- 73
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 74 --SIGYVFQAPTLLeWKRVIDNVLLPISLKR-KPAKEDYELAHDLLERVGLSAY--RDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:cd03260 80 rrRVGMVFQKPNPF-PGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELQADLLTLCRlqNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-160 |
4.09e-43 |
|
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: 143.17 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYVFQAPTLLEWKRVIDNV 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 LLPISLKRKPAKEDYELAHDLLERVGLSAYRDH----YPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-211 |
6.19e-43 |
|
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: 152.60 E-value: 6.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYV 78
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWkRVIDNVLLPislkrKPAKEDYELaHDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARALI 147
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLG-----RPDASDEEL-EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRlqNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLA-LLAQADRILVLDDGRIV 550
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-213 |
7.99e-43 |
|
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: 144.56 E-value: 7.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDgvsWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT------KPSSSigy 77
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaappadRPVSM--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-191 |
1.38e-42 |
|
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: 143.77 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----IGYVF 79
Cdd:COG4133 3 LEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAP------TLLEWkrvidnvlLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:COG4133 82 HADglkpelTVREN--------LRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1215498689 154 FLDEPFAALDAITREELqADLLTLCRLQNTSVLFITHD 191
Cdd:COG4133 154 LLDEPFTALDAAGVALL-AELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-211 |
3.09e-42 |
|
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: 143.28 E-value: 3.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPViDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS----SIGYVF 79
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRevrrRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 160 AALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-210 |
6.17e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.14 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KPSS-SIGY 77
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNelEPADrDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNvlLPISLK-RKPAKEDYEL----AHDLLErvgLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:PRK11650 81 VFQNYALYPHMSVREN--MAYGLKiRGMPKAEIEErvaeAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-211 |
1.23e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.23 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 2 SFLQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSI 75
Cdd:PRK13635 4 EIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAP-------TllewkrVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK13635 84 GMVFQNPdnqfvgaT------VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-211 |
2.79e-41 |
|
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: 148.38 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGY 77
Cdd:COG4987 334 LELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAP-----TLLewkrviDNVLLPislkrKPAKEDYELAhDLLERVGLSAYRDHYP-----------AQLSGGQQSRVA 141
Cdd:COG4987 414 VPQRPhlfdtTLR------ENLRLA-----RPDATDEELW-AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 142 MARALIQRPALLFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHDiAEAVYLADRIAVMAAGKIV 211
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHR-LAGLERMDRILVLEDGRIV 548
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-211 |
7.99e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.82 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE---KVTKPSSSIGYVFQ 80
Cdd:PRK11607 20 LEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlsHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-191 |
8.40e-41 |
|
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: 139.47 E-value: 8.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAV--------YLRGEKVTKPSSSIGYVFQ 80
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsDLRGRAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELqADLLTLCRLQNTSVLFITHD 191
Cdd:cd03292 166 NLDPDTTWEI-MNLLKKINKAGTTVVVATHA 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-240 |
8.92e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 140.23 E-value: 8.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSI-------G 76
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 156 DEPFAALDAITREELQADLLTLCRLQNTSVLfITHDIAEAVYLADRIAVMAAGKIVyaldVDLPKPRTLEMRYEPRFNEL 235
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIA----EDGDPQVLIKNPPSQRLQEF 235
|
....*
gi 1215498689 236 SFHVR 240
Cdd:PRK09493 236 LQHVS 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-211 |
1.20e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.77 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD---EGAVYLRGEKVTK-PSSS--IGY 77
Cdd:COG4136 2 LSLENLTITLGG-RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlPAEQrrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVL--LPISLKRKPAKEdyeLAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAfaLPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 156 DEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVyladriavmAAGKIV 211
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP---------AAGRVL 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-212 |
2.85e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.56 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDgvsWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGYVFQ 80
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALI-QRPALLfLDEPF 159
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVrEQPILL-LDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 160 AALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAW 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-210 |
5.12e-40 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 137.30 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDgvsWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGYVFQ 80
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFD---LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYqrpVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 161 ALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-211 |
6.80e-40 |
|
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: 136.62 E-value: 6.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP--SSSIGYVFQAP 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 T--LLEwkrviDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03226 81 DyqLFT-----DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 161 ALDAITREELqADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03226 156 GLDYKNMERV-GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-227 |
3.84e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.71 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG---LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:PRK11629 6 LQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK11629 86 nqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAeavyLADRIAvmaagkivyaldvdlpkpRTLEMR 227
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ----LAKRMS------------------RQLEMR 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-212 |
7.61e-39 |
|
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: 134.24 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGeFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----IGYVF 79
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 160 AALDAITREELQaDLLTlcRL-QNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03264 159 AGLDPEERIRFR-NLLS--ELgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-211 |
3.21e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 137.47 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---------IGYVFQAPTLL 85
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrrkkIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAI 165
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 166 TREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-212 |
3.98e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 132.56 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQA----PTLlewkRVIDNVLLPIS-LKRKPAKEDYELAHDLLERvgLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:cd03224 80 VPEGrrifPEL----TVEENLLLGAYaRRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQnTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVL 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-211 |
6.50e-38 |
|
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: 131.63 E-value: 6.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-KPSSSIGYVFQAP 82
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 TLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAAL 162
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1215498689 163 DAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03269 160 DPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-213 |
9.27e-38 |
|
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: 131.90 E-value: 9.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-PSS-----SIGY 77
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHkrarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 158 PFAALDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-211 |
9.58e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.57 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVY-----------LRGEK-- 67
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarsLSQQKgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 68 VTKPSSSIGYVFQAPTLLEWKRVIDNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 147 IQRPALLFLDEPFAALDAitreELQADLLTLCRL---QNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11264 160 AMRPEVILFDEPTSALDP----ELVGEVLNTIRQlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
2.26e-37 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 128.70 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarragIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFqaptllewkrvidnvllpislkrkpakedyelahdllervglsayrdhypaQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03216 80 VY---------------------------------------------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-231 |
2.94e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.30 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 3 FLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IG 76
Cdd:COG1129 4 LLEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLLPISLKRKPA---KEDYELAHDLLERVGLsayrDHYPAQ----LSGGQQSRVAMARALIQR 149
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGL----DIDPDTpvgdLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 150 PALLFLDEPFAALdaiTREELQAdLLTLCRL---QNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV-DLPKP---- 221
Cdd:COG1129 159 ARVLILDEPTASL---TEREVER-LFRIIRRlkaQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVaELTEDelvr 234
|
250
....*....|....
gi 1215498689 222 ----RTLEMRYEPR 231
Cdd:COG1129 235 lmvgRELEDLFPKR 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-217 |
3.34e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.15 E-value: 3.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-KPSSSIGYvfqap 82
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpEDRRRIGY----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 tLLE-------WKrVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:COG4152 76 -LPEerglypkMK-VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 156 DEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-211 |
4.51e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.83 E-value: 4.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG---EKVTKPS--SSIGYV 78
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESlrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNvllpISLKRKPAKEDyEL--------AHDLLER--------VGLSAYRdhypaqLSGGQQSRVAM 142
Cdd:COG1132 420 PQDTFLFS-GTIREN----IRYGRPDATDE-EVeeaakaaqAHEFIEAlpdgydtvVGERGVN------LSGGQRQRIAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 143 ARALIQRPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLS-TIRNADRILVLDDGRIV 553
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-216 |
4.67e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 131.08 E-value: 4.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 2 SFLQLDRVTYRYQ--------GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK--P 71
Cdd:TIGR02769 1 SLLEVRDVTHTYRtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 SS------SIGYVFQ-APTLLEWKRVIDNVLL-PI-SLKRKPAKEDYELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVA 141
Cdd:TIGR02769 81 KQrrafrrDVQLVFQdSPSAVNPRMTVRQIIGePLrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 142 MARALIQRPALLFLDEPFAALDAItreeLQADLLTLCR-LQN---TSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV 216
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMV----LQAVILELLRkLQQafgTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
9.00e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.50 E-value: 9.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:PRK13632 9 KVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlkeirKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPtllewkrviDNVLLPISL----------KRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK13632 89 FQNP---------DNQFIGATVeddiafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 149 RPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVyLADRIAVMAAGKIVY 212
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-211 |
2.17e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.82 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRY-----QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG------EKVTKPSSSIGY 77
Cdd:PRK13633 10 VSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAP------TLLEWkrviDNVLLPISLKRKPaKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK13633 90 VFQNPdnqivaTIVEE----DVAFGPENLGIPP-EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
3.96e-36 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 126.95 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS---IGYVFQ 80
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrrIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKRKPAKEdyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 161 ALDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03268 156 GLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-217 |
7.08e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.84 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:COG3845 6 LELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaialgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLL------PISLKRKPAKEDyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLgleptkGGRLDRKAARAR---IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-211 |
2.10e-35 |
|
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: 131.73 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 21 DGVSWTINEGEFHCLVGKSGCGKTTLlklaaGL----LQPDEGAVYLRGEKVTKPSSS--------IGYVFQAP------ 82
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTL-----GLallrLIPSEGEIRFDGQDLDGLSRRalrplrrrMQVVFQDPfgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 ------TLLEWKRVidnvlLPISLKRKpakEDYELAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:COG4172 378 rmtvgqIIAEGLRV-----HGPGLSAA---ERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 156 DEPFAALDAITreelQADLLTLCR-LQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4172 450 DEPTSALDVSV----QAQILDLLRdLQrehGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-211 |
2.16e-35 |
|
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: 125.39 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGL-TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK--PS---SSIGY 77
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLeWKRVIDNVLLpislkRKPAKEDYELAhDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARAL 146
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITL-----GAPLADDERIL-RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-191 |
2.80e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 125.66 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK---------PSSSIGYVFQAPTLLEWKR 89
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearaklRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 VIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREE 169
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|...
