|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
1.24e-148 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 412.52 E-value: 1.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
7.75e-123 |
|
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: 347.09 E-value: 7.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
9.29e-113 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 321.51 E-value: 9.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGI 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
6.86e-99 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 286.94 E-value: 6.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RR-KIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMkKRVIAIEDGIIVRDES 220
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARA-DRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
3.44e-96 |
|
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: 279.76 E-value: 3.44e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKE-IPFV 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMkKRVIAIEDGII 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
3.67e-79 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 240.75 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:COG1135 1 MIELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHN----KEIVNtmkkRVIAIEDGIIV 216
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvvRRICD----RVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-226 |
1.52e-76 |
|
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: 230.55 E-value: 1.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVrdesrgEYGS 226
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV------EEGT 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
1.45e-74 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 226.09 E-value: 1.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENV--------AFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-218 |
2.73e-73 |
|
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: 221.82 E-value: 2.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEIPFVRRKI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDfkllP-----KLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:COG1122 78 GLVFQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
1.12e-71 |
|
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: 218.32 E-value: 1.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENV--------AFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-213 |
1.61e-71 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 217.43 E-value: 1.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
1.62e-71 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 221.21 E-value: 1.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:PRK11153 1 MIELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-218 |
3.19e-70 |
|
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: 214.74 E-value: 3.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFA-------LEVIGEQPSVI-KKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
7.75e-69 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 214.96 E-value: 7.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKekeiPFvRRK 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 161 ADEPTGNLDP----DTSWEVMKTLEEInnrGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG3842 159 LDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
2.10e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 210.72 E-value: 2.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYP---NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeipfV 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHN 196
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
1.01e-67 |
|
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: 207.37 E-value: 1.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRKI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
2.84e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 204.46 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAiKEKEIPFVRRK 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFAL-EVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN----KEIVNtmkkRVIAIEDGIIV 216
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREVAD----RVVFMDGGRIV 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
8.77e-66 |
|
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: 202.31 E-value: 8.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKL-LPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
1.15e-65 |
|
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: 202.90 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDLSeAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
1.94e-65 |
|
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: 202.08 E-value: 1.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRKI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
1.37e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.90 E-value: 1.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRKI 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
1.68e-63 |
|
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: 197.27 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 R-RKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNtMKKRVIAIEDGIIVRDE 219
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVEDT 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
5.17e-63 |
|
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: 204.37 E-value: 5.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYP----NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPF 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VRRKIGVVFQD-FK-LLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSI 152
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-196 |
2.30e-62 |
|
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: 193.84 E-value: 2.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikEKEIPFVR 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 504478437 159 VIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHN 196
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHD 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
6.77e-62 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 196.83 E-value: 6.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvrRK 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
6.87e-62 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 193.11 E-value: 6.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQD--FKLLPKLTVFENVAFALEV--IGEQPSVIKKRVLEVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
1.34e-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: 190.02 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKI 81
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRLSeEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
6.67e-60 |
|
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: 187.35 E-value: 6.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAiKEKEIPFVRRKI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFAL-EVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.39e-59 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 185.47 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkEKEIPFVRRKI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFAlevigeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
9.82e-58 |
|
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: 182.07 E-value: 9.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNgVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvrRKI 81
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
2.36e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.97 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNgVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEkeipfVR-RK 80
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP-----PReRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 161 ADEPTGNLDPDTSWEV----MKTLEEInnrGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG1118 157 LDEPFGALDAKVRKELrrwlRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
3.65e-55 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 183.57 E-value: 3.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPT---KGQILINHKDLAAIKEKEIpf 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 vRRKIGVVFQDFK--LLPkLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:COG1123 82 -GRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-195 |
5.81e-55 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 177.59 E-value: 5.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRK 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504478437 159 VIADEPTGNLDP-------DtswEVMKTLEEInnrGTTVVMATH 195
Cdd:COG1125 158 LLMDEPFGALDPitreqlqD---ELLRLQREL---GKTIVFVTH 195
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-210 |
4.00e-54 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 172.41 E-value: 4.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEI-PFVRRKIG 82
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAsKFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 163 EPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNtMKKRVIAI 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
6.05e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 173.45 E-value: 6.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfv 77
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFK--LLPKLTVFENVAFALEVIGEQPsvIKKRVLEVLDLVQLKHKAR-QFPDQLSGGEQQRVSIARSIVN 154
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSFLdRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEINN-RGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-218 |
7.96e-54 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 173.31 E-value: 7.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFA----LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNkeiVNTMKK---RVIAIEDGIIVRD 218
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHD---LNLAARyadRLVLLKDGRIVAQ 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
1.36e-53 |
|
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: 172.10 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQL--KHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
5.66e-53 |
|
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: 167.44 E-value: 5.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEIPFVRRKIGVVFQDFKLLPKLTVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 98 ENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKA----RQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
7.54e-53 |
|
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: 171.07 E-value: 7.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkDLAAIKEKEIPFVRRK 80
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPK-----LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:TIGR04520 79 VGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINN-RGTTVVMATHN-KEIVntMKKRVIAIEDGIIVRD 218
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDmEEAV--LADRVIVMNKGKIVAE 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
2.58e-52 |
|
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: 179.26 E-value: 2.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYP-NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekEIPFVRRK 80
Cdd:COG2274 474 IELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLG------DPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEivnTMKK--RVIAIEDGIIVRDESRGE 223
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLS---TIRLadRIIVLDKGRIVEDGTHEE 695
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
5.18e-52 |
|
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: 167.74 E-value: 5.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDLAAIKEKEIPf 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VRRKIGVVFQDFKLLPKlTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQL--KHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:cd03260 79 LRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLkEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRgTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
5.67e-52 |
|
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: 167.90 E-value: 5.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNgVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvrRKI 81
Cdd:cd03296 3 IEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEV--IGEQPS--VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkpRSERPPeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-216 |
6.41e-52 |
|
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: 168.98 E-value: 6.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK-IGVVFQDFKLLPKLT 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504478437 176 VMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03294 199 MQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
1.25e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL--AAIKEKEIpfvR 78
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLI---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
5.36e-51 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 163.32 E-value: 5.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVafalevigeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNkeiVNTMKK--RVIAIEDG 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHR---LSTIRDadRIIVLDDG 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
1.35e-50 |
|
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: 162.18 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGvKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRKI 81
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVafalevigeqpsvikkrvlevldlvqlkhkarqfpdQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
3.01e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGvKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILI--NHKDL-AAIKEKEIPFVR 78
Cdd:PRK11124 3 IQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
5.45e-50 |
|
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: 163.10 E-value: 5.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRK 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-223 |
1.61e-49 |
|
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: 163.01 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY----PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQdF--KLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-213 |
2.24e-49 |
|
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: 161.07 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRKI 81
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQP----------SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARS 151
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 152 IVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-225 |
2.62e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 161.33 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILI--NHKDLAA-IKEKEIPFVR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVrdesrgEYG 225
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII------EQG 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-228 |
6.81e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.42 E-value: 6.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLpKLTVFENVAFALEVIGEQpsvikkRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYGRPDATDE------EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNkeiVNTMKK--RVIAIEDGIIVrdesrgEYGSYD 228
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHR---LSTIRNadRILVLDDGRIV------EQGTHE 559
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-220 |
7.87e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 163.96 E-value: 7.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekEIPFVRRKI 81
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDES 220
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
1.38e-48 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 167.24 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDfKLLPKLTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:COG4988 414 AWVPQN-PYLFAGTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMkKRVIAIEDGIIVRDESRGE 223
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEE 557
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-216 |
1.48e-48 |
|
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: 158.61 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 27 PGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEK-EIPFVRRKIGVVFQDFKLLPKLTVFENVAFALE 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 106 viGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEI-N 184
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkK 179
|
170 180 190
....*....|....*....|....*....|..