gi 1215498689 170 LqADLL-TLCRLQNTSVLFITHD 191
Cdd:PRK10584 185 I-ADLLfSLNREHGTTLILVTHD 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-210 |
3.00e-35 |
|
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: 123.48 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGY 77
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNVllpislkrkpakedyelahdllervglsayrdhypaqLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03246 81 LPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 158 PFAALDaITREELQADLLTLCRLQNTSVLFITHDIaEAVYLADRIAVMAAGKI 210
Cdd:cd03246 123 PNSHLD-VEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-211 |
3.59e-35 |
|
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: 131.35 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLTPVIDGVSWTINEGEFHCLVGKSGCGKT----TLLKLAAGLLQPDEGAVYLRGEKVTKPS---------SSIGYVFQ 80
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSerelrrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 AP-TLLewkrvidNVLLPI------------SLKRKPAKEdyeLAHDLLERVGL--SAYR-DHYPAQLSGGQQSRVAMAR 144
Cdd:COG4172 100 EPmTSL-------NPLHTIgkqiaevlrlhrGLSGAAARA---RALELLERVGIpdPERRlDAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 145 ALIQRPALLFLDEPFAALDAITreelQADLLTLCR-LQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTV----QAQILDLLKdLQrelGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-205 |
3.59e-35 |
|
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: 131.25 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYV 78
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswrdqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNVLLpislkRKPAKEDYELAhDLLERVGL----SAYRDHY-------PAQLSGGQQSRVAMARALI 147
Cdd:TIGR02857 402 PQHPFLFA-GTIAENIRL-----ARPDASDAEIR-EALERAGLdefvAALPQGLdtpigegGAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHDIAEAvYLADRIAVM 205
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-211 |
4.55e-35 |
|
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: 125.03 E-value: 4.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG---EKVTKPS--SSIGYVFQAPT 83
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSlrSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEwKRVIDNvllpISLKRKPAKEDYEL-------AHDLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:cd03254 88 LFS-GTIMEN----IRLGRPNATDEEVIeaakeagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-210 |
5.11e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.14 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-P-----SSS 74
Cdd:COG1137 1 MMTLEAENLVKSYGK-RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPmhkraRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLewkR---VIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:COG1137 80 IGYLPQEASIF---RkltVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLcRLQNTSVLfIT-HDIAEAVYLADRIAVMAAGKI 210
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVL-ITdHNVRETLGICDRAYIISEGKV 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-210 |
1.12e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.53 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV-TKPS---------- 72
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDrdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 73 -------SSIGYVFQAPTLLEWKRVIDNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMAR 144
Cdd:COG4598 88 rqlqrirTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 145 ALIQRPALLFLDEPFAALDAitreELQADLLTLCR---LQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDP----ELVGEVLKVMRdlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-210 |
1.67e-34 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 126.77 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-------KVTKPSS--SIGYVFQAPTLLEWKRVIDNvlLPISLKRKPA 105
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkGIFLPPEkrRIGYVFQEARLFPHLSVRGN--LRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 106 KEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSV 185
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185
|
170 180
....*....|....*....|....*
gi 1215498689 186 LFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-211 |
2.35e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 129.99 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 3 FLQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IG 76
Cdd:TIGR03375 463 EIEFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlrrnIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKrVIDNVLLpislkRKPAKEDYELAhDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARA 145
Cdd:TIGR03375 543 YVPQDPRLFYGT-LRDNIAL-----GAPYADDEEIL-RAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 146 LIQRPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRW--LAGKTLVLVTHRTS-LLDLVDRIIVMDNGRIV 678
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-211 |
3.26e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 123.34 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KP---------- 71
Cdd:PRK13548 3 LEARNLSVRLGG-RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPaelarrravl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 --SSSIGYVFqaptllewkRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ- 148
Cdd:PRK13548 82 pqHSSLSFPF---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 149 -----RPALLFLDEPFAALDaitreeL--QADLLTL----CRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALD------LahQHHVLRLarqlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-210 |
1.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.53 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLT--PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----S 73
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 74 SIGYVFQAP-TLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEaVYLADRIAVMAAGKI 210
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-212 |
1.93e-33 |
|
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: 120.86 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:COG0410 1 MPMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYV------FqaPTLlewkRVIDNVLLPISLKRKPA--KEDYELAHDLLERvgLSAYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:COG0410 80 IGYVpegrriF--PSL----TVEENLLLGAYARRDRAevRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVL 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-210 |
2.27e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 123.99 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK--PSS-SIGY 77
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvpPAErGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLPISL---------KR-KPAKEDYELAHdLLERvglsayrdhYPAQLSGGQQSRVAMARALI 147
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLagakkeeinQRvNQVAEVLQLAH-LLDR---------KPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
3.19e-33 |
|
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: 119.78 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVI---DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP----SSSIG 76
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEpaeaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLL---PISLKRKPAKEDYElahDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYfagLYGLKGDELTARLE---ELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-211 |
4.36e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.95 E-value: 4.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQ--------GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS 72
Cdd:PRK10419 1 MTLLNVSGLSHHYAhgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 73 SS--------IGYVFQ-APTLLEWKRVIDNVLL-PIS-LKRKPAKEDYELAHDLLERVGLSA-YRDHYPAQLSGGQQSRV 140
Cdd:PRK10419 81 RAqrkafrrdIQMVFQdSISAVNPRKTVREIIRePLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 141 AMARALIQRPALLFLDEPFAALDAItreeLQADLLTLC-RLQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLV----LQAGVIRLLkKLQqqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-248 |
8.63e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.51 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 6 LDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrGEKVTKPSSS------- 74
Cdd:PRK13634 5 FQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklkpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAP--TLLEWKRVIDNVLLPIS--LKRKPAKEdyeLAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARAL 146
Cdd:PRK13634 84 rkkVGIVFQFPehQLFEETVEKDICFGPMNfgVSEEDAKQ---KAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV--------------- 211
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFlqgtpreifadpdel 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1215498689 212 YALDVDLPK----PRTLEMRYEPRFN-------ELSFHVRQAMEGVKR 248
Cdd:PRK13634 241 EAIGLDLPEtvkfKRALEEKFGISFPkpcltleELAHEVVQLLRKGGH 288
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-203 |
1.72e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 6 LDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRgekvtkPSSSIGYVFQAPTLL 85
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EWKRVIDNVLLPIS-----------LKRKPAKEDYEL---------------------AHDLLERVGLSAyRDHY--PAQ 131
Cdd:COG0488 74 DDLTVLDTVLDGDAelraleaeleeLEAKLAEPDEDLerlaelqeefealggweaearAEEILSGLGFPE-EDLDrpVSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 132 LSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQAdllTLCRLQNTsVLFITHDiaeaVYLADRIA 203
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEE---FLKNYPGT-VLVVSHD----RYFLDRVA 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-211 |
2.56e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-- 74
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 -----IGYVFQAP--TLLEWKRVIDNVLLPISLKRKpAKEDYELAHDLLERVGLS--AYRDHYPAQLSGGQQSRVAMARA 145
Cdd:PRK13637 80 dirkkVGLVFQYPeyQLFEETIEKDIAFGPINLGLS-EEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 146 LIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-211 |
2.69e-32 |
|
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: 117.72 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE---KVTKPS--SSIGYV 78
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwkrviDNVLLPISLKRKPAKED--YELA-----HDLLERvglsaYRDHYPAQ-------LSGGQQSRVAMAR 144
Cdd:cd03253 81 PQDTVLFN-----DTIGYNIRYGRPDATDEevIEAAkaaqiHDKIMR-----FPDGYDTIvgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 145 ALIQRPALLFLDEPFAALDAITREELQADLLTLCRlqNTSVLFITHDIAEaVYLADRIAVMAAGKIV 211
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-211 |
5.29e-32 |
|
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: 117.26 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAPTLLEwKRVID 92
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NvllpISLKRKPAKEDYE-------LAHDLLE--------RVGlsayrDHYpAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:cd03249 96 N----IRYGKPDATDEEVeeaakkaNIHDFIMslpdgydtLVG-----ERG-SQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 158 PFAALDAITREELQADLLTLCRlqNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-217 |
5.52e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-----KPSSSIGYVFQAP--------TLL 85
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeyKRAKYIGRVFQDPmmgtapsmTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EwkrvidNVLL------PISLKRKPAKEDYELAHDLLERVGLS-AYRDHYPA-QLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG1101 101 E------NLALayrrgkRRGLRRGLTKKRRELFRELLATLGLGlENRLDTKVgLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 158 PFAALD--------AITREELQADLLTlcrlqntsVLFITHDIAEAVYLADRIAVMAAGKIVyaLDVD 217
Cdd:COG1101 175 HTAALDpktaalvlELTEKIVEENNLT--------TLMVTHNMEQALDYGNRLIMMHEGRII--LDVS 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-194 |
5.86e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.74 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KPSS---SIGYV 78
Cdd:PRK10247 8 LQLQNVGYLAGD-AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIyrqQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNVLLPISLkRKPAKEDYELAHDlLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:PRK10247 87 AQTPTLFG-DTVYDNLIFPWQI-RNQQPDPAIFLDD-LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAE 194
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-205 |
7.58e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 12 RYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekVTKPSSSIGYVFQApTLLEWK--- 88
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------RRAGGARVAYVPQR-SEVPDSlpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RVIDNVLL----PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:NF040873 73 TVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1215498689 165 ITREELqADLLTLCRLQNTSVLFITHDiAEAVYLADRIAVM 205
Cdd:NF040873 153 ESRERI-IALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-212 |
1.17e-31 |
|
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: 116.28 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAV----YLRGEKVTKPSSSIGYVFQAPTLLEWK-RVID 92
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRRIGVVFGQKTQLWWDlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQA 172
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1215498689 173 DLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-211 |
1.18e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 121.45 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY----QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLR-GEK---VTKP---- 71
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 ----SSSIGYVFQAPTLLEWKRVIDNVLLPISLKRkPAKEDYELAHDLLERVGLSAYR-----DHYPAQLSGGQQSRVAM 142
Cdd:TIGR03269 360 rgraKRYIGILHQEYDLYPHRTVLDNLTEAIGLEL-PDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 143 ARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-211 |
1.34e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 118.14 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS--------SSIGYVFQAP--TLLEWKR 89
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaqkllrQKIQIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 VIDNVLLPISLKRK-PAKEDYELAHDLLERVGLSA-YRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAitr 167
Cdd:PRK11308 111 VGQILEEPLLINTSlSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV--- 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1215498689 168 eELQADLLTL-CRLQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11308 188 -SVQAQVLNLmMDLQqelGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-191 |
5.28e-31 |
|
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: 119.77 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYV 78
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrrVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNVLLPislkrKPAKEDYELAhDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARALI 147
Cdd:TIGR02868 415 AQDAHLFD-TTVRENLRLA-----RPDATDEELW-AALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHD 191
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-211 |
8.96e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.43 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------I 75
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpflrrqI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 156 DEPFAALDaitrEELQADLLTLCRLQN---TSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10908 162 DEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-211 |
1.01e-30 |
|
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: 112.02 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP----SSSIGYV 78
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPtllewkrvidnvllpislkrkpakedYELAHDLLERVGlsayrdhypAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:cd03247 81 NQRP--------------------------YLFDTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 159 FAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03247 126 TVGLDPITERQLLSLIFEV--LKDKTLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-211 |
1.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.40 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 11 YRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-------IGYVFQ--- 80
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktVGIVFQnpd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 ----APTLLEwkrviDNVLLPISLKRkPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK13639 89 dqlfAPTVEE-----DVAFGPLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 157 EPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-209 |
2.64e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.16 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPViDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-KPSSSI---GYV- 78
Cdd:PRK11300 6 LSVSGLMMRFGGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIarmGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 -FQAPTLLEWKRVIDNVL-----------LPISLK----RKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAM 142
Cdd:PRK11300 85 tFQHVRLFREMTVIENLLvaqhqqlktglFSGLLKtpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 143 ARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-211 |
4.77e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQ---GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------ 74
Cdd:PRK10535 5 LELKDIRRSYPsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ---IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK10535 85 rehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-211 |
1.01e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV---TKPSSS--- 74
Cdd:COG4161 1 MS-IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 -----IGYVFQAPTLLEWKRVIDNVL-LPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:COG4161 79 llrqkVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 149 RPALLFLDEPFAALDAitreELQADLLTLCR-LQNTSV--LFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4161 159 EPQVLLFDEPTAALDP----EITAQVVEIIReLSQTGItqVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-211 |
1.07e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV---TKPSSS--- 74
Cdd:PRK11124 1 MS-IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 -----IGYVFQAPTLLEWKRVIDNVL-LPI---SLKRKPAKEDyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARA 145
Cdd:PRK11124 79 elrrnVGMVFQQYNLWPHLTVQQNLIeAPCrvlGLSKDQALAR---AEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 146 LIQRPALLFLDEPFAALDAitreELQADLLTLCR-LQNTSV--LFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDP----EITAQIVSIIReLAETGItqVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-211 |
1.13e-29 |
|
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: 111.04 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVI-DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGY 77
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlrrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNVLLP---ISLKRKPAKEDYELAHDLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:cd03252 81 VLQENVLFN-RSIRDNIALAdpgMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-219 |
1.85e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGA--------VYLRGEKVTKPSSSIGYVFQAP-TLLEWK 88
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIREKVGIVFQNPdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITRE 168
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 169 ELQADLLTLCRLQNTSVLFITHDIAEAVyLADRIAVMAAGKIvyaLDVDLP 219
Cdd:PRK13640 181 QILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL---LAQGSP 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-210 |
3.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 2 SFLQLDRVTYRYQGLTP-VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----I 75
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrkhI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPtllEWKRVIDNVLLPISLKRK----PAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK13648 86 GIVFQNP---DNQFVGSIVKYDVAFGLEnhavPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYlADRIAVMAAGKI 210
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-236 |
3.99e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.02 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG--------EKVTKP 71
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 -SSSIGYVFQAP--TLLEwkrviDNVLLPISLKRK----PAKEDYELAHDLLERVGLSayRD---HYPAQLSGGQQSRVA 141
Cdd:PRK13646 83 vRKRIGMVFQFPesQLFE-----DTVEREIIFGPKnfkmNLDEVKNYAHRLLMDLGFS--RDvmsQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 142 MARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV---------- 211
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVsqtspkelfk 235
|
250 260 270
....*....|....*....|....*....|....
gi 1215498689 212 ---YALD--VDLPK----PRTLEMRYEPRFNELS 236
Cdd:PRK13646 236 dkkKLADwhIGLPEivqlQYDFEQKYQTKLKDIA 269
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-217 |
4.40e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 109.38 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD----EGAVYLRGeKVTKPSS----SIGYVFQAP-TLLEWKRV 90
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDG-RPLLPLSirgrHIATIMQNPrTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDNVLL-PISLKRKPAKEDYELAHDLLERVGLSAYR---DHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAIT 166
Cdd:TIGR02770 81 MGNHAIeTLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 167 REELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVK 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-211 |
4.47e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPV--IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIG 76
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnlrRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAP-TLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 156 DEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-211 |
4.62e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS------SSIGY 77
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklqgirKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVI--------DNVLLPISLKRKpaKEDYELAhdlleRVGLSAYRDHYPAQLSGGQQSRVAMARALIQR 149
Cdd:PRK13644 82 VFQNPETQFVGRTVeedlafgpENLCLPPIEIRK--RVDRALA-----EIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 150 PALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIaEAVYLADRIAVMAAGKIV 211
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNL-EELHDADRIIVMDRGKIV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-211 |
8.13e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.50 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 37 GKSGCGKTTLLKLAAGLLQPDEGAVYLrGEKVTKPSSS----------IGYVFQAPTLLEWKRVIDNvllpisLKRKPAK 106
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKgiclppekrrIGYVFQDARLFPHYKVRGN------LRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 107 EDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVL 186
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPIL 183
|
170 180
....*....|....*....|....*
gi 1215498689 187 FITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11144 184 YVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
2.68e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPT-LLEWKRVIDNVLL-PISLKRKPaKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK13647 85 FQDPDdQVFSSTVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 157 EPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVDL 218
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-210 |
2.97e-28 |
|
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: 105.59 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLT--PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGYV----FQA 81
Cdd:cd03215 8 RGLSvkGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdairagIAYVpedrKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 82 PTLLEWkRVIDNVLLPIslkrkpakedyelahdllervglsayrdhypaQLSGGQQSRVAMARALIQRPALLFLDEPFAA 161
Cdd:cd03215 88 GLVLDL-SVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1215498689 162 LDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:cd03215 135 VDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-208 |
3.41e-28 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 106.75 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLR--GEKVTKPSSS-----------IGYVFQaptL 84
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQASpreilalrrrtIGYVSQ---F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LewkRVI------DNVLLPISLKRKPAKEDYELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:COG4778 102 L---RVIprvsalDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 158 PFAALDAITREELqADLLTLCRLQNTSVLFITHDIA--EAVylADRIAVMAAG 208
Cdd:COG4778 179 PTASLDAANRAVV-VELIEEAKARGTAIIGIFHDEEvrEAV--ADRVVDVTPF 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
5.69e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.40 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLR----GEKVTKPSSS-----------------IGY 77
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELItnpyskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVI--DNVLLPISLKrKPAKEDYELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK13631 121 VFQFPEYQLFKDTIekDIMFGPVALG-VKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQaDLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-211 |
6.03e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.04 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLaagL-----LQPD---EGAVYLRGEKVTKPS--- 72
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRC---LnrmndLIPGarvEGEILLDGEDIYDPDvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 73 ----SSIGYVFQAPTLLEwKRVIDNVLLPISL--KRKPAKEDyELAHDLLERVGL----------SAYRdhypaqLSGGQ 136
Cdd:COG1117 88 velrRRVGMVFQKPNPFP-KSIYDNVAYGLRLhgIKSKSELD-EIVEESLRKAALwdevkdrlkkSALG------LSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 137 QSRVAMARALIQRPALLFLDEPFAALDAI-TR--EELqadLLTLCrlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPIsTAkiEEL---ILELK--KDYTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-246 |
1.31e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRvtyryqgltPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGY--- 77
Cdd:PRK11831 13 VSFTRGNR---------CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 -----VFQAPTLLEWKRVIDNVLLPIslkRKPAKEDYELAHDL----LERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK11831 84 krmsmLFQSGALFTDMNVFDNVAYPL---REHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 149 RPALLFLDEPFAALDAITR-------EELQADLLTLCrlqntsvLFITHDIAEAVYLADRIAVMAAGKIVYAldvdlPKP 221
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMgvlvkliSELNSALGVTC-------VVVSHDVPEVLSIADHAYIVADKKIVAH-----GSA 228
|
250 260
....*....|....*....|....*
gi 1215498689 222 RTLEMRYEPRfnelsfhVRQAMEGV 246
Cdd:PRK11831 229 QALQANPDPR-------VRQFLDGI 246
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-211 |
1.42e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 110.22 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-----KPSSSIGY 77
Cdd:COG4618 331 LSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNvllpISLKRKPAKEDYELA------HDLLER--------VGLSAyrdhypAQLSGGQQSRVAMA 143
Cdd:COG4618 411 LPQDVELFD-GTIAEN----IARFGDADPEKVVAAaklagvHEMILRlpdgydtrIGEGG------ARLSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 144 RALIQRPALLFLDEPFAALDAITREELQADLLTLcRLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-210 |
1.98e-27 |
|
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: 104.86 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 10 TYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAPTL 84
Cdd:cd03248 20 AYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LEwKRVIDNV---LLPISLKRKPAKEDYELAHDLLERVGLSAYRD--HYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03248 100 FA-RSLQDNIaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 160 AALDAITREELQADLltLCRLQNTSVLFITHDIaEAVYLADRIAVMAAGKI 210
Cdd:cd03248 179 SALDAESEQQVQQAL--YDWPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-212 |
5.69e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.55 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAV--YLRGEKVTKPSSS-------- 74
Cdd:PRK13651 8 IVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEkekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 -------------------IGYVFQAPTLLEWKRVI--DNVLLPISLKRKPaKEDYELAHDLLERVGLS-AYRDHYPAQL 132
Cdd:PRK13651 88 viqktrfkkikkikeirrrVGVVFQFAEYQLFEQTIekDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDeSYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 133 SGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELqADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-211 |
6.38e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYlRGEKVTkpsssIGYVFQAPT 83
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETVK-----IGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEW-KRVIDNVllpislkRKPAKEDYEL-AHDLLERVGLSAYRDHYP-AQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:COG0488 389 ELDPdKTVLDEL-------RDGAPGGTEQeVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 161 ALDAITREELQaDLL-----TlcrlqntsVLFITHDIA--EAVylADRIAVMAAGKIV 211
Cdd:COG0488 462 HLDIETLEALE-EALddfpgT--------VLLVSHDRYflDRV--ATRILEFEDGGVR 508
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
6.61e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV-------TKPSSSIG 76
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAP--TLLEWKRVIDNVLLPISLKRkPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
1.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSI 75
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirevrKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVI--DNVLLPISLkrkpAKEDYELAH---DLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRP 150
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVeqDIAFGPINL----GLDEETVAHrvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 151 ALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-213 |
1.16e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.99 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHeraragIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQA----PTLlewkRVIDNVL-----LPISLKRKPAkEDYEL---AHDLLERVGlsayrdhypAQLSGGQQSRVAMARA 145
Cdd:TIGR03410 80 VPQGreifPRL----TVEENLLtglaaLPRRSRKIPD-EIYELfpvLKEMLGRRG---------GDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 146 LIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVAS 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-211 |
1.27e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.06 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----- 74
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 ----IGYVFQAPtllEWKRVIDNVLLPISLKRKP---AKEDYE-LAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARA 145
Cdd:PRK13649 83 irkkVGLVFQFP---ESQLFEETVLKDVAFGPQNfgvSQEEAEaLAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 146 LIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLfITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-211 |
1.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSfLQLDRVTYRYQGLTPV----IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-- 74
Cdd:PRK13641 1 MS-IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 -------IGYVFQAP--TLLEwKRVIDNVLL-PISL--KRKPAKEDyelAHDLLERVGLS-AYRDHYPAQLSGGQQSRVA 141
Cdd:PRK13641 80 lkklrkkVSLVFQFPeaQLFE-NTVLKDVEFgPKNFgfSEDEAKEK---ALKWLKKVGLSeDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 142 MARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-211 |
1.95e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 104.60 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQP------DEgaVYLRGEKVTKPSSS---------IGYV 78
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtaDR--FRWNGIDLLKLSPRerrkiigreIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPT------------LLEwkrVIDNVLLPISL-KRKPAKEDYelAHDLLERVGLsayRDH------YPAQLSGGQQSR 139
Cdd:COG4170 95 FQEPSscldpsakigdqLIE---AIPSWTFKGKWwQRFKWRKKR--AIELLHRVGI---KDHkdimnsYPHELTEGECQK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 140 VAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-211 |
2.37e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.83 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGY 77
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaalrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQ-----APTLlewkRviDNVLLPislkrKPAKEDYELaHDLLERVGLSAYRDHYPA----------QLSGGQQSRVAM 142
Cdd:PRK11160 419 VSQrvhlfSATL----R--DNLLLA-----APNASDEAL-IEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 143 ARALIQRPALLFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHdiaEAVYLA--DRIAVMAAGKIV 211
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITH---RLTGLEqfDRICVMDNGQII 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-211 |
3.92e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.94 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTtLLKLAAGLLQPDEGAVYLRGEKVTKPSS-------------- 73
Cdd:PRK15134 13 VAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKS-VTALSILRLLPSPPVVYPSGDIRFHGESllhaseqtlrgvrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 74 -SIGYVFQAPTL-------LEwKRVIDNVLLPISLKRKPAKEDyelAHDLLERVGL--SAYR-DHYPAQLSGGQQSRVAM 142
Cdd:PRK15134 92 nKIAMIFQEPMVslnplhtLE-KQLYEVLSLHRGMRREAARGE---ILNCLDRVGIrqAAKRlTDYPHQLSGGERQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 143 ARALIQRPALLFLDEPFAALDAitreELQADLLTLCR-LQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDV----SVQAQILQLLReLQqelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-164 |
5.63e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 100.51 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRyQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK----PSSSIGYVF 79
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdePHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLpisLKRKPAKEDYELaHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:TIGR01189 80 HLPGLKPELSALENLHF---WAAIHGGAQRTI-EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*
gi 1215498689 160 AALDA 164
Cdd:TIGR01189 156 TALDK 160
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-211 |
1.00e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.86 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS--------SSIGYVFQAP-TLLEWKRV 90
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewravrSDIQMIFQDPlASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDNVL---LPISLKRKPAKEDYELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAit 166
Cdd:PRK15079 117 IGEIIaepLRTYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV-- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1215498689 167 reELQADLLTLCR-LQNT---SVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK15079 195 --SIQAQVVNLLQqLQREmglSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-210 |
1.11e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.77 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS--------------SIGYVFQ 80
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAraasrrvasvpqdtSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVidnvllPISLKRKPAKEDYELAHD-LLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:PRK09536 94 VRQVVEMGRT------PHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 160 AALD---AITREELQADLLTLCRlqntSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK09536 168 ASLDinhQVRTLELVRRLVDDGK----TAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-211 |
1.24e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 100.38 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV---TKPS--SSIGY 77
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQaPTLLEWKRVIDNVLLPislKRKPAKEDYE------LAHDLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALIQR 149
Cdd:cd03251 81 VSQ-DVFLFNDTVAENIAYG---RPGATREEVEeaaraaNAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 150 PALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIV 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-211 |
1.37e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLT--PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGYVfqapT-- 83
Cdd:COG1129 260 EGLSvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagIAYV----Ped 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 ------LLEWKrVIDNVLLPiSLKR-------KPAKEDyELAHDLLERVGLSAYRDHYPAQ-LSGGQQSRVAMARALIQR 149
Cdd:COG1129 336 rkgeglVLDLS-IRENITLA-SLDRlsrggllDRRRER-ALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 150 PALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
1.96e-25 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 97.13 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekVTKPSSSIGYVfqapt 83
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------TWGSTVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 llewkrvidnvllpislkrkpakedyelahdllervglsayrdhypAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:cd03221 69 ----------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1215498689 164 AITREELQADLLTLcrlqNTSVLFITHDIaeavYLADRIA 203
Cdd:cd03221 103 LESIEALEEALKEY----PGTVILVSHDR----YFLDQVA 134
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-211 |
2.34e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.89 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE---KVTKPS--SSIGYVF 79
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASlrRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEwkRVI-DNVLLPislkrKPAKEDYEL--------AHDLLER--VGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK13657 416 QDAGLFN--RSIeDNIRVG-----RPDATDEEMraaaeraqAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRVV 548
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-211 |
2.39e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT------KPSSS 74
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhaRARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYE-LAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-209 |
2.84e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS----SSIGYVF 79
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArlarARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 160 AALDAITREELQADLLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
23-211 |
3.67e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 99.52 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLR--------------GEKVTKPSSSIGYVFQAPTLLEWK 88
Cdd:TIGR02323 22 VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsgaelelyqlseAERRRLMRTEWGFVHQNPRDGLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RV-----IDNVLLPISLKRkpAKEDYELAHDLLERVGLSAYR-DHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAAL 162
Cdd:TIGR02323 102 RVsaganIGERLMAIGARH--YGNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1215498689 163 DAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-211 |
4.40e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 6 LDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYL----------RGEKVTKP 71
Cdd:PRK13645 9 LDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 SSSIGYVFQAPTLLEWKRVI--DNVLLPISLKRKpAKEDYELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQETIekDIAFGPVNLGEN-KQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-209 |
4.67e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 97.93 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGekvtkpssSIGYVFQAPTLL----------- 85
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVSQEPWIQngtirenilfg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 -----EW-KRVIDNVLLPISLKRKPAKEDYELAhdllERvGLSayrdhypaqLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:cd03250 90 kpfdeERyEKVIKACALEPDLEILPDGDLTEIG----EK-GIN---------LSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 160 AALDAITREELQADLLTLCRLQNTSVLFITHDIaEAVYLADRIAVMAAGK 209
Cdd:cd03250 156 SAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-211 |
5.33e-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: 103.28 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhtlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwKRVIDNVLLpiSLKRKPAKEDYELAHDLLE--------RVGLSAYRDHYPAQLSGGQQSRVAMARALIQRP 150
Cdd:TIGR01193 554 PQEPYIFS-GSILENLLL--GAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 151 ALLFLDEPFAALDAITREELQADLLtlcRLQNTSVLFITH--DIAEAVylaDRIAVMAAGKIV 211
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLL---NLQDKTIIFVAHrlSVAKQS---DKIIVLDHGKII 687
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-211 |
6.04e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDgVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAV-YLRGEKVTKPSSSI------- 75
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRD-VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 ------GYVFQAPTllewkrviDNVLLPISL-----KRKPAKED--Y----ELAHDLLERVGLSAYR-DHYPAQLSGGQQ 137
Cdd:PRK11701 86 llrtewGFVHQHPR--------DGLRMQVSAggnigERLMAVGArhYgdirATAGDWLERVEIDAARiDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 138 SRVAMARALIQRPALLFLDEPFAALDAitreELQADLL----TLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLdllrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-213 |
1.26e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.34 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDE---GAVYLRGEKVTKPS--SSIGYVFQAPTLL------EW 87
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQfqKCVAYVRQDDILLpgltvrET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 88 KRVIDNVLLPislKRKPAKEDYELAHDLLER-VGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAIT 166
Cdd:cd03234 102 LTYTAILRLP---RKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 167 REELQADLLTLCRlQNTSVLFITH----DIAEavyLADRIAVMAAGKIVYA 213
Cdd:cd03234 179 ALNLVSTLSQLAR-RNRIVILTIHqprsDLFR---LFDRILLLSSGEIVYS 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
1.57e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGekvtKPSS--SIGYVFQaPTLlewkRVIDNVLL 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSllGLGGGFN-PEL----TGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 97 PISLKRKPAKEDYELAHDLLERVGLSAYRD----HYpaqlSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQA 172
Cdd:cd03220 108 NGRLLGLSRKEIDEKIDEIIEFSELGDFIDlpvkTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1215498689 173 DLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03220 184 RLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-190 |
1.84e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.41 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 21 DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK----PSSSIGYVFQAPTllewkrvIDNVLL 96
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdeYHQDLLYLGHQPG-------IKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 97 PI----SLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQA 172
Cdd:PRK13538 91 ALenlrFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*...