gi 504478437 185 NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
2.98e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 158.71 E-value: 2.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeipfVRRK 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKL---LPkLTVFENVAFALevIGEQP------SVIKKRVLEVLDLVQLKHKA-RQFpDQLSGGEQQRVSIAR 150
Cdd:COG1121 77 IGYVPQRAEVdwdFP-ITVRDVVLMGR--YGRRGlfrrpsRADREAVDEALERVGLEDLAdRPI-GELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
8.56e-48 |
|
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: 155.29 E-value: 8.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIG 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQdfkllpkltvfenvafalevigeqpsvikkrvleVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:cd03214 77 YVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 163 EPTGNLDPDTSWEVMKTLEEINN-RGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
2.31e-47 |
|
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: 164.17 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRK 80
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPKL---TVFENVAFALEVIGEQpsvikkRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRV 146
Cdd:COG4987 411 IAVVPQR----PHLfdtTLRENLRLARPDATDE------ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 147 SIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMkKRVIAIEDGIIVRDESRGE 223
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-216 |
3.70e-47 |
|
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: 159.05 E-value: 3.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRKIGVVFQDFKLLPKLTV 96
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL-----PPQKRDYGIVFQSYALFPNLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 97 FENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEV 176
Cdd:TIGR03265 94 ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504478437 177 MKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:TIGR03265 174 RTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-220 |
4.62e-47 |
|
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: 158.04 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 33 VVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekEIPFVRRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPS 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 113 VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVV 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180
....*....|....*....|....*....
gi 504478437 192 MATHNKEIVNTMKKRVIAIEDGIIVRDES 220
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
8.27e-47 |
|
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: 152.01 E-value: 8.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYPNGvKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKIG 82
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQdfkllpkltvfenvafalevigeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 163 EPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
1.02e-46 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 163.36 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFV 77
Cdd:PRK10535 4 LLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRK-IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNtMKKRVIAIEDGIIVRD 218
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAA-QAERVIEIRDGEIVRN 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-217 |
1.14e-46 |
|
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: 158.09 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRR-KIGVVFQDFKLLP 92
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT 172
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504478437 173 SWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:TIGR01186 165 RDSMQDELKKLQaTLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQ 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-216 |
4.31e-46 |
|
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: 152.77 E-value: 4.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEIPFVRRKI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKkrVIAIEDGIIV 216
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADK--IIVLKDGRIV 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-213 |
6.88e-46 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 152.28 E-value: 6.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVR-RKIGVV 84
Cdd:PRK11629 13 KRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 85 FQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEP 164
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 165 TGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMkKRVIAIEDG 213
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
18-213 |
1.62e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 150.35 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKekeIPFVRRKIGVVFQDFKLLPKlTVF 97
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQEPALWGG-TVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQPSviKKRVLEVLDLVQLKHKARQFP-DQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEV 176
Cdd:COG4619 92 DNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRV 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 177 MKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:COG4619 170 EELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-196 |
4.20e-45 |
|
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: 152.90 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKP---TKGQILINHKDLAAIKEKEI 74
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 75 PFVR-RKIGVVFQD-FKLL-PKLTVFENVAFALEV-IGEQPSVIKKRVLEVLDLVQL---KHKARQFPDQLSGGEQQRVS 147
Cdd:COG0444 81 RKIRgREIQMIFQDpMTSLnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 148 IARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINN-RGTTVVMATHN 196
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHD 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-215 |
4.35e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 153.70 E-value: 4.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNgVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvrRKI 81
Cdd:PRK10851 3 IEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIG--EQPS--VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVLPrrERPNaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-210 |
6.49e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 153.84 E-value: 6.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekEIPFVRRK 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 161 ADEPTGNLDPD----TSWEVMKTLEEInnrGTTVVMATHNKEIVNTMKKRvIAI 210
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGR-IAI 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
2.46e-44 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 146.80 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKeKEIPFVRRKIGVVFQDF-K 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-KGLLERRQRVGLVFQDPdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLD 169
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|
gi 504478437 170 PDTSWEVMKTLEEINNRGTTVVMATHNKEI 199
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
7.58e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 147.70 E-value: 7.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeiPFV 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRkiGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 158 VVIADEPTGNLDPDTSwEVMKT--LEEINNRGTTVVMATHNKE 198
Cdd:COG4525 155 FLLMDEPFGALDALTR-EQMQEllLDVWQRTGKGVFLITHSVE 196
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-216 |
8.31e-44 |
|
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: 147.10 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekEIPFVRRKIGVVFQDFKLLPKLTVF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVM 177
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 178 KTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03299 170 EELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.75e-43 |
|
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: 145.59 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRKI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 162 DEPTGNLDPDTS---WEVMKTLEEINnrGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:cd03265 156 DEPTIGLDPQTRahvWEYIEKLKEEF--GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-209 |
2.19e-43 |
|
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: 144.98 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeipfVRRKIG 82
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQ------DFkllPkLTVFENVAFAL----EVIGEQPSVIKKRVLEVLDLVQLKHKA-RQFpDQLSGGEQQRVSIARS 151
Cdd:cd03235 72 YVPQrrsidrDF---P-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELAdRQI-GELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 152 IVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNT-------MKKRVIA 209
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEyfdrvllLNRTVVA 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-223 |
3.58e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 147.15 E-value: 3.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRKIGVVFQDF 88
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 169 DPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
6.79e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.51 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpnGVKALNgVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRK 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALevigeQPS-----VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGL-----RPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
6.96e-43 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 145.18 E-value: 6.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRK 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--ARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFA---------LEVIGEQPSV------IKKRVLEVLDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAaharlgrglLAALLRLPRArreereARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
9.82e-43 |
|
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: 144.11 E-value: 9.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYP----NGVK--ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHK----DLAAIK 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 71 EKEIPFVRRK-IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSI 148
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-196 |
1.21e-42 |
|
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: 143.41 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfVRRK 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA----ARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHN 196
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHS 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
1.27e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.51 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIK-----EKEIP 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FVRRKIGVVFQDFKLLPKLTVFENVAfalevigEQPSVIKK--------RVLEVLDLVQLKHKARQFPDQLSGGEQQRVS 147
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENII-------EGPVIVKGepkeeataRARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 148 IARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-169 |
3.76e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 145.26 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD-FKLL-P 92
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpYASLnP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIGEQPSV-IKKRVLEVLDLVQLK--HkARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLD 169
Cdd:COG4608 111 RMTVGDIIAEPLRIHGLASKAeRRERVAELLELVGLRpeH-ADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-215 |
5.53e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 143.19 E-value: 5.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKE----------KEIPFVRRKIGVVF 85
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDFKLLPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-215 |
1.01e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 142.48 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaikeKEIPFVRRKIGV 83
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.11e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.26 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDfkllP-----KLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:PRK13647 82 GLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-216 |
1.15e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 138.34 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRKIGVVFQDFKLLPK 93
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVIGeqPSVIKKRVLEVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT 172
Cdd:cd03224 90 LTVEENLLLGAYARR--RAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504478437 173 SWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.71e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 139.44 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKeKEIPFVRRK 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQ--DFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:PRK13639 80 VGIVFQnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 159 VIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-195 |
1.86e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 139.17 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILIN----------HKDLAAIK 70
Cdd:COG4598 8 ALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkpdrDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 71 EKEIPFVRRKIGVVFQDFKLLPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIA 149
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
2.74e-40 |
|
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: 137.32 E-value: 2.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGvKALNGVSVAIHPGEFVyVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfVRRKI 81
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
2.85e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 138.44 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvrRK 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 504478437 161 ADEPTGNLD 169
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-218 |
4.40e-39 |
|
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: 134.16 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 22 SVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRKIGVVFQDFKLLPKLTVFENVA 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-----PPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 102 FALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLE 181
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 182 EIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03298 173 DLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
1.18e-38 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 133.75 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeiPFVRRKigVVFQDFKLLPKLTVF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE------PGPDRM--VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQPSVIKKR--VLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 504478437 176 VMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:TIGR01184 153 LQEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-216 |
1.49e-38 |
|
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: 133.12 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTmkKRVIAIEDGIIV 216
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA--DKILVLDDGKII 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.54e-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: 132.79 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNgVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekeiPFVRRKI 81
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 162 DEPTGNLDPdTSWEVMKT-LEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03269 153 DEPFSGLDP-VNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-195 |
1.79e-38 |
|
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: 131.90 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI--YREEKPTKGQILINHKDLAAIKekeipfVRRKIGVVFQDFKLLPKLT 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS------FRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:cd03213 99 VRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|
gi 504478437 176 VMKTLEEINNRGTTVVMATH 195
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIH 169
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-198 |
2.18e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.22 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 20 GVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKP---TKGQILINHKDLAAIkekeiPFVRRKIGVVFQDFKLLPKLTV 96
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-----PAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 97 FENVAFALevigeqPSVIKK-----RVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:COG4136 94 GENLAFAL------PPTIGRaqrraRVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180
....*....|....*....|....*...
gi 504478437 172 TSWEVMK-TLEEINNRGTTVVMATHNKE 198
Cdd:COG4136 168 LRAQFREfVFEQIRQRGIPALLVTHDEE 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
2.41e-38 |
|
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: 132.49 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPN---GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFV 77
Cdd:cd03266 1 MITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-195 |
2.61e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 138.62 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL------AAIkekei 74
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsprDAI----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 75 pfvRRKIGVVFQDFKLLPKLTVFENVAFALEvigeqpsvikKRVLEVLDLVQLKHKARQF---------PD----QLSGG 141
Cdd:COG3845 79 ---ALGIGMVHQHFMLVPNLTVAENIVLGLE----------PTKGGRLDRKAARARIRELserygldvdPDakveDLSVG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 142 EQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
4.33e-38 |
|
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: 131.94 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLpKLTVFENVAFALevigeqPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITLGA------PLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHnKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITH-RPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
5.02e-38 |
|
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: 132.52 E-value: 5.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQ--ILINHK----DLAAIkekei 74
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGERrggeDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 75 pfvRRKIGVVFQDF--KLLPKLTVFENV---AFAleVIG--EQPSVI-KKRVLEVLDLVQLKHKA-RQFpDQLSGGEQQR 145
Cdd:COG1119 77 ---RKRIGLVSPALqlRFPRDETVLDVVlsgFFD--SIGlyREPTDEqRERARELLELLGLAHLAdRPF-GTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRG-TTVVMATHNKE-IVNTMkKRVIAIEDGIIVRD 218
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAA 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-217 |
5.46e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.23 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEIPfvRRKI 81
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQ--QRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
5.52e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.06 E-value: 5.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfVRRK 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIkkRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-216 |
2.35e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaiKEKEIPFVRRK 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPK-----LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:PRK13635 83 VGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGT-TVVMATHNKEIVnTMKKRVIAIEDGIIV 216
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEA-AQADRVIVMNKGEIL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
2.71e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 132.13 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY----PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKD------------ 65
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 66 ------LAAIKEKEIPFV---RRKIGVVFQ--DFKLLpKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQ- 133
Cdd:PRK13651 83 vleklvIQKTRFKKIKKIkeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 134 FPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*
gi 504478437 214 IIVRD 218
Cdd:PRK13651 242 KIIKD 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
4.58e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.21 E-value: 4.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAY----PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEkeipF 76
Cdd:COG1101 1 MLELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VR-RKIGVVFQDFKL--LPKLTVFENVAFAL---EVIGEQPSVIKKRV------LEVLDLvQLKHKARQFPDQLSGGEQQ 144
Cdd:COG1101 77 KRaKYIGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRelfrelLATLGL-GLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 145 RVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNkeivntMKK------RVIAIEDGIIVR 217
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN------MEQaldygnRLIMMHEGRIIL 229
|
.
gi 504478437 218 D 218
Cdd:COG1101 230 D 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-207 |
4.93e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 129.51 E-value: 4.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVR-RKIGVVFQDFKLLPKLTV 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 97 FENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEV 176
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190
....*....|....*....|....*....|..
gi 504478437 177 MKTLEEINNR-GTTVVMATHNKEIVNTMKKRV 207
Cdd:PRK10584 186 ADLLFSLNREhGTTLILVTHDLQLAARCDRRL 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
5.56e-37 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 130.13 E-value: 5.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIK----MIYREEKP-TKGQILINHKDLAAIKEKEIP 75
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAgSHIELLGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FVRRKIGVVFQDFKLLPKLTVFENVAFAleVIGEQP----------SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIG--ALGSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGEY 224
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
6.10e-37 |
|
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: 135.49 E-value: 6.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipFVRRKI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVAFALeviGEQPSVIKKRVLEVLDLVQLKHKARQFPDQ--------LSGGEQQRVSIARSIV 153
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLAR---PDASDAEIREALERAGLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMKKRV 207
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIV 527
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-226 |
8.00e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 130.61 E-value: 8.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeipfVRRK 80
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE-------DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV----RDESRGEYGS 226
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsgsVDEIRRQFGR 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-217 |
9.73e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 132.85 E-value: 9.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 22 SVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK-IGVVFQDFKLLPKLTVFENV 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 101 AFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTL 180
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 181 EEINNRGT-TVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-223 |
1.06e-36 |
|
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: 129.54 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQDF--KLLPKLT 95
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSpsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALE-VIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTS 173
Cdd:TIGR02769 107 VRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 174 WEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:TIGR02769 187 AVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-196 |
2.21e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.18 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDLAAiKEKEIPFVRRKIGVVF 85
Cdd:TIGR00972 10 FYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRmndlvPGVRIEGKVLFDGQDIYD-KKIDVVELRRRVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDFKLLPKlTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQL----KHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:TIGR00972 89 QKPNPFPM-SIYDNIAYGPRLHGIKDkKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEVLL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRgTTVVMATHN 196
Cdd:TIGR00972 168 LDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHN 202
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
2.77e-36 |
|
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: 127.35 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN-GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAtHNkeiVNTMKK--RVIAIEDGIIVrdesrgEYGSY 227
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HR---LSTIENadRIVVLEDGKIV------ERGTH 220
|
.
gi 504478437 228 D 228
Cdd:cd03251 221 E 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-216 |
2.85e-36 |
|
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: 127.66 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN--GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEIPFVRR 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDfkllPKL---TVFENVAFALevigeqPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQR 145
Cdd:cd03249 78 QIGLVSQE----PVLfdgTIAENIRYGK------PDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNkeiVNTMKK--RVIAIEDGIIV 216
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHR---LSTIRNadLIAVLQNGQVV 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
4.96e-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: 126.18 E-value: 4.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEkeipfVRRKI 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENvafaLEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03268 75 GALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-196 |
5.38e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 126.64 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRK 80
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENvafaLEV---IGEQPSVIKKRVLEVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEEN----LLLgayARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQN 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
6.98e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 132.50 E-value: 6.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEkPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD-F-KLLP 92
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFgSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIGEQPSV--IKKRVLEVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLD 169
Cdd:COG4172 378 RMTVGQIIAEGLRVHGPGLSAaeRRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 170 PDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG4172 458 VSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-215 |
7.40e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.10 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfvrrkIGVVFQDFKLLPKLTVF 97
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED--------TRLMFQDARLLPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEviGEQpsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVM 177
Cdd:PRK11247 100 DNVGLGLK--GQW----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 178 KTLEEI-NNRGTTVVMATHN-KEIVnTMKKRVIAIEDGII 215
Cdd:PRK11247 174 DLIESLwQQHGFTVLLVTHDvSEAV-AMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
9.07e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.41 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkDLAAIKEKEIPFVRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---DGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDfkllPK-----LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:PRK13632 84 KIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGT-TVVMATHN-KEIVNTmkKRVIAIEDGIIVR 217
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDmDEAILA--DKVIVFSEGKLIA 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-218 |
2.81e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVK-----ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhKDLAAIKEKEIP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FVRRKIGVVFQ--DFKLLPKLtVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATH-NKEIVNTmkKRVIAIEDGIIVRD 218
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHyMEEAVEA--DRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-216 |
2.89e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAiKEKEIPFVRRKIGVVFQ--DFKLLPK 93
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 lTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504478437 172 TSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13637 179 GRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-196 |
3.37e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.15 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR--EEKP---TKGQILINHKDLAAiKEKEIPFVRRKIGVVFQDFKL 90
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 LPKlTVFENVAFALEVIGE-QPSVIKKRVLEVLDLVQL----KHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:COG1117 104 FPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190
....*....|....*....|....*....|.