gi 1215498689 173 DLLTLCRlQNTSVLFITH 190
Cdd:PRK13538 171 LLAQHAE-QGGMVILTTH 187
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-212 |
4.19e-24 |
|
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: 95.31 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQP--DEGAVYLRGEKVTK--PSSSIGYVFQaptllewkrviD 92
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKrsFRKIIGYVPQ-----------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NVLLPislkrkpakedyelahDLLERVGLsayrdHYPAQL---SGGQQSRVAMARALIQRPALLFLDEPFAALDAITREE 169
Cdd:cd03213 91 DILHP----------------TLTVRETL-----MFAAKLrglSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 170 LqadLLTLCRL--QNTSVLFITHDI-AEAVYLADRIAVMAAGKIVY 212
Cdd:cd03213 150 V---MSLLRRLadTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIY 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-211 |
7.09e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 13 YQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD-----EGAVYLRGEKVTKPS-------SSIGYVFQ 80
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdpievrREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKRVIDNVLLPISLKR--KPAKEDYELAHDLLERVGL-SAYRDH---YPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-210 |
7.47e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 12 RYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIG--------------- 76
Cdd:PRK10619 14 RY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrllrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 ---YVFQAPTLLEWKRVIDNVL-LPISLKRKPAKEDYELAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK10619 93 rltMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 152 LLFLDEPFAALDAitreELQADLLTLCRL---QNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK10619 173 VLLFDEPTSALDP----ELVGEVLRIMQQlaeEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-211 |
7.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTP----VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYL--------RGEKVTKP 71
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 72 -SSSIGYVFQAP--TLLEWKRVIDNVLLPISLKrkPAKEDYE-LAHDLLERVGLSA-YRDHYPAQLSGGQQSRVAMARAL 146
Cdd:PRK13643 82 vRKKVGVVFQFPesQLFEETVLKDVAFGPQNFG--IPKEKAEkIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLfITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-211 |
1.01e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPD---EGAVYLRGEKVTKPSSS-----IGYVFQAPTL 84
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIelrrrVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LEWKRVIDNVLLPISLKR--KPAKEDYELAHDLLERVGL---SAYRDHYPA-QLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdeVKDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 159 FAALDAITREELQADLLTLCRlqNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-204 |
1.19e-23 |
|
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: 94.48 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP----SSSIGYVFQAPTLLEWKRVIDNv 94
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdsiARGLLYLGHAPGIKTTLSVLEN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 llpisLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADL 174
Cdd:cd03231 94 -----LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180 190
....*....|....*....|....*....|...
gi 1215498689 175 LTLCRlQNTSVLFITH---DIAEAVYLADRIAV 204
Cdd:cd03231 169 AGHCA-RGGMVVLTTHqdlGLSEAGARELDLGF 200
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
1.46e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-------SIgy 77
Cdd:COG4604 3 EIKNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlAI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLL---PISlKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSR--VAMARAliQRPAL 152
Cdd:COG4604 80 LRQENHINSRLTVRELVAFgrfPYS-KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAMVLA--QDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-212 |
3.62e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD---EGAVYLRGEKVT----------KPSSSIGYVFQAPTLLE 86
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQregrlardirKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 WKRVIDNVLLPiSLKRKP---------AKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:PRK09984 100 RLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 158 PFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-211 |
4.15e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-----SIGYVFQAPTLLEWKR 89
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlarRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 VIDNVllpiSLKRKP--------AKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAA 161
Cdd:PRK11231 93 VRELV----AYGRSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 162 LDaITReelQADLLTLCRLQNT---SVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11231 169 LD-INH---QVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-211 |
4.48e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 10 TYRYQ-GL-----TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT-----KPSSSIGYV 78
Cdd:PRK15112 13 TFRYRtGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAP-TLLEWKRVIDNVL-LPISLKRKPAKEDYELA-HDLLERVGLsaYRDH---YPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:PRK15112 93 FQDPsTSLNPRQRISQILdFPLRLNTDLEPEQREKQiIETLRQVGL--LPDHasyYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-211 |
5.37e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 6 LDRVTYRYQGltpvIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--------IGY 77
Cdd:PRK10261 330 LNRVTREVHA----VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrdIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAP--TLLEWKRVIDNVLLPISLKR-KPAKEDYELAHDLLERVGLS---AYRdhYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK10261 406 IFQDPyaSLDPRQTVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLpehAWR--YPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-219 |
1.53e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.96 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 21 DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTkPSS-----SIGYVFQAPTLLEWKRVIDNVL 95
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-AGDiatrrRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 96 LPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLL 175
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1215498689 176 TLCRLQNTSVlFI-THDIAEAVyLADRIAVMAAGKIvyaLDVDLP 219
Cdd:NF033858 442 ELSREDGVTI-FIsTHFMNEAE-RCDRISLMHAGRV---LASDTP 481
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-209 |
1.91e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS----SSIGYVF 79
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRArharQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 160 AALDAITREELQADLLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-217 |
2.21e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerrrlgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQ-------APTLlewkRVIDNVLL------PIS----LKRKPAKedyELAHDLLERVGLSAYRDHYPA-QLSGGQQSR 139
Cdd:COG3845 338 IPEdrlgrglVPDM----SVAENLILgryrrpPFSrggfLDRKAIR---AFAEELIEEFDVRTPGPDTPArSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 140 VAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-211 |
2.61e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 7 DRVTYRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLqPDEGAVYLRGEKVTKPSSS-----IGYVFQA 81
Cdd:PRK11174 354 DLEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswrkhLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 82 PTLLEwKRVIDNVLLpislkRKPAKEDYELaHDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARALIQRP 150
Cdd:PRK11174 432 PQLPH-GTLRDNVLL-----GNPDASDEQL-QQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 151 ALLFLDEPFAALDAITREELQADLLTLCRLQNTsvLFITHDIaEAVYLADRIAVMAAGKIV 211
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQL-EDLAQWDQIWVMQDGQIV 562
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-209 |
2.76e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.38 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 11 YRYQGlTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-------SSIGYVFQAPT 83
Cdd:PRK13638 9 FRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllalrQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDNVlLPISLKRKPAKEDyELAH---DLLERVGLSAYRdHYPAQ-LSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:PRK13638 88 QQIFYTDIDSD-IAFSLRNLGVPEA-EITRrvdEALTLVDAQHFR-HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 160 AALDAITREELQADLLTLCRlQNTSVLFITHDI------AEAVYLADRIAVMAAGK 209
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIdliyeiSDAVYVLRQGQILTHGA 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-212 |
2.92e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 93.23 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG----EKVTKPSSSIGYVFQAPTLLEWK-RVIDNV 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEFARRIGVVFGQRSQLWWDlPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 LLpisLKR--KPAKEDYE--LAHdLLERVGLSAYRDHyPA-QLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREE 169
Cdd:COG4586 118 RL---LKAiyRIPDAEYKkrLDE-LVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1215498689 170 LQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG4586 193 IREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-211 |
5.96e-22 |
|
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: 90.25 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGY 77
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwKRVIDNvLLPISLKrkpakEDYELaHDLLERVGLSAYRDHYP-----------AQLSGGQQSRVAMARAL 146
Cdd:cd03244 83 IPQDPVLFS-GTIRSN-LDPFGEY-----SDEEL-WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTlcRLQNTSVLFITHDIaEAVYLADRIAVMAAGKIV 211
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVV 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-210 |
7.11e-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: 93.95 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG--------EKVTKpssS 74
Cdd:TIGR01842 317 LSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdrETFGK---H 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQaptllewkrviDNVLLPISLKRKPAKED--------YELA-----HDLLERV--GLSAYRDHYPAQLSGGQQSR 139
Cdd:TIGR01842 394 IGYLPQ-----------DVELFPGTVAENIARFGenadpekiIEAAklagvHELILRLpdGYDTVIGPGGATLSGGQRQR 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 140 VAMARALIQRPALLFLDEPFAALDAITREELQADLLTLcRLQNTSVLFITHDIAeAVYLADRIAVMAAGKI 210
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-211 |
1.87e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 13 YQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLA--AGLLQPD---EGAVYLRGEKVTKPSS-------SIGYVFQ 80
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTdtvdlrkEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEWKrVIDNVLLPISLKrkpAKEDYELAHDLLER--VGLSAY-----RDHYPA-QLSGGQQSRVAMARALIQRPAL 152
Cdd:PRK14239 94 QPNPFPMS-IYENVVYGLRLK---GIKDKQVLDEAVEKslKGASIWdevkdRLHDSAlGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-190 |
2.83e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVT-YRYQGlTPVIDGVSWTINEGEfHCLV-GKSGCGKTTLLKLAAGLLQPDEGAVYL-RGEKVT----KPsssig 76
Cdd:COG4178 363 LALEDLTlRTPDG-RPLLEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqRP----- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQApTLLEwkrvidNVLLPislkRKPAKEDYELAHDLLERVGLSAYRDHY------PAQLSGGQQSRVAMARALIQRP 150
Cdd:COG4178 436 YLPLG-TLRE------ALLYP----ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1215498689 151 ALLFLDEPFAALDaitrEELQADLLTLCR--LQNTSVLFITH 190
Cdd:COG4178 505 DWLFLDEATSALD----EENEAALYQLLReeLPGTTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-213 |
5.36e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLtPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGY 77
Cdd:PRK15439 12 LCARSISKQYSGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahqlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKRVIDNVLLpiSLKRKPAkeDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILF--GLPKRQA--SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 158 PFAALDAITREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYA 213
Cdd:PRK15439 167 PTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALS 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-211 |
5.60e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 91.32 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAP 82
Cdd:TIGR02203 336 VTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslrRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 TLLEwKRVIDNVllpislkRKPAKEDYELAHdlLERVGLSAYR----DHYP-----------AQLSGGQQSRVAMARALI 147
Cdd:TIGR02203 416 VLFN-DTIANNI-------AYGRTEQADRAE--IERALAAAYAqdfvDKLPlgldtpigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIV 546
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-211 |
8.37e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.40 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRyQGLTPVIDGvSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP--SSSIGYVFQA----- 81
Cdd:PRK15056 14 VTWR-NGHTALRDA-SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqKNLVAYVPQSeevdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 82 --PTLLEwkrviDNVLLP----ISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:PRK15056 92 sfPVLVE-----DVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 156 DEPFAALDAITREELqADLLTLCRLQNTSVLFITHDIAEAVYLADrIAVMAAGKIV 211
Cdd:PRK15056 167 DEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVL 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-210 |
1.41e-20 |
|
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: 90.46 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP----SSSIGYVFQAPTLLEWKRVIDN 93
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 VLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQaD 173
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW-D 1102
|
170 180 190
....*....|....*....|....*....|....*..
gi 1215498689 174 LLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:TIGR01257 1103 LLLKYRSGRT-IIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-190 |
1.43e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS--SSIGYV----FQAPTL-----LE 86
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaEACHYLghrnAMKPALtvaenLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 -WKRVIDNVLLPIslkrkpakedyelaHDLLERVGLSAYrDHYPAQ-LSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:PRK13539 96 fWAAFLGGEELDI--------------AAALEAVGLAPL-AHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*.
gi 1215498689 165 ITrEELQADLLTLCRLQNTSVLFITH 190
Cdd:PRK13539 161 AA-VALFAELIRAHLAQGGIVIAATH 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-211 |
1.91e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.78 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAPTLleWKR-VI 91
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVL--FSGsVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 92 DNVLLpiSLKRKPAKEDYELA-----HDLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:TIGR00958 573 ENIAY--GLTDTPDEEIMAAAkaanaHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1215498689 165 itreELQADLLTLCRLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVV 692
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-211 |
2.54e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 12 RYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLlKLAAGLLQPDEGAVYLRGEKVTKPS--------SSIGYVFQAPT 83
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTT-GLALLRLINSQGEIWFDGQPLHNLNrrqllpvrHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVidNVL------LPISLKRKPAKEDYELAHDLLERVGLS-AYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK15134 373 SSLNPRL--NVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 157 EPFAALDaitrEELQADLLTLCR-LQNT---SVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK15134 451 EPTSSLD----KTVQAQILALLKsLQQKhqlAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-209 |
3.79e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.47 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 8 RVTYRYQ-GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD---EGAVYLRG-EKVTKP--------SSS 74
Cdd:PRK09473 19 RVTFSTPdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGrEILNLPekelnklrAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAP--TLLEWKRVIDNVLLPISLKRKPAK-EDYELAHDLLERVGLSAYRDH---YPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK09473 99 ISMIFQDPmtSLNPYMRVGEQLMEVLMLHKGMSKaEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 149 RPALLFLDEPFAALDaITreeLQADLLTLC----RLQNTSVLFITHDIAEAVYLADRIAVMAAGK 209
Cdd:PRK09473 179 RPKLLIADEPTTALD-VT---VQAQIMTLLnelkREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-211 |
5.96e-20 |
|
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: 88.32 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPDEGAVYLR----------------G 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 66 EKVTKPSSS----------------------IGYVFQAP-TLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLS 122
Cdd:TIGR03269 80 EPCPVCGGTlepeevdfwnlsdklrrrirkrIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 123 AYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITH--DIAEAvyLAD 200
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIED--LSD 237
|
250
....*....|.