gi 504478437 166 GNLDPDTSWEVMKTLEEINNRgTTVVMATHN 196
Cdd:COG1117 183 SALDPISTAKIEELILELKKD-YTIVIVTHN 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-213 |
4.81e-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: 122.32 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKA-LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVafalevigeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMkKRVIAIEDG 213
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-216 |
5.20e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.52 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaIKEKEipfVRRKIGVVFQD--F 88
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE---RRKSIGYVMQDvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPKlTVFENVAFALEVIGEQPSVIKKrVLEVLDLVQLKHkarQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:cd03226 83 QLFTD-SVREELLLGLKELDAGNEQAET-VLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 169 DPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
6.06e-35 |
|
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: 129.92 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI--YREEKPTKGQILIN----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 63 -------------HKDLAAIKEKEIPFVRRKIGVVFQ-DFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLK 128
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 129 HKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEE-INNRGTTVVMATHNKEIVNTMKKRV 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 504478437 208 IAIEDGIIV 216
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
1.64e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 123.94 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaAIKEKEIPFVRRK 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPKL-----TVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:PRK13644 79 VGIVFQN----PETqfvgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTmKKRVIAIEDGIIV 216
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-223 |
2.47e-34 |
|
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: 122.59 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY-PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekEIPFVRRK 80
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:cd03252 78 VGVVLQENVLFNR-SIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTmKKRVIAIEDGIIVRDESRGE 223
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-228 |
2.71e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.26 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQDF--KLLPKLT 95
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFAL-EVIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTS 173
Cdd:PRK10419 108 VREIIREPLrHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 174 WEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGEYGSYD 228
Cdd:PRK10419 188 AGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFS 243
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
16-196 |
6.30e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 121.50 E-value: 6.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaikEKEIPFVRRKIGVVF--QDFKLLPK 93
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLPMHKRARLGIGYlpQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTS 173
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180
....*....|....*....|...
gi 504478437 174 WEVMKTLEEINNRGTTVVMATHN 196
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITDHN 192
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-195 |
9.92e-34 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 120.84 E-value: 9.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI---YREEKPTKGQILINHKdlaaikEKEIPFVRRKIGVVFQDFKLL 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ------PRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 PKLTVFENVAFALEVIG--EQPSVIKKRVLEVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:cd03234 94 PGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
2.50e-33 |
|
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: 117.53 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikEKEIPF----- 76
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--------GKEVSFasprd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 -VRRKIGVVFqdfkllpkltvfenvafalevigeqpsvikkrvlevldlvqlkhkarqfpdQLSGGEQQRVSIARSIVNN 155
Cdd:cd03216 72 aRRAGIAMVY---------------------------------------------------QLSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN-KEIVNTmKKRVIAIEDGIIV 216
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEI-ADRVTVLRDGRVV 161
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-169 |
3.35e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 122.00 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD--FKLLP 92
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVfenvafalEVIGEQPSVI---------KKRVLEVLDLVQLK--HKARqFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK11308 108 RKKV--------GQILEEPLLIntslsaaerREKALAMMAKVGLRpeHYDR-YPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 504478437 162 DEPTGNLD 169
Cdd:PRK11308 179 DEPVSALD 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
4.81e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.42 E-value: 4.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPfvrRK 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAF--------ALEVIGEQpsvIKKRVLEVLDLVQLKHKarqFPDQLSGGEQQRVSIARSI 152
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfpyskgRLTAEDRE---IIDEAIAYLDLEDLADR---YLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-216 |
5.15e-33 |
|
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: 124.83 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYP-NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFaleviGEQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAtHNkeiVNTMKK--RVIAIEDGIIV 216
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HR---LSTIEKadRIVVMDDGRIV 546
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.00e-32 |
|
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: 123.62 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLA------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHN 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-195 |
1.96e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.29 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRrkiGVVFQDFKL-LPkLTV 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR---AVLPQHSSLaFP-FTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 97 FENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKA-RQFPdQLSGGEQQRVSIARsivnnpdvVIA-------------- 161
Cdd:COG4559 93 EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAgRSYQ-TLSGGEQQRVQLAR--------VLAqlwepvdggprwlf 163
|
170 180 190
....*....|....*....|....*....|....*
gi 504478437 162 -DEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:COG4559 164 lDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
2.06e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.87 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKS-TFIKMI----YREEKPTkGQILINHKDLAAIKEKEIPFVR-RKIGVVFQD- 87
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGLSERELRRIRgNRIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 88 -FKLLPKLTVFENVAfalEVI----GEQPSVIKKRVLEVLDLVQLKHKAR---QFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:COG4172 102 mTSLNPLHTIGKQIA---EVLrlhrGLSGAAARARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
2.24e-32 |
|
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: 123.39 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKI 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDfkllPKL---TVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRVS 147
Cdd:COG5265 435 GIVPQD----TVLfndTIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 148 IARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMA------THNKEIvntmkkrvIAIEDGIIV 216
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAhrlstiVDADEI--------LVLEAGRIV 571
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
2.26e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 117.88 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeiPFVRRk 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 iGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 161 ADEPTGNLDPDTSwEVMKT--LEEINNRGTTVVMATHNKE 198
Cdd:PRK11248 152 LDEPFGALDAFTR-EQMQTllLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-213 |
2.59e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 118.30 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEV-YKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikEKEIPFVR 78
Cdd:PRK13650 4 IIEVKNLtFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDfkllPK-----LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13650 81 HKIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVnTMKKRVIAIEDG 213
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-195 |
3.76e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHK--DLAAIKEKEipfvR 78
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDAQ----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKLTVFENVAfalevIGEQPS--------VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIF-----LGREPRrgglidwrAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDtswEV---MKTLEEINNRGTTVVMATH 195
Cdd:COG1129 154 ALSRDARVLILDEPTASLTER---EVerlFRIIRRLKAQGVAIIYISH 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.37e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.06 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaAIKEKEIPFVRRK 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQ---DFKLLPklTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK13652 80 VGLVFQnpdDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-216 |
2.46e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 120.19 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN--GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRR 79
Cdd:TIGR02204 338 IEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE---LRA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSI 148
Cdd:TIGR02204 415 RMALVPQDPVLFAA-SVMENIRYG------RPDATDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAtHNkeiVNTMKK--RVIAIEDGIIV 216
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA-HR---LATVLKadRIVVMDQGRIV 553
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
3.35e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY----PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAA-IKEKEIPF 76
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VRRKIGVVFQdfklLPKLTVFE-----NVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKAR-QFPDQLSGGEQQRVSIAR 150
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINN-RGTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-218 |
3.50e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.29 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 22 SVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRRKIGVVFQDFKLLPKLTVFENVA 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT-----PPSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 102 F----ALEVIGEQpsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVM 177
Cdd:PRK10771 94 LglnpGLKLNAAQ----REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504478437 178 KTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:PRK10771 170 TLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
3.54e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.72 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaIKEKEIPFVRRK 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQD-FKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
7.10e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.29 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikeKEIPFVRRKI 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 162 DEPTGNLDPDTS---WEVMKTLEEinnRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK13537 163 DEPTTGLDPQARhlmWERLRSLLA---RGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
1.04e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.39 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFAlevigeQPSVIKKRVLEVLDLVQLkHKARQFPD-----------QLSGGEQQRVSIA 149
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGL-EKLLEDDKglnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMkKRVIAIEDGIIVrdesrgEYGSYD 228
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQII------EQGTHQ 558
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-228 |
1.90e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.75 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENV------------------AFALEVIGEQPSVIKKRVLEvldlvqlkhKARqfpdQLSGGEQ 143
Cdd:PRK13657 412 AVVFQDAGLFNR-SIEDNIrvgrpdatdeemraaaerAQAHDFIERKPDGYDTVVGE---------RGR----QLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 144 QRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTmkKRVIAIEDGIIVrdesrgE 223
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA--DRILVFDNGRVV------E 549
|
....*
gi 504478437 224 YGSYD 228
Cdd:PRK13657 550 SGSFD 554
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-213 |
2.79e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.82 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 35 GPSGAGKSTFIKMIYREEKPTKGQILINHKDLA-AIKEKEIPFVRRKIGVVFQDFKLLPKLTVFENVAFAL-EVIGEQPS 112
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMkRARPSERR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 113 VIKKRVLEVLDLvqlKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVV 191
Cdd:TIGR02142 110 ISFERVIELLGI---GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPIL 186
|
170 180
....*....|....*....|..
gi 504478437 192 MATHNKEIVNTMKKRVIAIEDG 213
Cdd:TIGR02142 187 YVSHSLQEVLRLADRVVVLEDG 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-216 |
3.76e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILI-NHKDLAAIKE-KEIPFVRRKIGVVFQ 86
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKiKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 --DFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK13645 98 fpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 164 PTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-216 |
6.77e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAY----PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAI-KEKEIP 75
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FVRRKIGVVFQ--DFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSI 152
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-195 |
1.74e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDlaaIKEKEIPFVRRKIGVVFQDFK 89
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQD---IFKMDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKLTVFENVAFALEV--IGEQPSVIKKRVLEVLDLVQLKHKARQFPD----QLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK14247 93 PIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|..
gi 504478437 164 PTGNLDPDTSWEVMKTLEEInNRGTTVVMATH 195
Cdd:PRK14247 173 PTANLDPENTAKIESLFLEL-KKDMTIVLVTH 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
2.40e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.85 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkdLAAIKEKEIPFVRRKI 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 162 DEPTGNLDPDTS---WEVMKTLEEinnRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK13536 197 DEPTTGLDPHARhliWERLRSLLA---RGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-196 |
3.12e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 109.29 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLA--AIKEKeipfVRRKIGVVFQ 86
Cdd:TIGR04406 9 KSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlPMHER----ARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 DFKLLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:TIGR04406 84 EASIFRKLTVEENIMAVLEIRKDLDrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190
....*....|....*....|....*....|.
gi 504478437 166 GNLDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDHN 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-217 |
3.81e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGV----KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAI-KEKEIPF 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VRRKIGVVFQ--DFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKAR-QFPDQLSGGEQQRVSIARSIV 153
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFeKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 154 NNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-217 |
5.28e-29 |
|
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: 111.35 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL----AAIkekeipFV---RRKIGVVFQDFKLLPK 93
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGI------FLpphRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVIGEQPSVIkkRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTS 173
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504478437 174 WEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:COG4148 170 AEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-196 |
1.17e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.59 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDlaaIKEKEIPF--VRRKIGVVFQDF 88
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmneleSEVRVEGRVEFFNQN---IYERRVNLnrLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPkLTVFENVAFALEVIGEQPSV----IKKRVLEVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRGT-TVVMATHN 196
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-218 |
1.18e-28 |
|
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: 107.80 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikeKEIPFVRRK-----IGVVF-QDF 88
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA---------GLVPWKRRKkflrrIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 169 DPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:cd03267 185 DVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-226 |
1.28e-28 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 107.19 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY-PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPKL---TVFENvafaLEVIGEQPSvikKRVLEVLDLVQLKHKARQFPDQL-----------SGGEQQRV 146
Cdd:cd03244 80 ISIIPQD----PVLfsgTIRSN----LDPFGEYSD---EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 147 SIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEiNNRGTTVVMATHNkeiVNTMKK--RVIAIEDGIIVrdesrgEY 224
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHR---LDTIIDsdRILVLDKGRVV------EF 218
|
..
gi 504478437 225 GS 226
Cdd:cd03244 219 DS 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-221 |
1.48e-28 |
|
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: 107.17 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN--GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipFVRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDFKLLPKlTVFENVAFALevigeqPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSI 148
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGL------QSCSFECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHnkeiVNTMKKrviaiEDGIIVRDESR 221
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR----LSTVER-----ADQILVLDGGR 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-217 |
2.37e-28 |
|
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: 111.67 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkDLAAIKEKEIPFVRRK 80
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL---DGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQlkhkarQFPD-----------QLSGGEQQRVSIA 149
Cdd:TIGR01842 394 IGYLPQDVELFPG-TVAENIARFGENADPEKIIEAAKLAGVHELIL------RLPDgydtvigpggaTLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKrVIAIEDGIIVR 217
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDK-ILVLQDGRIAR 533
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-196 |
2.69e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.17 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDLAAIKEKEIPfVRRKIGVVF 85
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnPEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDFKLLPkLTVFENVAFALEVIGEQPSVIKKRVLE-------VLDLVqlKHKARQFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkslkgasIWDEV--KDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 159 VIADEPTGNLDPDTSWEVMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRS 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
3.69e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 106.65 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeiPFVRR- 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-----PMHKRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGV--------VFQdfkllpKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARS 151
Cdd:COG1137 77 RLGIgylpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170
....*....|....*....
gi 504478437 152 IVNNPDVVIADEPTGNLDP 170
Cdd:COG1137 151 LATNPKFILLDEPFAGVDP 169
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-195 |
6.82e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 110.52 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-YREEKPTKGQ--ILINHKDLaaikekEIPFVRRKIGVVFQDFKLLPKL 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKGSgsVLLNGMPI------DAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 95 TVFENVAFALEV-IGEQPSVIKK--RVLEVLDLVQLKHKAR---QFPDQ---LSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:TIGR00955 115 TVREHLMFQAHLrMPRRVTKKEKreRVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 504478437 166 GNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-228 |
9.69e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.48 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD--FK 89
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKLTVFENVAFALEVIgeQPSV----IKKRVLEVLDLVQL-KHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEP 164
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTY--HPKLsrqeVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 165 TGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVrdesrgEYGSYD 228
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV------ELGTYD 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-196 |
1.02e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.00 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQDFKLLPKLTVFENV 100
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 101 AFAL-EVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKT 179
Cdd:PRK11831 106 AYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170
....*....|....*...
gi 504478437 180 LEEINNR-GTTVVMATHN 196
Cdd:PRK11831 186 ISELNSAlGVTCVVVSHD 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-228 |
1.06e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInHKDLaaikekeipfvrrKIGV 83
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGL-------------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFKLLPKLTVFENVAFALEVIGE-------------QPSVIKKRV------LEVLDLVQLKHKARQ------FPD-- 136
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRAleaeleeleaklaEPDEDLERLaelqeeFEALGGWEAEARAEEilsglgFPEed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 137 ------QLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT-SWevmktLEE-INNRGTTVVMATHNKEIVNTMKKRVI 208
Cdd:COG0488 146 ldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiEW-----LEEfLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
250 260
....*....|....*....|.
gi 504478437 209 AIEDGIIVRdesrgeY-GSYD 228
Cdd:COG0488 221 ELDRGKLTL------YpGNYS 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
1.07e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.55 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYP-NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfVRRK 80
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENvafalevIGEQpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNN-------LGRR---------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATHNKEIVNTMKKrVIAIEDGIIV 216
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDK-ILFLENGKII 175
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-196 |
3.87e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.45 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDfkllPK-----LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:PRK13648 84 HIGIVFQN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHN 196
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHD 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-217 |
6.62e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.58 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAY---PNGV-KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPF 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VR----RKIGVVFQDFKLLPKLTVFENV--AFALEVIGEqpsVIKKRVLEVLDLVQL-KHKAR----QFPDQLSGGEQQR 145
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLteAIGLELPDE---LARMKAVITLKMVGFdEEKAEeildKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTSWEV----MKTLEEINNrgtTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVthsiLKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-220 |
6.92e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.17 E-value: 6.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM----IYreekPTKGQILINHKDlaaIKEKEIPFVRRkIGVVF-QDFK 89
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMltgiLV----PTSGEVRVLGYV---PFKRRKEFARR-IGVVFgQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKLTVFENvaFAL--EVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:COG4586 107 LWWDLPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 168 LDPDTSWEVMKTLEEINN-RGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDES 220
Cdd:COG4586 185 LDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-215 |
8.05e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 102.48 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILIN-----HKDLaaikekeipf 76
Cdd:TIGR03740 1 LETKNLSKRFGKQT-AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDghpwtRKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 vrRKIGVVFQDFKLLPKLTVFENvafaLEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:TIGR03740 70 --HKIGSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-216 |
1.09e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.10 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKST----FIKMIyreekPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD--FKL 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 LPKLTVFENVAFALEVigEQPSVIKK----RVLEVLDLVQLKHKARQ-FPDQLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:PRK15134 376 NPRLNVLQIIEEGLRV--HQPTLSAAqreqQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504478437 166 GNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-220 |
1.92e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGV----KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAA-IKEKEIPF 76
Cdd:PRK13641 3 IKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 VRRKIGVVFQdfklLPKLTVFEN-----VAFALEVIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSIAR 150
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDES 220
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-191 |
4.11e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPfvrRKIGVVFQDFKLLPKLTVF 97
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA---RRRAVLPQHSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKA-RQFPdQLSGGEQQRVSIAR------SIVNNPDVVIADEPTGNLDP 170
Cdd:PRK13548 95 EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARvlaqlwEPDGPPRWLLLDEPTSALDL 173
|
170 180
....*....|....*....|..