gi 1215498689 201 RIAVMAAGKIV 211
Cdd:TIGR03269 238 KAIWLENGEIK 248
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-211 |
7.44e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.65 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQpdeGAVYLRGEKVT-------KPSSSIgyvfQAPTLLEWKRVI 91
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTgdvtlngEPLAAI----DAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 92 DNVLLP---------ISLKRKP--------AKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ------ 148
Cdd:PRK13547 89 PQAAQPafafsareiVLLGRYPharragalTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 149 ---RPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-212 |
8.80e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPDEGAVYLRGEKVTKPSSS------IGYVFQAP------T 83
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDeraragIFLAFQYPveipgvS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDNvllPISLKRKPAKEDYELAHDLLERVGLS---AYRDhYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:COG0396 94 VSNFLRTALN---ARRGEELSAREFLKLLKEKMKELGLDedfLDRY-VNEGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 161 ALDAitrEELQ--ADLLTLCRLQNTSVLFITH-----DIAEavylADRIAVMAAGKIVY 212
Cdd:COG0396 170 GLDI---DALRivAEGVNKLRSPDRGILIITHyqrilDYIK----PDFVHVLVDGRIVK 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-211 |
1.49e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.31 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAV-YLRGEKVTK-----PSSSIGYVF--------- 79
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARlqqdpPRNVEGTVYdfvaegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPIS------LKRKPAKEDYELA-------HDLLERVGLSAyrDHYPAQLSGGQQSRVAMARAL 146
Cdd:PRK11147 94 QAEYLKRYHDISHLVETDPSeknlneLAKLQEQLDHHNLwqlenriNEVLAQLGLDP--DAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 147 IQRPALLFLDEPFAALDAITREELQADLLTLcrlqNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
1.60e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-PSSSIgyVF 79
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKI--MR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLL-EWKRVIDNVLLPISL-------KRKPAKEDYELAHDLLERvgLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK11614 80 EAVAIVpEGRRVFSRMTVEENLamggffaERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 152 LLFLDEPFAALDAITREELqADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-216 |
2.46e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 3 FLQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRG---EKVTKPSSS---IG 76
Cdd:PRK09700 5 YISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAAqlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 77 YVFQAPTLLEWKRVIDNVLLPISLKRK-------PAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQR 149
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 150 PALLFLDEPFAALdaiTREELQADLLTLCRLQN--TSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV 216
Cdd:PRK09700 164 AKVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-216 |
2.82e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD----EGAVYLRGEKVTkPSS----SIGYVFQAPtllewkR 89
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA-PCAlrgrKIATIMQNP------R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 VIDNvllPISLKRKPAKE----------DYELAHdLLERVGLSAYR---DHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK10418 90 SAFN---PLHTMHTHAREtclalgkpadDATLTA-ALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 157 EPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV 216
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDV 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-211 |
3.48e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.79 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRY-QGLTP--VIDGVSWTINEGEFHCLVGKSGCGKTT-------LL----KLAAGLLQPDEGAVYLRGE 66
Cdd:PRK11022 1 MALLNVDKLSVHFgDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIdypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 67 KVTKP--SSSIGYVFQAP--TLLEWKRVIDNVLLPISLKRKPA-KEDYELAHDLLERVGL---SAYRDHYPAQLSGGQQS 138
Cdd:PRK11022 81 KERRNlvGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVHQGGNkKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 139 RVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-211 |
3.63e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS-----IGYV 78
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarrIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQ---APTLLEWKRVIDNVLLPIS-LKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK10253 87 AQnatTPGDITVQELVARGRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-208 |
6.79e-19 |
|
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: 85.84 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLT-PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS----SIGYV 78
Cdd:TIGR01257 1938 LRLNELTKVYSGTSsPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISdvhqNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 159 FAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAG 208
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-211 |
7.67e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVY----LRGEK-------VTKPSSSIGY 77
Cdd:PRK14271 27 LTLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvLLGGRsifnyrdVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKrVIDNVLLPI-SLKRKPAKEDYELAHDLLERVGL-SAYRDHY---PAQLSGGQQSRVAMARALIQRPAL 152
Cdd:PRK14271 106 LFQRPNPFPMS-IMDNVLAGVrAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTLCrlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-208 |
8.92e-19 |
|
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: 81.99 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS---------SIGYVFQAPTLLEwK 88
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFeatrsrnrySVAYAAQKPWLLN-A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RVIDNVLL--PISLKRKPAKEDyelAHDLLERVGLSAYRDHYPA-----QLSGGQQSRVAMARALIQRPALLFLDEPFAA 161
Cdd:cd03290 94 TVEENITFgsPFNKQRYKAVTD---ACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 162 LDAITREEL-QADLLTLCRLQNTSVLFITHDIAeavYL--ADRIAVMAAG 208
Cdd:cd03290 171 LDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ---YLphADWIIAMKDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-211 |
1.22e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.49 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLlQPD---EGAVYLRGEKVTKPS------SS 74
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNirdterAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYEL----AHDLLERVGLSAYRDHYP-AQLSGGQQSRVAMARALIQR 149
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 150 PALLFLDEPFAALdaiTREELQA--DLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:TIGR02633 160 ARLLILDEPSSSL---TEKETEIllDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-211 |
1.29e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.02 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 11 YRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-----------KVTKPSSSIGYVF 79
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqiDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVLLPI-SLKRKPAKEDYELAHDLLERVGL--SAY-RDHYPA-QLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLkSHGIKEKREIKKIVEECLRKVGLwkEVYdRLNSPAsQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQaDLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIE-KLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-195 |
1.70e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLL--QPDEGAVYLRGEKVTKPSSsigyvfqaptllewkrVIDNV 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS----------------LIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 llpislkrkPAKEDYELAHDLLERVGLS---AYRDHYpAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQ 171
Cdd:COG2401 107 ---------GRKGDFKDAVELLNAVGLSdavLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|....*.
gi 1215498689 172 ADLLTLCRLQNTSVLFITH--DIAEA 195
Cdd:COG2401 177 RNLQKLARRAGITLVVATHhyDVIDD 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-211 |
4.08e-18 |
|
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: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE---KVTKPS--SSIGYV 78
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirDVTQASlrAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQaptllewkrviDNVLLPISLK------RKPA-KEDYELA------HDLLERV-----------GLsayrdhypaQLSG 134
Cdd:COG5265 438 PQ-----------DTVLFNDTIAyniaygRPDAsEEEVEAAaraaqiHDFIESLpdgydtrvgerGL---------KLSG 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 135 GQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRlqNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-218 |
1.16e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.34 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPDEGAVYLRGEKVTKPSSS------IGYVFQAPTLLEWKRV 90
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerarlgIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDnvllpislkrkpakedyelahdLLERVGLSayrdhypaqLSGGQQSRVAMARALIQRPALLFLDEPFAALDaITREEL 170
Cdd:cd03217 95 AD----------------------FLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 171 QADLLTLCRLQNTSVLFITH--DIAEAVyLADRIAVMAAGKIVYALDVDL 218
Cdd:cd03217 143 VAEVINKLREEGKSVLIITHyqRLLDYI-KPDRVHVLYDGRIVKSGDKEL 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-211 |
2.43e-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: 77.84 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQ-GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-----KVTKPSSSIGY 77
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKrvidnvlLPISLKRKPAKEDYELAHDLleRV---GLSayrdhypaqLSGGQQSRVAMARALIQRPALLF 154
Cdd:cd03369 87 IPQDPTLFSGT-------IRSNLDPFDEYSDEEIYGAL--RVsegGLN---------LSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 155 LDEPFAALDAITREELQADLLTLcrLQNTSVLFITHDIaEAVYLADRIAVMAAGKIV 211
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREE--FTNSTILTIAHRL-RTIIDYDKILVMDAGEVK 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-211 |
2.50e-17 |
|
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: 80.61 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG--------LTPVidgvSWTINEGE--FhcLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTkpss 73
Cdd:COG4615 328 LELRGVTYRYPGedgdegftLGPI----DLTIRRGElvF--IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 74 sigyvfqaPTLLEWKR----VI-------DNVLLPislkrkPAKEDYELAHDLLERVGLS---AYRDHY--PAQLSGGQQ 137
Cdd:COG4615 398 --------ADNREAYRqlfsAVfsdfhlfDRLLGL------DGEADPARARELLERLELDhkvSVEDGRfsTTDLSQGQR 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 138 SRVAMARALI-QRPALLFlDEpFAA-LDAITREELQADLLTLCRLQNTSVLFITHDIAeavY--LADRIAVMAAGKIV 211
Cdd:COG4615 464 KRLALLVALLeDRPILVF-DE-WAAdQDPEFRRVFYTELLPELKARGKTVIAISHDDR---YfdLADRVLKMDYGKLV 536
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-190 |
2.56e-17 |
|
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: 76.42 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQpdegavyLRGEKVTKPSSS-IGYVFQAP 82
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP-------WGSGRIGMPEGEdLLFLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 -----TLLE-----WKRVidnvllpislkrkpakedyelahdllervglsayrdhypaqLSGGQQSRVAMARALIQRPAL 152
Cdd:cd03223 74 ylplgTLREqliypWDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 1215498689 153 LFLDEPFAALDaitrEELQADLLTLCRLQNTSVLFITH 190
Cdd:cd03223 113 VFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-217 |
4.35e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTT-------LLKLAAGLLQPDEGAVYLRGEKVTKPS------------SS 74
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSeqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAP--TLLEWKRVIDNVLLPISLKRKPAKEDYEL-AHDLLERVGL---SAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK10261 106 MAMIFQEPmtSLNPVFTVGEQIAESIRLHQGASREEAMVeAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAItreeLQADLLTLCR-LQ---NTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD 217
Cdd:PRK10261 186 RPAVLIADEPTTALDVT----IQAQILQLIKvLQkemSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-211 |
4.56e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYV 78
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsvlrQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQAPTLLEwkrviDNVLLPISLKRKPAKEDyelAHDLLERVGLSAYRDHYPA-----------QLSGGQQSRVAMARALI 147
Cdd:PRK10790 421 QQDPVVLA-----DTFLANVTLGRDISEEQ---VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQaDLLTLCRlQNTSVLFITHDIAEAVYlADRIAVMAAGKIV 211
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQ-QALAAVR-EHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-212 |
7.03e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD---EGAVYLRGEKVTKPSSSI--GYVFQ----APTL--LEWK 88
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisAYVQQddlfIPTLtvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RVIDNVLLPislKRKPAKEDYELAHDLLERVGLSAYRD---HYPAQ---LSGGQQSRVAMARALIQRPALLFLDEPFAAL 162
Cdd:TIGR00955 121 MFQAHLRMP---RRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 163 DAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-210 |
7.51e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTkpsssigyvfqAPT 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-----------AEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDNV-----LLPISLKRKPAKEDYELAHDLLERVGLS---AYRDHYPA--QLSGGQQSRVAMARALIQRPALL 153
Cdd:PRK10522 392 PEDYRKLFSAVftdfhLFDQLLGPEGKPANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 154 FLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAeavY--LADRIAVMAAGKI 210
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDH---YfiHADRLLEMRNGQL 527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-192 |
7.62e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekVTKPSSSIGYVFQAPTLlewkrvidNVLLPI 98
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYL--------DTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 99 SLKR----KPA--KEDYELAhdlLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQa 172
Cdd:PRK09544 85 TVNRflrlRPGtkKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY- 160
|
170 180
....*....|....*....|.
gi 1215498689 173 DLLTLCRLQ-NTSVLFITHDI 192
Cdd:PRK09544 161 DLIDQLRRElDCAVLMVSHDL 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
1.31e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS------SS 74
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttaalaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 75 IGYVFQAPTLLEWKRVIDNVLL---PIS---LKRKPAKEDyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLgqlPHKggiVNRRLLNYE---AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELQAdLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFR-VIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-195 |
1.93e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.13 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAG-----------LLQPDEGAvylrGEKVTKPSSSIGYVfqAPTL-L 85
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDIKKHIGYV--SSSLhL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 86 EWkRV---IDNVLLP-----ISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQ-LSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK10938 348 DY-RVstsVRNVILSgffdsIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....*....
gi 1215498689 157 EPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEA 195
Cdd:PRK10938 427 EPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-163 |
3.00e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS--IGYVFQAPTLLEWKRVIDNV 94
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 95 LLPISLKRKPAKEdyeLAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PRK13543 104 HFLCGLHGRRAKQ---MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-240 |
3.77e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 21 DGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLlQPD---EGAVYLRGE----KVTKPSSSIGYVF--QAPTLLEWKRVI 91
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEvcrfKDIRDSEALGIVIihQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 92 DNvllpISLKRKPAK-------EDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDa 164
Cdd:NF040905 97 EN----IFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 165 itrEELQADLLTLCR-LQN---TSVLfITHDIAEAVYLADRIAVMAAGKIVYALDVDLPK-----------PRTLEMRY- 228
Cdd:NF040905 172 ---EEDSAALLDLLLeLKAqgiTSII-ISHKLNEIRRVADSITVLRDGRTIETLDCRADEvtedriirgmvGRDLEDRYp 247
|
250
....*....|....
gi 1215498689 229 --EPRFNELSFHVR 240
Cdd:NF040905 248 erTPKIGEVVFEVK 261
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-211 |
6.60e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRY---QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL---------------------LQP 56
Cdd:PRK15093 1 MPLLDIRNLTIEFktsDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrvtadrmrfddidllrLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 57 DE---------GAVYLRGEKVTKPSSSIGY-VFQA-PTLLE----WKRVidnvllpiSLKRKPAKEdyelahdLLERVGL 121
Cdd:PRK15093 81 RErrklvghnvSMIFQEPQSCLDPSERVGRqLMQNiPGWTYkgrwWQRF--------GWRKRRAIE-------LLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 122 SAYRD---HYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYL 198
Cdd:PRK15093 146 KDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQW 225
|
250
....*....|...