gi 504478437 171 DTSWEVMKTLEEI-NNRGTTVV 191
Cdd:PRK13548 174 AHQHHVLRLARQLaHERGLAVI 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-216 |
6.78e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN--GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaiKEKEIPFVRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDfKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQlkhkarQFPD-----------QLSGGEQQRVSI 148
Cdd:TIGR00958 556 QVALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM------EFPNgydtevgekgsQLSGGQKQRIAI 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPdtswEVMKTLEEINNRGT-TVVMATHNKEIVNTMKKrVIAIEDGIIV 216
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASrTVLLIAHRLSTVERADQ-ILVLKKGSVV 692
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-196 |
1.44e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGvKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPfvrRK 80
Cdd:PRK11231 2 TLRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFkLLPK-LTVFENVAFA----LEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:PRK11231 78 LALLPQHH-LTPEgITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-219 |
1.71e-25 |
|
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: 103.67 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQDFKLLPKlTVF 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRHIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVA-FAlEVIGEQpsVIK--KRVlEVLDLVQlkhkarQFPD-----------QLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:COG4618 424 ENIArFG-DADPEK--VVAaaKLA-GVHEMIL------RLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKrVIAIEDGIIV----RDE 219
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDK-LLVLRDGRVQafgpRDE 552
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-228 |
2.64e-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: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVafaleVIGEQPSVIKKRVLEVLDLVQLKHKARQFP-----------DQLSGGEQQRVSIAR 150
Cdd:TIGR01193 551 NYLPQEPYIFSG-SILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRgtTVVMATHNKEIVNtMKKRVIAIEDGIIVrdesrgEYGSYD 228
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAK-QSDKIIVLDHGKII------EQGSHD 693
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-228 |
2.98e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaaikekeipfVrrK 80
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET------------V--K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLL-PKLTVFENVAFALEVIGEQpsvikkrvlevldlvqlkhKARQF-------PDQ-------LSGGEQQR 145
Cdd:COG0488 380 IGYFDQHQEELdPDKTVLDELRDGAPGGTEQ-------------------EVRGYlgrflfsGDDafkpvgvLSGGEKAR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDtswevmkTLEEINN-----RGtTVVMATHNKEIVNTMKKRVIAIEDGIIVrdes 220
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIE-------TLEALEEalddfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR---- 508
|
....*....
gi 504478437 221 rgEY-GSYD 228
Cdd:COG0488 509 --EYpGGYD 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-216 |
3.61e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAA-IKEKEIPFVRRKIGVVFQd 87
Cdd:PRK13646 14 KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVRKRIGMVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 88 fklLPKLTVFEN-----VAFALEVIGEQPSVIKKRVLEVL-DLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:PRK13646 93 ---FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLmDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 162 DEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-196 |
4.08e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDLAAiKEKEIPFVRRKIGVVFQDFKLL 91
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndliPGFRVEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 PKlTVFENVAFALEVIGEQ---PSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180
....*....|....*....|....*...
gi 504478437 169 DPDTSWEVMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14243 183 DPISTLRIEELMHELKEQ-YTIIIVTHN 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-223 |
8.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikeKEIPFVRRKIGVVFQD-FKLLPK 93
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTS 173
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 174 WEVMKTLEEINNR-GTTVVMATHNKEIVNTmKKRVIAIEDGIIVRDESRGE 223
Cdd:PRK13642 177 QEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-221 |
1.16e-24 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 101.49 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPT--KGQILINHKDLAaikeKEIpfvRRKIGVVFQDFKLLPKLT 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQI---LKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFAL------EVIGEQPSVIKKRVLEVLDLVQLKHK--ARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PLN03211 157 VRETLVFCSllrlpkSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHNKEivntmkKRVIAIEDGIIVRDESR 221
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPS------SRVYQMFDSVLVLSEGR 284
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-200 |
1.41e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 10 AYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekeipFVRRKIGVVfqdfK 89
Cdd:NF040873 1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-------YVPQRSEVP----D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPkLTVFENVAF-------ALEVIGEQPSVIKKRVLEVLDLVQLKHkaRQFpDQLSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:NF040873 69 SLP-LTVRDLVAMgrwarrgLWRRLTRDDRAAVDDALERVGLADLAG--RQL-GELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 163 EPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIV 200
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-196 |
1.95e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.89 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipFVRRKIGVVFQDF 88
Cdd:PRK10895 11 KAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPKLTVFENVAFALEVIGEQPSVIKK-RVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180
....*....|....*....|....*....
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
4.02e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRK 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVAFALEVIGEQPsvIKKRVLEVLDLV-QLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQ--FQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDES 220
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-223 |
8.61e-24 |
|
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: 94.90 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKekeiPF--VRRKIGVVFQDFKLLPKL 94
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHerARAGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 95 TVFENVAFALEVIGEQPsviKKRVLEVLDL--VQLKHKARQFPDqLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT 172
Cdd:TIGR03410 91 TVEENLLTGLAALPRRS---RKIPDEIYELfpVLKEMLGRRGGD-LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504478437 173 SWEVMKTLEEINNRGT-TVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:TIGR03410 167 IKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-228 |
1.02e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-----YReekptkGQILINHKDLAAIKEKEIpfvRRKIGVVFQ 86
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQ------GSLKINGIELRELDPESW---RKHLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 DfKLLPKLTVFENVAFALEVIGEQpsvikkRVLEVLDLVQLKHKARQFP--------DQ---LSGGEQQRVSIARSIVNN 155
Cdd:PRK11174 431 N-PQLPHGTLRDNVLLGNPDASDE------QLQQALENAWVSEFLPLLPqgldtpigDQaagLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEiNNRGTTVVMATHNKEIVNTMKKrVIAIEDGIIVrdesrgEYGSYD 228
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIV------QQGDYA 568
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-192 |
3.21e-23 |
|
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: 92.11 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipFVRRKIGVVFQDFK---LLP 92
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFalevigeqpsvikkrvlevldlvqlkhkarqfPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT 172
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180
....*....|....*....|
gi 504478437 173 SWEVMKTLEEINNRGTTVVM 192
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLL 159
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-196 |
3.79e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYR-----EEKPTKGQILINHKDLAAIKEKEIPfVRRKIGVVFQDFKLLP 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllelnEEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIG------EQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGlvkskkELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|
gi 504478437 167 NLDPDTSWEVMKTLEEINNRgTTVVMATHN 196
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKE-YTIVLVTHS 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-223 |
9.62e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM------IYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVV 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKL---RKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 85 FQDFKLLPKLTVFENVAFALEVIG-EQPSVIKKRVLEVLDLVQL---KHKARQFP-DQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkeVYDRLNSPaSQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRgTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-201 |
1.18e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 13 NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKIGVVFQDfkllP 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQT----P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KL---TVFENVAFALEVIGEQPSviKKRVLEVLDLVQLKHKARQFP-DQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:PRK10247 91 TLfgdTVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|....
gi 504478437 169 DPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVN 201
Cdd:PRK10247 169 DESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEIN 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-196 |
1.64e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.43 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNG-VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKP----TKGQILINHKDLAAIKEKEI-PFVRRKIGVVF 85
Cdd:COG4170 16 PQGrVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrKIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDFK--LLPKLTVFENVAFAL---EVIG---EQPSVIKKRVLEVLDLVQLK-HKA--RQFPDQLSGGEQQRVSIARSIVN 154
Cdd:COG4170 96 QEPSscLDPSAKIGDQLIEAIpswTFKGkwwQRFKWRKKRAIELLHRVGIKdHKDimNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHN 196
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHD 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-219 |
2.21e-22 |
|
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: 91.05 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInHKDLAAIKEkeipfvrrkIGVVFQdf 88
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLLG---------LGGGFN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 kllPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKhkarQFPDQ----LSGGEQQRVSIARSIVNNPDVVIADEP 164
Cdd:cd03220 97 ---PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELG----DFIDLpvktYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 165 TGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDE 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-228 |
2.46e-22 |
|
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: 90.55 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY-PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRK 80
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENvafaLEVIGEQPSVIKKRVLEVldlvqlkhkaRQFPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSN----LDPFDEYSDEEIYGALRV----------SEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAtHnkeivntmKKRVIAIEDGIIVRDesRGEYGSYD 228
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFTNSTILTIA-H--------RLRTIIDYDKILVMD--AGEVKEYD 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
3.69e-22 |
|
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: 88.27 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaikekeipfvrrKI 81
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVfqdfkllpkltvfenvafalevigeqpsvikkrvlevldlvqlkhkarqfpDQLSGGEQQRVSIARSIVNNPDVVIA 161
Cdd:cd03221 66 GYF---------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 162 DEPTGNLDPDT-SWevmktLEE-INNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:cd03221 95 DEPTNHLDLESiEA-----LEEaLKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
4.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQ--DFKLLPKlTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:PRK13640 86 VGIVFQnpDNQFVGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 159 VIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNtMKKRVIAIEDGIIV 216
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLL 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
5.90e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRK 80
Cdd:PRK09700 5 YISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA--AQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKLTVFENVafaleVIGEQP------------SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSI 148
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENL-----YIGRHLtkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
8.34e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---------------------VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQI 59
Cdd:COG1134 4 MIEVENVSKSYRLYhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 60 LINHKdLAAIKEkeipfvrrkIGVVFQdfkllPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKhkarQFPDQ-- 137
Cdd:COG1134 84 EVNGR-VSALLE---------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELG----DFIDQpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 138 --LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:COG1134 145 ktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*
gi 504478437 216 VRDES 220
Cdd:COG1134 225 VMDGD 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-196 |
1.09e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.23 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPfvrRKIGVVFQDFKLLPKLTVF 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAfalevIGEQP---------SVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:PRK10575 104 ELVA-----IGRYPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180
....*....|....*....|....*....
gi 504478437 169 DPDTSWEVMKTLEEINN-RGTTVVMATHN 196
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQeRGLTVIAVLHD 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-216 |
1.21e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVVFQD--FKLLP 92
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIG-EQPSVIKKRVLEVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDP 170
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504478437 171 DTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK10261 497 SIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-216 |
1.60e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.57 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKS----TFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvRRKI-----GVVFQ 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE----RRNLvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 D--FKLLPKLTVFENVAFALEV-IGEQPSVIKKRVLEVLDLVQLKHKARQ---FPDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK11022 97 DpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-223 |
1.61e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKeKEIPFVRRKIGVVFQDfkllPKLTVF 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 -----ENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHkARQFPDQ-LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504478437 172 TSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-221 |
2.54e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 19 NGVSVAIHPGEFVYVVGPSGAGKS-TFIKMIYREEKP----TKGQILINHKDLAAIKEKEIPFVR-RKIGVVFQD--FKL 90
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEpmVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 LPKLTVFENVAfalEVI----GEQPSVIKKRVLEVLDLVQLKHKARQ---FPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK15134 106 NPLHTLEKQLY---EVLslhrGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESR 221
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-193 |
2.59e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 91.70 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKlTVFENVAFALEvIGEQpsvikkRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLGRD-ISEE------QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMA 193
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-213 |
3.04e-21 |
|
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: 92.00 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAY-PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaikEKEIPFVRRKIG 82
Cdd:TIGR01257 931 VKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 163 EPTGNLDPDTSWEVMKTLEEINNrGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
3.20e-21 |
|
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: 87.52 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGV----KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIlinhkdlaaikekeipFV 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV----------------SV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKIGVVFQdFKLLPKLTVFENVAFALEVIgeqpsviKKRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRV 146
Cdd:cd03250 65 PGSIAYVSQ-EPWIQNGTIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 147 SIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLeeINN---RGTTVVMATHNKEIVntmKK--RVIAIEDG 213
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGlllNNKTRILVTHQLQLL---PHadQIVVLDNG 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-217 |
3.58e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKG-----QILINHKDLAAI--------KEKEIPFVR 78
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNHElitnpyskKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQ--DFKLLpKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHK-ARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:PRK13631 116 RRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-195 |
4.70e-21 |
|
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: 87.03 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 13 NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaiKEKEIPfvRRKIGVVFQDFKLLP 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEP--HENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIG-EQPSVikkrvLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:TIGR01189 87 ELSALENLHFWAAIHGgAQRTI-----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 504478437 172 TSWEVMKTLEEINNRGTTVVMATH 195
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-216 |
5.75e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 33 VVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkEKEI--PFVRRKIGVVFQDFKLLPKLTVFENVAFALEvigeq 110
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDA-EKGIclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 111 psviKKRVLEVLDLVQL---KHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLE----EI 183
Cdd:PRK11144 103 ----KSMVAQFDKIVALlgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLErlarEI 178
|
170 180 190
....*....|....*....|....*....|....
gi 504478437 184 NnrgTTVVMATHN-KEIVNtMKKRVIAIEDGIIV 216
Cdd:PRK11144 179 N---IPILYVSHSlDEILR-LADRVVVLEQGKVK 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-195 |
9.02e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-----YreekpTKGQILI-NHKDLAAIKEKeiPFvrrkigvvf 85
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpY-----GSGRIARpAGARVLFLPQR--PY--------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 qdfklLPKLTVFENVAFALEVigEQPSviKKRVLEVLDLVQLKHKARQF------PDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:COG4178 437 -----LPLGTLREALLYPATA--EAFS--DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*.
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEiNNRGTTVVMATH 195
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-224 |
1.11e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKekeiPFVRRK 80
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGV--VFQDFKLLPKLTVFENVAFALevigEQPSVIKKRVLEVLDL--VQLKhkarqfPDQLSG----GEQQRVSIARSI 152
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAAlgCQLD------LDSSAGslevADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 153 VNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGEY 224
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-221 |
2.04e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaIKEKEIPfvrrkigvvfqdfkllPKLTVF 97
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFG----------------REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVigeqpsvikKRVLEVLDLVQLKHKA--RQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:COG2401 104 DAIGRKGDF---------KDAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 176 VMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIED-GIIVRDESR 221
Cdd:COG2401 175 VARNLQKLARRaGITLVVATHHYDVIDDLQPDLLIFVGyGGVPEEKRR 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-227 |
2.25e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLaaiKEKEIPFVRRK 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLLPKlTVFENVAFALEVIGEQPSVIK-KRVLEVLDLVQlkhKARQFPDQ--------LSGGEQQRVSIARS 151
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQYSREQIEEaARMAYAMDFIN---KMDNGLDTvigengvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 152 IVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAtHNkeiVNTMKK--RVIAIEDGIIVrdesrgEYGSY 227
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HR---LSTIEKadEILVVEDGEIV------ERGTH 562
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-199 |
2.40e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM---IYreekptkgqilinHKDLAAIK--EKEIP 75
Cdd:PRK10762 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVltgIY-------------TRDAGSILylGKEVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FVRRK------IGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLE----VLDLVQLKHKARQFPDQLSGGEQQR 145
Cdd:PRK10762 70 FNGPKssqeagIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAeadkLLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDpDTSWEVM-KTLEEINNRGTTVVMATHN-KEI 199
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALT-DTETESLfRVIRELKSQGRGIVYISHRlKEI 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-218 |
2.51e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKG-----QILINHKDLaaIKEKEIPFVRRKIGVVFQDF 88
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 KLLPkLTVFENV-----AFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK14271 111 NPFP-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRgTTVVMATHNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-213 |
2.96e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPfvrRKiGVV--FQDFKLL 91
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RM-GVVrtFQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 PKLTVFENVAFA---------LEVIGEQPSVIKK------RVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:PRK11300 93 REMTVIENLLVAqhqqlktglFSGLLKTPAFRRAesealdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-218 |
3.79e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM---IYreekPT---KGQILINHKDLAA--IKEK 72
Cdd:PRK13549 5 LLEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVlsgVY----PHgtyEGEIIFEGEELQAsnIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 73 EipfvRRKIGVVFQDFKLLPKLTVFENVafaleVIGEQPS--------VIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQ 144
Cdd:PRK13549 80 E----RAGIAIIHQELALVKELSVLENI-----FLGNEITpggimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 145 RVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEivntmkkRVIAIEDGIIV-RD 218
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLN-------EVKAISDTICViRD 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-197 |
3.85e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 10 AYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDlaaikeKEIPFVRRKIGVV-FQDF 88
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYLgHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 kLLPKLTVFENVAFALEVIGEQPSvikkRVLEVLDLVQLKHKA-RQFPDqLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK13539 84 -MKPALTVAENLEFWAAFLGGEEL----DIAAALEAVGLAPLAhLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHNK 197
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-196 |
4.41e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQDFKLLPK 93
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFA-------LEVIGEQPSVIKKRVLEVLDLVQLkhkARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrFDTWTETDRAAVERAMERTGVAQF---ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190
....*....|....*....|....*....|
gi 504478437 167 NLDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
6.53e-20 |
|
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: 84.88 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGvKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKD-----LAAIKEKEIP 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 FV-RRKIGVVFQDFK--LLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQL-KHKARQFPDQLSGGEQQRVSIAR 150