gi 1215498689 199 ADRIAVMAAGKIV 211
Cdd:PRK15093 226 ADKINVLYCGQTV 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-203 |
9.53e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 13 YQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPD---EGAVYLRGEKVTKPS-------SSIGYVFQ 80
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDvdpvevrRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEwKRVIDNV---------------LLPISLKRKPAkedYELAHDLLERVGLSayrdhypaqLSGGQQSRVAMARA 145
Cdd:PRK14243 99 KPNPFP-KSIYDNIaygaringykgdmdeLVERSLRQAAL---WDEVKDKLKQSGLS---------LSGGQQQRLCIARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 146 LIQRPALLFLDEPFAALDAITR---EELQADLltlcrLQNTSVLFITHDIAEAVYLADRIA 203
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTlriEELMHEL-----KEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-208 |
1.12e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.10 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekvtKPSSSIGYVFQAPTLLEwKRVIDNVLL 96
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------KHSGRISFSPQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 97 PISLkrkpakEDYEL-----AHDLLERVGLSAYRDHYP-----AQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAIT 166
Cdd:TIGR01271 510 GLSY------DEYRYtsvikACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1215498689 167 REELQADllTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAG 208
Cdd:TIGR01271 584 EKEIFES--CLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-212 |
1.26e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.58 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGekvtKPSS--SIGYVFQaPTLlewkRVIDNV-- 94
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSAllELGAGFH-PEL----TGRENIyl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 ---LLPISLKRKPAKEDY--ELAhdllervGLSAYRD----HYpaqlSGGQQSRVAMARALIQRPALLFLDEPFAALDAI 165
Cdd:COG1134 112 ngrLLGLSRKEIDEKFDEivEFA-------ELGDFIDqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1215498689 166 TREELQADLLTLcRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:COG1134 181 FQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-203 |
1.80e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD-----EGAV-------YLRGEKVTKPSSSIGYVFQAPTLLE 86
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVeffnqniYERRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 WKrVIDNVLLPISLKR-----------KPAKEDYELAHDLLERVGLSAYrdhypaQLSGGQQSRVAMARALIQRPALLFL 155
Cdd:PRK14258 102 MS-VYDNVAYGVKIVGwrpkleiddivESALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1215498689 156 DEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIA 203
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-209 |
1.87e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLqPD---EGAVYLRGEKVTKPS------SSIGYVFQAPTLLEWKRV 90
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNirdterAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 91 IDNVLL---PISLKRKPAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALdaiTR 167
Cdd:PRK13549 100 LENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL---TE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1215498689 168 EELQADLLTLCRLQNTSV--LFITHDIAEAVYLADRIAVMAAGK 209
Cdd:PRK13549 177 SETAVLLDIIRDLKAHGIacIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-191 |
2.29e-15 |
|
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: 74.97 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGavylrgEKVTKPSSSIGYVFQAPTL 84
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------EARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LEWKRVIDNVLLPIS-----LKR----------------KPAKEDYEL--------AHDL---LErVGLSAYR----DHY 128
Cdd:TIGR03719 80 DPTKTVRENVEEGVAeikdaLDRfneisakyaepdadfdKLAAEQAELqeiidaadAWDLdsqLE-IAMDALRcppwDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 129 PAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLtlcRLQNTsVLFITHD 191
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPGT-VVAVTHD 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-214 |
2.54e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSI----GYVF-----QAPTL-----LEWk 88
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarGLVYlpedrQSSGLyldapLAW- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 rvidNV------LLPISLKrkPAKEDyelahDLLER----VGLSAYRDHYPAQ-LSGGQQSRVAMARALIQRPALLFLDE 157
Cdd:PRK15439 361 ----NVcalthnRRGFWIK--PAREN-----AVLERyrraLNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 158 PFAALDAITReelqADLLTLCR---LQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYAL 214
Cdd:PRK15439 430 PTRGVDVSAR----NDIYQLIRsiaAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGAL 485
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-212 |
2.71e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD--EGAVYLRGEKVTKPS-SSIGYVFQAPTLLEWKRVIDNVL 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIlKRTGFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 96 ------LPISLKRKpakEDYELAHDLLERVGLSAYRD-----HYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:PLN03211 163 fcsllrLPKSLTKQ---EKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1215498689 165 ITREELQADLLTLCRLQNTSVLFItHDIAEAVY-LADRIAVMAAGKIVY 212
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSM-HQPSSRVYqMFDSVLVLSEGRCLF 287
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-211 |
4.00e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGL-TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-----KVTKPSSSIGY 77
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwkrviDNVLLPISLKRKP--AKEDYE----LAH--DLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALI 147
Cdd:PRK11176 422 VSQNVHLFN-----DTIANNIAYARTEqySREQIEeaarMAYamDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTLCRlqNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIV 557
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-210 |
4.17e-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: 74.60 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 14 QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGekvtkpssSIGYV-----FQAPTLLEwk 88
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------SVAYVpqqawIQNDSLRE-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 rvidNVLLPISLKRKPAKEDYElAHDLLERVGLSAYRDHYP-----AQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:TIGR00957 718 ----NILFGKALNEKYYQQVLE-ACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 164 A-ITREELQADLLTLCRLQNTSVLFITHDIAeavYL--ADRIAVMAAGKI 210
Cdd:TIGR00957 793 AhVGKHIFEHVIGPEGVLKNKTRILVTHGIS---YLpqVDVIIVMSGGKI 839
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-235 |
4.63e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.06 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 26 TINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFQAptllewkRVIDnvLLPISLKRKPA 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEG-------TVRD--LLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 106 KEDYElaHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD---------AITREELQAdllt 176
Cdd:cd03237 92 HPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaskVIRRFAENN---- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 177 lcrlqNTSVLFITHDIAEAVYLADRIAV----------------MAAG--KIVYALDVDLPK-PRTlemrYEPRFNEL 235
Cdd:cd03237 166 -----EKTAFVVEHDIIMIDYLADRLIVfegepsvngvanppqsLRSGmnRFLKNLDITFRRdPET----GRPRINKL 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-204 |
6.77e-15 |
|
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: 73.67 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 26 TINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrGEKVT-KPSssigYVfqaptllewkrVIDNVLLPISLKRKP 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISyKPQ----YI-----------SPDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 105 AKEDYE---LAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD---------AITReelqa 172
Cdd:COG1245 426 NTDDFGssyYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavakAIRR----- 500
|
170 180 190
....*....|....*....|....*....|..
gi 1215498689 173 dlltLCRLQNTSVLFITHDIAEAVYLADRIAV 204
Cdd:COG1245 501 ----FAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
1.28e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 26 TINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVyLRGEKVT-KPSssigYVFQAP--TLLEWKRVIdnvllpislkr 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISyKPQ----YIKPDYdgTVEDLLRSI----------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 103 kpaKEDYE---LAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD---------AITReel 170
Cdd:PRK13409 425 ---TDDLGssyYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavakAIRR--- 498
|
170 180 190
....*....|....*....|....*....|....
gi 1215498689 171 qadlltLCRLQNTSVLFITHDIAEAVYLADRIAV 204
Cdd:PRK13409 499 ------IAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-210 |
1.47e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGYVFQaptllewKRVI 91
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangIVYISE-------DRKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 92 DNVLLPISLK--------RKPAKEDYELAHDLlERVGLSAY----------RDHYPAQLSGGQQSRVAMARALIQRPALL 153
Cdd:PRK10762 339 DGLVLGMSVKenmsltalRYFSRAGGSLKHAD-EQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 154 FLDEPFAALDAITREELQaDLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIY-QLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-206 |
1.71e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYR-YQGLTPVIDgvSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPdegavyLRGEKVTKpsssigyvF 79
Cdd:PRK10938 1 MSSLQISQGTFRlSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPL------LSGERQSQ--------F 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLL-----------EWKRVIDNVLLP------------ISLKRKpakeDYELAHDLLERVGLSAYRDHYPAQLSGGQ 136
Cdd:PRK10938 65 SHITRLsfeqlqklvsdEWQRNNTDMLSPgeddtgrttaeiIQDEVK----DPARCEQLAQQFGITALLDRRFKYLSTGE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215498689 137 QSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFIT--HDIAEAVylaDRIAVMA 206
Cdd:PRK10938 141 TRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNrfDEIPDFV---QFAGVLA 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
98-227 |
1.83e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 98 ISLKRKPAKEDyelAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTL 177
Cdd:NF000106 114 LDLSRKDARAR---ADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 178 CRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVDLPKP----RTLEMR 227
Cdd:NF000106 191 VR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTkvggRTLQIR 243
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-208 |
2.32e-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: 70.66 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekvtKPSSSIGYVFQAPTLLEwKRVIDNVLL 96
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------KHSGRISFSSQFSWIMP-GTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 97 PISLKRKPAKEDYElAHDLLERVGLSAYRDHYP-----AQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQ 171
Cdd:cd03291 121 GVSYDEYRYKSVVK-ACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 1215498689 172 ADllTLCRLQ-NTSVLFITHDIaEAVYLADRIAVMAAG 208
Cdd:cd03291 200 ES--CVCKLMaNKTRILVTSKM-EHLKKADKILILHEG 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-220 |
9.42e-14 |
|
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: 68.55 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 29 EGEFHCLVGKSGCGKTTLLKLAAGLLQP-----------DEGAVYLRG-----------EKVTKPSSSIGYVFQAPtlle 86
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPnlgkfddppdwDEILDEFRGselqnyftkllEGDVKVIVKPQYVDLIP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 wKRVIDNVLLPISLKRKPAKEDYelahdLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDaiT 166
Cdd:cd03236 101 -KAVKGKVGELLKKKDERGKLDE-----LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1215498689 167 REELQADLLTLCRLQNT-SVLFITHDIAEAVYLADRIAVMAAGKIVYALdVDLPK 220
Cdd:cd03236 173 KQRLNAARLIRELAEDDnYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGV-VTLPK 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-226 |
1.92e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KPSSS----IGYVFQAPTLLEWKRVIDN 93
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 vllpISLKRKPA--------KEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPfaaLDAI 165
Cdd:PRK10762 100 ----IFLGREFVnrfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 166 TREELQA--DLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV-DLPKPRTLEM 226
Cdd:PRK10762 173 TDTETESlfRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVaDLTEDSLIEM 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-228 |
2.19e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSS-----SIGYVF 79
Cdd:PRK10575 13 ALRNVSFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 80 QAPTLLEWKRVIDNVllpiSLKRKP--------AKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPA 151
Cdd:PRK10575 92 QQLPAAEGMTVRELV----AIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 152 LLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALD-VDLPKPRTLEMRY 228
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTpAELMRGETLEQIY 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-218 |
2.62e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP------SSSIGYVFQAPTLLEwKRVIDNVLL 96
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwRSKIGVVSQDPLLFS-NSIKNNIKY 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 97 PI-SLKRKPAKEDY------------------------------------ELAH--------------DLLERVGL---- 121
Cdd:PTZ00265 483 SLySLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsnELIEmrknyqtikdsevvDVSKKVLIhdfv 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 122 SAYRDHY-------PAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAE 194
Cdd:PTZ00265 563 SALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLST 642
|
250 260
....*....|....*....|....
gi 1215498689 195 AVYlADRIAVMAAGKIVYALDVDL 218
Cdd:PTZ00265 643 IRY-ANTIFVLSNRERGSTVDVDI 665
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
5.28e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLtPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgeKVTKpSSSIGYVFQAP- 82
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE-NANIGYYAQDHa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 -------TLLEWkrvidnvllpISLKRKPaKEDYELAHDLLERVGLSAYRDHYPAQ-LSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK15064 393 ydfendlTLFDW----------MSQWRQE-GDDEQAVRGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 155 LDEPFAALDAITREELQadlLTLCRLQNTsVLFITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:PRK15064 462 MDEPTNHMDMESIESLN---MALEKYEGT-LIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-191 |
1.03e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAVYLrgekvtKPSSSIGYVFQAPTLLEWKRVIDNVLLPIS-----LKR------- 102
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGIKVGYLPQEPQLDPEKTVRENVEEGVAevkaaLDRfneiyaa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 103 ---------KPAKEDYEL--------AHDL---LERVgLSAYR----DHYPAQLSGGQQSRVAMARALIQRPALLFLDEP 158
Cdd:PRK11819 112 yaepdadfdALAAEQGELqeiidaadAWDLdsqLEIA-MDALRcppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
170 180 190
....*....|....*....|....*....|...
gi 1215498689 159 FAALDAITREELQAdllTLCRLQNTsVLFITHD 191
Cdd:PRK11819 191 TNHLDAESVAWLEQ---FLHDYPGT-VVAVTHD 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-190 |
1.19e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS----IGYVFQAPTLLEWKRVIDN 93
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyqkqLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 VLLPISLKRKPAKEDyelahDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQAD 173
Cdd:PRK13540 95 CLYDIHFSPGAVGIT-----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 1215498689 174 LLTLcRLQNTSVLFITH 190
Cdd:PRK13540 170 IQEH-RAKGGAVLLTSH 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-191 |
1.77e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYQGLTpVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYlRGEKVtkpssSIGYVFQAPTL 84
Cdd:PRK11147 321 EMENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL-----EVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 LE-WKRVIDNVllpislkrKPAKEDYEL----AHDL--LERVGLSAYRDHYPAQ-LSGGQQSRVAMARALIqRPA-LLFL 155
Cdd:PRK11147 394 LDpEKTVMDNL--------AEGKQEVMVngrpRHVLgyLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFL-KPSnLLIL 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 1215498689 156 DEPFAALDAITREELQaDLLTlcRLQNTsVLFITHD 191
Cdd:PRK11147 465 DEPTNDLDVETLELLE-ELLD--SYQGT-VLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-220 |
1.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQ-GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-----PSSSIGY 77
Cdd:PLN03232 1235 IKFEDVHLRYRpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltdLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLleWKRVIDNVLLPISLKRKPAK-EDYELAH--DLLER--VGLSAYRDHYPAQLSGGQQSRVAMARALIQRPAL 152
Cdd:PLN03232 1315 IPQSPVL--FSGTVRFNIDPFSEHNDADLwEALERAHikDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 153 LFLDEPFAALDAITREELQADLLTlcRLQNTSVLFITHDIaEAVYLADRIAVMAAGKIvyaLDVDLPK 220
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRL-NTIIDCDKILVLSSGQV---LEYDSPQ 1454
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-212 |
1.49e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.51 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 1 MSFLQLDRVTYRYQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEgavylrgekvtKPSSSIGYvfq 80
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNV-----------SVEGDIHY--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 aptllewkrvidnvllpislKRKPAKEDYELAHdllervGLSAY---RDHYPAQL---------------------SGGQ 136
Cdd:cd03233 70 --------------------NGIPYKEFAEKYP------GEIIYvseEDVHFPTLtvretldfalrckgnefvrgiSGGE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 137 QSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVY-LADRIAVMAAGKIVY 212
Cdd:cd03233 124 RKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQIY 200
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-212 |
1.50e-11 |
|
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: 61.05 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 27 INEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVylrgekvtkpsssigyvfqaptllEWKRvidnvllpISLKRKPAK 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------------------EWDG--------ITPVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 107 EDyelahdllervglsayrdhypaqLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVL 186
Cdd:cd03222 70 ID-----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170 180
....*....|....*....|....*.
gi 1215498689 187 FITHDIAEAVYLADRIAVMAAGKIVY 212
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHVFEGEPGVY 152
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-211 |
4.33e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLqPDEGAVYLRGEKV-TKPSSSI----GYVFQ---APTLLE-WKrvidn 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeAWSAAELarhrAYLSQqqtPPFAMPvFQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 vLLPISLKRKPAKEDYELA-HDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQ-----RPA--LLFLDEPFAALDAI 165
Cdd:PRK03695 89 -YLTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 166 TREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-220 |
4.69e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGllQPD----EGAVYLRGEKVT------KPSSSIGYVFQAPtlLE 86
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILdlepeeRAHLGIFLAFQYP--IE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 WKRV--IDNVLLPISLKRKPAK-------EDYELAHDLLERVGLSAYRDHYPAQ--LSGGQQSRVAMARALIQRPALLFL 155
Cdd:CHL00131 96 IPGVsnADFLRLAYNSKRKFQGlpeldplEFLEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 156 DEPFAALDaITREELQADLLTLCRLQNTSVLFITHDIAEAVYLA-DRIAVMAAGKIVYALDVDLPK 220
Cdd:CHL00131 176 DETDSGLD-IDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAELAK 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-211 |
5.60e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRYQ-GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAP 82
Cdd:PLN03130 1243 VVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrKVLGIIPQAP 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 TLleWKRVIDNVLLPISlKRKPAK--EDYELAH--DLLER--VGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PLN03130 1323 VL--FSGTVRFNLDPFN-EHNDADlwESLERAHlkDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 157 EPFAALDAIT--------REELQAdlltlCrlqntSVLFITHDIaEAVYLADRIAVMAAGKIV 211
Cdd:PLN03130 1400 EATAAVDVRTdaliqktiREEFKS-----C-----TMLIIAHRL-NTIIDCDRILVLDAGRVV 1451
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-217 |
6.01e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.92 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 34 CLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrgekvtkpsssigyvfqaptllewkrvidnvllpISLKRKPAKEDYELAH 113
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------IDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 114 DLLERVGLSayrdhypaqLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQAD-----LLTLCRLQNTSVLFI 188
Cdd:smart00382 52 IIVGGKKAS---------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVILT 122
|
170 180
....*....|....*....|....*....
gi 1215498689 189 THDIAEavyLADRIAVMAAGKIVYALDVD 217
Cdd:smart00382 123 TNDEKD---LGPALLRRRFDRRIVLLLIL 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-210 |
6.11e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAVYlRGEKVTKPSSSIGYVfqaptllEWKRVIDNVLLPISLKRKPAKEDYELAHd 114
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF-RSAKVRMAVFSQHHV-------DGLDLSSNPLLYMMRCFPGVPEQKLRAH- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 115 lLERVGLS---AYRDHYpaQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLtlcrLQNTSVLFITHD 191
Cdd:PLN03073 611 -LGSFGVTgnlALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV----LFQGGVLMVSHD 683
|
170 180
....*....|....*....|..
gi 1215498689 192 ---IAEAVylaDRIAVMAAGKI 210
Cdd:PLN03073 684 ehlISGSV---DELWVVSEGKV 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-203 |
6.93e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrGEKVtkpssSIGYVFQAPTLLE-----WKRVID- 92
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQSRDALDpnktvWEEISGg 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NVLLPISLKRKPAKedyelAH---------DLLERVGlsayrdhypaQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:TIGR03719 411 LDIIKLGKREIPSR-----AYvgrfnfkgsDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1215498689 164 AITREELQADLLTL--CrlqntsVLFITHDiaeaVYLADRIA 203
Cdd:TIGR03719 476 VETLRALEEALLNFagC------AVVISHD----RWFLDRIA 507
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-211 |
2.20e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPSSS------IGYVFQAPTLLEWKRVIDN 93
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 vllpISLKRKPAK-------EDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALdaiT 166
Cdd:PRK10982 94 ----MWLGRYPTKgmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---T 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1215498689 167 REELQADLLTLCRLQNT--SVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-213 |
2.55e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYlrGEKvtkpssSIGYVFQAPTLLEwKRVIDNVLLpislkr 102
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AER------SIAYVPQQAWIMN-ATVRGNILF------ 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 103 kPAKEDYELAHDLLERVGLSAYRDHYPA-----------QLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQ 171
Cdd:PTZ00243 744 -FDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1215498689 172 ADLLtLCRLQNTSVLFITHDIaEAVYLADRIAVMAAGKIVYA 213
Cdd:PTZ00243 823 EECF-LGALAGKTRVLATHQV-HVVPRADYVVALGDGRVEFS 862
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-210 |
3.30e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPD-EGAVYLRGEKVT--KPSSSIGY-VFQAPTllEWKR------ 89
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirNPAQAIRAgIAMVPE--DRKRhgivpi 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 --VIDNVLLPiSLKRKPAKEDYELAHDL------LERVGLSAYRDHYP-AQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:TIGR02633 354 lgVGKNITLS-VLKSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1215498689 161 ALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-211 |
4.58e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVT--KPSSSI--GYVF-----QAPTLLEWKRVIDN 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIraGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 vlLPISLKRK---------PAKEDyELAHDLLERVGL-SAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PRK11288 352 --INISARRHhlragclinNRWEA-ENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1215498689 164 AITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK11288 429 VGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-164 |
5.39e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGA-VYLRGekvtkpssSIGYVFQAPTLLEwKRVIDNVLL 96
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRG--------SVAYVPQVSWIFN-ATVRENILF 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 97 PISLKRK---PAKEDYELAHDLlervGLSAYRD-----HYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:PLN03232 702 GSDFESErywRAIDVTALQHDL----DLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-190 |
5.80e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQpdegavyLRGEKVTKPS-SSIGYVFQAP-----TLLewkrviD 92
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRLTKPAkGKLFYVPQRPymtlgTLR------D 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NVLLPIS---LKRKpAKEDYELA--------HDLLER-VGLSAYRDhYPAQLSGGQQSRVAMARALIQRPALLFLDEPFA 160
Cdd:TIGR00954 534 QIIYPDSsedMKRR-GLSDKDLEqildnvqlTHILEReGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 1215498689 161 ALDAitreELQADLLTLCRLQNTSVLFITH 190
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-163 |
6.03e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 2 SFLQLDRvtyryqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAvylrgekVTKPSS-SIGYVFQ 80
Cdd:PRK10636 5 SSLQIRR------GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGS-------YTFPGNwQLAWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 81 APTLLEwKRVIDNVL--------LPISLKRKPAKED-YELAH------------------DLLERVGLSAYRDHYPAQ-L 132
Cdd:PRK10636 72 ETPALP-QPALEYVIdgdreyrqLEAQLHDANERNDgHAIATihgkldaidawtirsraaSLLHGLGFSNEQLERPVSdF 150
|
170 180 190
....*....|....*....|....*....|.
gi 1215498689 133 SGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-205 |
1.22e-09 |
|
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: 57.87 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAV-----------YLRG-----------EKVTKPSSSIGYVFQAPtllewKRVID 92
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGtelqdyfkklaNGEIKVAHKPQYVDLIP-----KVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 NV--LLPISLKRKPAKEdyelahdLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITReel 170
Cdd:COG1245 179 TVreLLEKVDERGKLDE-------LAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR--- 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1215498689 171 qadlLTLCRL------QNTSVLFITHDIAEAVYLADRIAVM 205
Cdd:COG1245 249 ----LNVARLirelaeEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-190 |
1.34e-09 |
|
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: 58.03 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRyQGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGYVFQAPT 83
Cdd:TIGR00957 1292 LRYR-EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrFKITIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 84 LLEWKRVIDnvLLPISlkrKPAKED----YELAHDLLERVGLSAYRDHYPAQ----LSGGQQSRVAMARALIQRPALLFL 155
Cdd:TIGR00957 1371 LFSGSLRMN--LDPFS---QYSDEEvwwaLELAHLKTFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190
....*....|....*....|....*....|....*
gi 1215498689 156 DEPFAALDAITREELQADLLTlcRLQNTSVLFITH 190
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAH 1478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-205 |
1.50e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 35 LVGKSGCGKTTLLKLAAGLLQPDEGAV-----------YLRG-----------EKVTKPSSSIGYVFQAPTLLEWKrVID 92
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGtelqnyfkklyNGEIKVVHKPQYVDLIPKVFKGK-VRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 93 nvLLPISLKRKPAKEdyelahdLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDaiTREELQA 172
Cdd:PRK13409 183 --LLKKVDERGKLDE-------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLNV 251
|
170 180 190
....*....|....*....|....*....|...
gi 1215498689 173 DLLTLCRLQNTSVLFITHDIAEAVYLADRIAVM 205
Cdd:PRK13409 252 ARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-212 |
1.54e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.71 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAA-----GLLqpdEGAVYLRGEKVTKP-SSSIGYVFQAPTLLEWKRVIDN 93
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLDKNfQRSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 VLLPISLKrkpakedyelahdllervGLSAYrdhypaqlsggQQSRVAMARALIQRPALLFLDEPFAALDAitreelQAD 173
Cdd:cd03232 100 LRFSALLR------------------GLSVE-----------QRKRLTIGVELAAKPSILFLDEPTSGLDS------QAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1215498689 174 LLTLCRLQNT-----SVLFITHDIAEAVY-LADRIAVMA-AGKIVY 212
Cdd:cd03232 145 YNIVRFLKKLadsgqAILCTIHQPSASIFeKFDRLLLLKrGGKTVY 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-175 |
1.93e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYL-RGEKvtkpsssIGYVFQAP 82
Cdd:PRK10636 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIK-------LGYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 tlLEWKRVIDNVLLpiSLKRKPAKEDYELAHDLLERVGLSAYRDHYP-AQLSGGQQSRVAMARALIQRPALLFLDEPFAA 161
Cdd:PRK10636 385 --LEFLRADESPLQ--HLARLAPQELEQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|....
gi 1215498689 162 LDAITREELQADLL 175
Cdd:PRK10636 461 LDLDMRQALTEALI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-229 |
6.10e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQGLTPViDGVswtINEGEFHCLVGKSGCGKTTLLKLAAGL----------------LQPDEGAVYLRGEK 67
Cdd:TIGR00956 65 LKKFRDTKTFDILKPM-DGL---IKPGELTVVLGRPGSGCSTLLKTIASNtdgfhigvegvitydgITPEEIKKHYRGDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 68 VtkpsssigYVFQAPTLLEWKRVIDNVLLPISLkRKPA-------KEDY--ELAHDLLERVGLSAYRD-----HYPAQLS 133
Cdd:TIGR00956 141 V--------YNAETDVHFPHLTVGETLDFAARC-KTPQnrpdgvsREEYakHIADVYMATYGLSHTRNtkvgnDFVRGVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 134 GGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAEAVY-LADRIAVMAAGKIVY 212
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYeLFDKVIVLYEGYQIY 291
|
250
....*....|....*..
gi 1215498689 213 ALDVDLPKPRTLEMRYE 229
Cdd:TIGR00956 292 FGPADKAKQYFEKMGFK 308
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-204 |
9.12e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 9.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 128 YPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQNTSVLFITHDIAeAVYLADRIAV 204
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVV 1430
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-215 |
9.67e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 23 VSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTkPSS-------SIGYVfqaptlLEWKR------ 89
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSpldavkkGMAYI------TESRRdngffp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 ---VIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRD------HYPAQ----LSGGQQSRVAMARALIQRPALLFLD 156
Cdd:PRK09700 355 nfsIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQREllalkcHSVNQniteLSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 157 EPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALD 215
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-211 |
1.25e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 54.72 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKPS-----SSIGY 77
Cdd:PRK10789 314 LDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswrSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEwkrviDNVLLPISLKRKPA-KEDYELA------HDLLERV--GLSAYRDHYPAQLSGGQQSRVAMARALIQ 148
Cdd:PRK10789 394 VSQTPFLFS-----DTVANNIALGRPDAtQQEIEHVarlasvHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 149 RPALLFLDEPFAALDAITREELqadLLTLCRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIV 211
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-210 |
1.54e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQ-PDEGAVYLRGEKVT--KPSSS----IGYVFQaptllEWKR-- 89
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirNPQQAiaqgIAMVPE-----DRKRdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 90 ------VIDNVLLPiSLKR--------KPAKEDYelAHDLLERVGLSAYRDHYP-AQLSGGQQSRVAMARALIQRPALLF 154
Cdd:PRK13549 352 ivpvmgVGKNITLA-ALDRftggsridDAAELKT--ILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 155 LDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-164 |
1.92e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGA-VYLRGEKVTKPSSSigYVFQAPtllewkrVIDNVL- 95
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsVVIRGTVAYVPQVS--WIFNAT-------VRDNILf 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215498689 96 -LPISLKR-KPAKEDYELAHDLlervGLSAYRDHYP-----AQLSGGQQSRVAMARALIQRPALLFLDEPFAALDA 164
Cdd:PLN03130 702 gSPFDPERyERAIDVTALQHDL----DLLPGGDLTEigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-210 |
4.16e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 18 PVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKV--TKPSSSIGYVFQAPTL----------- 84
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFALVTEerrstgiyayl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 85 -LEWKRVIDNVLLPIS----LKRKPAKEDYELAHDLLeRVGLSAYRDHYpAQLSGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:PRK10982 342 dIGFNSLISNIRNYKNkvglLDNSRMKSDTQWVIDSM-RVKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 160 AALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYLADRIAVMAAGKI 210
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-170 |
1.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 37 GKSGCGKTTLLKLAAGLLQPDEGAVYLRG---EKVTKP-SSSIGY---------VFQapTLLEWKRVIDnvllpiSLKRK 103
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNcniNNIAKPyCTYIGHnlglklemtVFE--NLKFWSEIYN------SAETL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215498689 104 PAKEDYELAHDLLervglsayrDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREEL 170
Cdd:PRK13541 105 YAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-166 |
2.93e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLL-----KLAAGLLQPDEGAVYLRGEKVTKPsSSIGYVFQAPTLLEWKRVIDN 93
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVITGGDRLVNGRPLDSSFQ-RSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 94 VLLPISLkRKPA----KEDYELAHDLLERVGLSAYRDHY---PAQ-LSGGQQSRVAMARALIQRPALL-FLDEPFAALDA 164
Cdd:TIGR00956 857 LRFSAYL-RQPKsvskSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLDS 935
|
..
gi 1215498689 165 IT 166
Cdd:TIGR00956 936 QT 937
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-191 |
3.60e-07 |
|
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: 48.51 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 26 TINEGEFHCLVGKSGCGKTTLLK---LAAGLLQPDEGAVYLRGEKVTKPSSSIGYVFqaptllewkrvidnvLLPislkr 102
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGCIVAAVSAELIF---------------TRL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 103 kpakedyelahdllervglsayrdhypaQLSGGQQSRVAMARAL----IQRPALLFLDEPFAALDAITREELqADLLTLC 178
Cdd:cd03227 77 ----------------------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL-AEAILEH 127
|
170
....*....|...
gi 1215498689 179 RLQNTSVLFITHD 191
Cdd:cd03227 128 LVKGAQVIVITHL 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-174 |
3.98e-07 |
|
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: 50.68 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDegavylrGEkvtkpSSSIGYVFQAPTLLEWKR---VIDNVL 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-------GE-----IQIDGVSWNSVTLQTWRKafgVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 96 LPISLKRKPAKEDYELAHD-----LLERVGLSAYRDHYPAQL-----------SGGQQSRVAMARALIQRPALLFLDEPF 159
Cdd:TIGR01271 1302 FIFSGTFRKNLDPYEQWSDeeiwkVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170
....*....|....*
gi 1215498689 160 AALDAITREELQADL 174
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTL 1396
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-210 |
4.47e-07 |
|
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: 49.47 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 9 VTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQpdegavylrgekvTKPSSSI-GYVFQAPTLLE 86
Cdd:cd03289 8 LTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-------------TEGDIQIdGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 87 WKR---VIDNVLLPISLKRKPAKEDYELAHD-----LLERVGLSAYRDHYPAQL-----------SGGQQSRVAMARALI 147
Cdd:cd03289 75 WRKafgVIPQKVFIFSGTFRKNLDPYGKWSDeeiwkVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215498689 148 QRPALLFLDEPFAALDAITREELQADLLTlcRLQNTSVLFITHDIaEAVYLADRIAVMAAGKI 210
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-203 |
8.91e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrGEKVtkpssSIGYVFQAPTLLEwkrvidnvllpis 99
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----KLAYVDQSRDALD------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 100 lkrkPAKEDYELAHDLLE--RVG---------LSAYRDHYPAQ------LSGGQQSRVAMARALIQRPALLFLDEPFAAL 162
Cdd:PRK11819 401 ----PNKTVWEEISGGLDiiKVGnreipsrayVGRFNFKGGDQqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1215498689 163 DAITREELQADLLTL--CrlqntsVLFITHDiaeaVYLADRIA 203
Cdd:PRK11819 477 DVETLRALEEALLEFpgC------AVVISHD----RWFLDRIA 509
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-220 |
1.26e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-KVTKPSSSIGYVFQAPTLLEWKrvidnvLLPI 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGIENIEFK------MLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 99 SLKRKPAKedyELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAiTREELQADLLTLC 178
Cdd:PRK13546 114 GFKRKEIK---AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ-TFAQKCLDKIYEF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1215498689 179 RLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDVD--LPK 220
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDdvLPK 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-210 |
3.50e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 5 QLDRVTYRYqGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTKP------SSSIGYV 78
Cdd:NF033858 3 RLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 79 FQA------PTLlewkRVIDNVLLPISLKRKPAKEDYELAHDLLERVGLSAYRDHyPA-QLSGGQQSRVAMARALIQRPA 151
Cdd:NF033858 82 PQGlgknlyPTL----SVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215498689 152 LLFLDEPFAALDAITRE---ELQADLltlcRLQNT--SVLFITHDIAEAVYLaDRIAVMAAGKI 210
Cdd:NF033858 157 LLILDEPTTGVDPLSRRqfwELIDRI----RAERPgmSVLVATAYMEEAERF-DWLVAMDAGRV 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-235 |
3.92e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRY-QGLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGekvtKPSSSIGyvfqap 82
Cdd:PTZ00243 1309 LVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIGAYG------ 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 83 tLLEWKRVI-----DNVLLPIS--------LKRKPAKedyelAHDLLERVGLsayRDHYPAQlSGGQQSRV--------- 140
Cdd:PTZ00243 1379 -LRELRRQFsmipqDPVLFDGTvrqnvdpfLEASSAE-----VWAALELVGL---RERVASE-SEGIDSRVleggsnysv 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 141 ------AMARALIQR-PALLFLDEPFAALDAITREELQADLLTlcRLQNTSVLFITHDIaEAVYLADRIAVMAAGKIvya 213
Cdd:PTZ00243 1449 gqrqlmCMARALLKKgSGFILMDEATANIDPALDRQIQATVMS--AFSAYTVITIAHRL-HTVAQYDKIIVMDHGAV--- 1522
|
250 260
....*....|....*....|..
gi 1215498689 214 ldVDLPKPRTLEMRYEPRFNEL 235
Cdd:PTZ00243 1523 --AEMGSPRELVMNRQSIFHSM 1542
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-191 |
6.65e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 15 GLTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLrgekvtKPSSSIGYVFQAPTLLEWKRVIDNV 94
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL------DPNERLGKLRQDQFAFEEFTVLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 95 LL-------------PISLKRKPAKEDY----EL---------------AHDLLERVGLsAYRDHYP--AQLSGGQQSRV 140
Cdd:PRK15064 86 IMghtelwevkqerdRIYALPEMSEEDGmkvaDLevkfaemdgytaearAGELLLGVGI-PEEQHYGlmSEVAPGWKLRV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1215498689 141 AMARALIQRPALLFLDEPFAALDAITREELQADLltlcRLQNTSVLFITHD 191
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-211 |
1.61e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.90 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 4 LQLDRVTYRYQG-LTPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGEKVTK-P----SSSIGY 77
Cdd:cd03288 20 IKIHDLCVRYENnLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPlhtlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 78 VFQAPTLLEWKrvidnvllpISLKRKPAK--------EDYELAHdlLERV------GLSAYRDHYPAQLSGGQQSRVAMA 143
Cdd:cd03288 100 ILQDPILFSGS---------IRFNLDPECkctddrlwEALEIAQ--LKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 144 RALIQRPALLFLDEPFAALDAITREELQADLLTlcRLQNTSVLFITHDIAeAVYLADRIAVMAAGKIV 211
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVS-TILDADLVLVLSRGILV 233
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-192 |
1.86e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 34 CLVGKSGCGKTTLL---------------KLAAGLLQPDEGAVYLRGE--------KVTKP---------------SSSI 75
Cdd:COG0419 27 LIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEEASVELEfehggkryRIERRqgefaefleakpserKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 76 GYVFQAPTLLEWKRVIDNVLLPISLKRKPAKEDYELAHDLLERvgLSAYRDhyPAQLSGGQQSRVAMARALiqrpaLLFL 155
Cdd:COG0419 107 KRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQ--LSGLDP--IETLSGGERLRLALADLL-----SLIL 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1215498689 156 DepFAALDAITREELqADLLtlcrlqnTSVLFITHDI 192
Cdd:COG0419 178 D--FGSLDEERLERL-LDAL-------EELAIITHVI 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
129-191 |
2.49e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 2.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 129 PAQLSGGQQS------RVAMARALIQRPALLFLDEPFAALDAITREELQADLLTLCRLQ-NTSVLFITHD 191
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQkNFQLIVITHD 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-202 |
2.73e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.47 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKlaAGLlqpdEGAVYLRGEKVTKPSSSIGYVFqaptLLEWKRVIDNVLLPIS 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGL----YASGKARLISFLPKFSRNKLIF----IDQLQFLIDVGLGYLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 100 LKRKpakedyelahdllervgLSAyrdhypaqLSGGQQSRVAMARALIQRP--ALLFLDEPFAALDAITREELQADLLTL 177
Cdd:cd03238 81 LGQK-----------------LST--------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170 180
....*....|....*....|....*
gi 1215498689 178 CRLQNTsVLFITHDIaEAVYLADRI 202
Cdd:cd03238 136 IDLGNT-VILIEHNL-DVLSSADWI 158
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
132-211 |
5.60e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 132 LSGGQQSRVAMARALIQRPALLFLDEPfaaldaiTR--------------EELQAdlltlcrlQNTSVLFITHDIAEAVY 197
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP-------TRgidvgakyeiytiiNELAA--------EGKGVIVISSELPELLG 469
|
90
....*....|....
gi 1215498689 198 LADRIAVMAAGKIV 211
Cdd:NF040905 470 MCDRIYVMNEGRIT 483
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-194 |
6.97e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 20 IDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGAVYLRGE-KVTKPSSSIGYVFQAPTLLEWKRvidnvlLPI 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSGLNGQLTGIENIELKG------LMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 99 SLKRKPAKedyELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALD-AITREELqaDLLTL 177
Cdd:PRK13545 114 GLTKEKIK---EIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCL--DKMNE 188
|
170
....*....|....*..
gi 1215498689 178 CRLQNTSVLFITHDIAE 194
Cdd:PRK13545 189 FKEQGKTIFFISHSLSQ 205
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-220 |
4.17e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 17 TPVIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGL--LQPDEGAVYLRGEKVTK--PSSSIG----YVFQAPtlLEWK 88
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLElsPEDRAGegifMAFQYP--VEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 89 RVIDNVLLPISL------KRKPAKEDYELAHDLLERVGLSayrdHYPAQL---------SGGQQSRVAMARALIQRPALL 153
Cdd:PRK09580 92 GVSNQFFLQTALnavrsyRGQEPLDRFDFQDLMEEKIALL----KMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 154 FLDEPFAALDaITREELQADLLTLCRLQNTSVLFITHDIAEAVYLA-DRIAVMAAGKIVYALDVDLPK 220
Cdd:PRK09580 168 ILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFTLVK 234
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
131-175 |
6.06e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.94 E-value: 6.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1215498689 131 QLSGGQQSRVAMARAL-IQR--PALLFL-DEPFAALDAITREELqADLL 175
Cdd:cd03272 158 QLSGGQKSLVALALIFaIQKcdPAPFYLfDEIDAALDAQYRTAV-ANMI 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
131-163 |
8.67e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 8.67e-04
10 20 30
....*....|....*....|....*....|...
gi 1215498689 131 QLSGGQQSRVAMARALIQRPALLFLDEPFAALD 163
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
132-205 |
8.71e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 132 LSGGQQSRVAMARAL-----IQRPA-----LLFLDEPFAALDAITREELqADLLTLCRLQNTSVLFITH--DIAEAvyLA 199
Cdd:cd03279 124 LSGGETFLASLSLALalsevLQNRGgarleALFIDEGFGTLDPEALEAV-ATALELIRTENRMVGVISHveELKER--IP 200
|
....*.
gi 1215498689 200 DRIAVM 205
Cdd:cd03279 201 QRLEVI 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-208 |
2.49e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 130 AQLSGGQQSRVAMARALI---QRPALLFLDEPFAALDAITREELQADLLTLCRlQNTSVLFITHDIAEAVYlADRIAVMA 206
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVS-LGHSVIYIDHDPALLKQ-ADYLIEMG 1775
|
..
gi 1215498689 207 AG 208
Cdd:PRK00635 1776 PG 1777
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-202 |
3.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215498689 130 AQLSGGQQSRVAMARALiqrPALLF-----LDEPFAALDAITREELqADLLTLCRLQNTSVLFITHDiAEAVYLADRI 202
Cdd:PRK00635 475 ATLSGGEQERTALAKHL---GAELIgityiLDEPSIGLHPQDTHKL-INVIKKLRDQGNTVLLVEHD-EQMISLADRI 547
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
124-179 |
3.97e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.67 E-value: 3.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215498689 124 YRDHypAQLSGGQQSR---VAMARALIQ----------RPALLFLDEPFAALDaitrEELQADLLTLCR 179
Cdd:pfam13558 27 YRRS--GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLD----EENIRTALELLR 89
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
19-216 |
5.04e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 36.96 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 19 VIDGVSWTINEGEFHCLVGKSGCGKTTLLKLAAGLLQPDEGA-VYLRGEKVtkPSSSIGYVFQAPTLLEWKRVIDNVLlp 97
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDAL--PLGANSFILPGLTGEENARMMASLY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215498689 98 islkrkpAKEDYELAHDLLERVGLSAYRDHYPAQLSGGQQSRVAMARALIQRPALLFLDEPFAALDAITREELQADLltL 177
Cdd:PRK15177 78 -------GLDGDEFSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAAL--A 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1215498689 178 CRLQNTSVLFITHDIAEAVYLADRIAVMAAGKIVYALDV 216
Cdd:PRK15177 149 CQLQQKGLIVLTHNPRLIKEHCHAFGVLLHGKITMCEDL 187
|
|
| |