Cdd:TIGR02323 82 RLmRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEE-INNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-216 |
1.24e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRRKIGVVFQDFKLLPKLTVFENV 100
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 101 AFALevIGEQPSVIKKR------VLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSW 174
Cdd:PRK10253 103 ARGR--YPHQPLFTRWRkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 175 EVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK10253 181 DLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-226 |
1.35e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNG-VKALNGVSVAIHPGEFVYVVGPSGAGKS--TFIKM-IYREEKPTKGQILINHKDLAAIKEKEIPFVR-RKIGVVFQ 86
Cdd:PRK09473 25 PDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtAFALMgLLAANGRIGGSATFNGREILNLPEKELNKLRaEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 D--FKLLPKLTVFENVafaLEVIGEQPSVIKKRVLE----VLDLVQL---KHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK09473 105 DpmTSLNPYMRVGEQL---MEVLMLHKGMSKAEAFEesvrMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNR-GTTVVMATHNKEIvntmkkrVIAIEDGIIVRDESRG-EYGS 226
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGV-------VAGICDKVLVMYAGRTmEYGN 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-217 |
3.97e-19 |
|
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: 81.80 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 13 NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-----YreeKPTKGQILINHKDLAAIKEKEIpfVRRKIGVVFQD 87
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkY---EVTEGEILFKGEDITDLPPEER--ARLGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 88 fkllpkltvfenvafALEVIGeqpsvikkrvlevldlVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:cd03217 86 ---------------PPEIPG----------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMK-KRVIAIEDGIIVR 217
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKpDRVHVLYDGRIVK 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-216 |
4.22e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHK-----DLAAIKEKEipfvRRKI-----GV 83
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAE----RRRLlrtewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFK--LLPKLTVFENVAFALEVIGEQP-SVIKKRVLEVLDLVQLKhKAR--QFPDQLSGGEQQRVSIARSIVNNPDV 158
Cdd:PRK11701 94 VHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEID-AARidDLPTTFSGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 159 VIADEPTGNLDPDTS---WEVMKTLeeINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11701 173 VFMDEPTGGLDVSVQarlLDLLRGL--VRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-217 |
4.49e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 9 KAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikEKEIPFVRRK------IG 82
Cdd:PRK11288 12 KTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID--------GQEMRFASTTaalaagVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 VVFQDFKLLPKLTVFENVafaleVIGEQPS---VIKKRVLEVLDLVQLKHKARQF-PDQ----LSGGEQQRVSIARSIVN 154
Cdd:PRK11288 83 IIYQELHLVPEMTVAENL-----YLGQLPHkggIVNRRLLNYEAREQLEHLGVDIdPDTplkyLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVR 217
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-196 |
6.57e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEkPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQDFKLLPKLTVF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAEL---ARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQPSVIkKRVLEVLDLVQLKHK-ARQFpDQLSGGEQQRVSIARSIV-----NNPD--VVIADEPTGNLD 169
Cdd:COG4138 88 QYLALHQPAGASSEAVE-QLLAQLAEALGLEDKlSRPL-TQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
170 180 190
....*....|....*....|....*....|.
gi 504478437 170 pdtsW--EVM--KTLEEINNRGTTVVMATHN 196
Cdd:COG4138 166 ----VaqQAAldRLLRELCQQGITVVMSSHD 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
2.11e-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: 83.34 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM---IYrEEKPTKGQILINHKDLAA--IKEKEip 75
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsgVY-PHGTWDGEIYWSGSPLKAsnIRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 76 fvRRKIGVVFQDFKLLPKLTVFENVAFALEV-----IGEQPSVIkKRVLEVLDLVQLKHKARQFP-DQLSGGEQQRVSIA 149
Cdd:TIGR02633 77 --RAGIVIIHQELTLVPELSVAENIFLGNEItlpggRMAYNAMY-LRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-200 |
3.96e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaaikekeipfvrRKIGVVFQDFKLLPKLT 95
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------------LRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALevigeQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:PRK09544 84 LTVNRFLRL-----RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*.
gi 504478437 176 VMKTLEEINNR-GTTVVMATHNKEIV 200
Cdd:PRK09544 159 LYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-207 |
5.52e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.00 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKP----TKGQILINHKDLAAIKEKEipfvRRK-----IGVVF 85
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE----RRKlvghnVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDfkllPKLTVFENVAFALEVIGEQPSVI------------KKRVLEVLDLVQLK-HKA--RQFPDQLSGGEQQRVSIAR 150
Cdd:PRK15093 96 QE----PQSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrKRRAIELLHRVGIKdHKDamRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEIN-NRGTTVVMATHNKEIVNTMKKRV 207
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKI 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-193 |
3.70e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN--GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkDLAAIKEKEIPFVRR 79
Cdd:PTZ00265 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDfKLLPKLTVFENVAFAL------EVIGEQ---------------PSVIKKRVLEVLDLVQ------LKHKAR 132
Cdd:PTZ00265 461 KIGVVSQD-PLLFSNSIKNNIKYSLyslkdlEALSNYynedgndsqenknkrNSCRAKCAGDLNDMSNttdsneLIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 133 QF------------------------PDQ-----------LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVM 177
Cdd:PTZ00265 540 NYqtikdsevvdvskkvlihdfvsalPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250
....*....|....*...
gi 504478437 178 KTLEEI--NNRGTTVVMA 193
Cdd:PTZ00265 620 KTINNLkgNENRITIIIA 637
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-195 |
7.06e-17 |
|
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: 75.74 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-YREEKPT-KGQILINHKdlaaikEKEIPFvRRKIGVVFQDFKLLPKLT 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGR------PLDKNF-QRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGeqpsvikkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:cd03232 96 VREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
gi 504478437 176 VMKTLEEINNRGTTVVMATH 195
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-217 |
1.13e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 10 AYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-----YreeKPTKGQILINHKDLAAIKEKEIpfVRRKIGVV 84
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkY---EVTSGSILLDGEDILELSPDER--ARAGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 85 FQDFKLLPKLTVFENVAFALEVIGEQPSVI---KKRVLEVLDLVQLKHKA--RQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:COG0396 83 FQYPVEIPGVSVSNFLRTALNARRGEELSArefLKLLKEKMKELGLDEDFldRYVNEGFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMK-KRVIAIEDGIIVR 217
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVK 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-197 |
3.04e-16 |
|
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: 76.90 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQilinhkdlaAIKEKEIpfvrrKIGV 83
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---------ARPQPGI-----KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFKLLPKLTVFENV-------------------AFALE------VIGEQPSVIKKrvLEVLDLVQLKHK------AR 132
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVeegvaeikdaldrfneisaKYAEPdadfdkLAAEQAELQEI--IDAADAWDLDSQleiamdAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 133 QFPD------QLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT-SWevmktLEE--INNRGtTVVMATHNK 197
Cdd:TIGR03719 151 RCPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvAW-----LERhlQEYPG-TVVAVTHDR 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-195 |
3.56e-16 |
|
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: 74.07 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKekeiPFVRRKIGVVFQDFKLLPKLTVF 97
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR----DSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEQpsvikkRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVM 177
Cdd:cd03231 92 ENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*...
gi 504478437 178 KTLEEINNRGTTVVMATH 195
Cdd:cd03231 166 EAMAGHCARGGMVVLTTH 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-195 |
7.65e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.93 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIL-----INHKDLAaikekeipfVRRKIGVVFQDFKLL 91
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIA---------TRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 PKLTVFENVA-----FALEvigeqPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:NF033858 352 GELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|..
gi 504478437 167 NLDP---DTSWEVMKTLEEinNRGTTVVMATH 195
Cdd:NF033858 427 GVDPvarDMFWRLLIELSR--EDGVTIFISTH 456
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
9.41e-16 |
|
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: 75.36 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpnGVKAL-NGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikekeiPFVrrK 80
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------------ETV--K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLL-PKLTVFENVAFALEVIgeqpsVIKKRvlEVldlvqlkhKARQF--------PDQ------LSGGEQQR 145
Cdd:TIGR03719 387 LAYVDQSRDALdPNKTVWEEISGGLDII-----KLGKR--EI--------PSRAYvgrfnfkgSDQqkkvgqLSGGERNR 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTswevMKTLEE--INNRGTTVV----------MATH 195
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEalLNFAGCAVVishdrwfldrIATH 509
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-223 |
1.31e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikeKEIPFVRRKIGVVFQD--FKLLP 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---GDYSYRSQRIRMIFQDpsTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIGE-QPSVIKKRVLEVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDP 170
Cdd:PRK15112 103 RQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 171 DTSWEVMKTLEEINNR-GTTVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGE 223
Cdd:PRK15112 183 SMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-216 |
1.32e-15 |
|
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: 72.30 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 13 NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI---YREEKPTKGQILINHKDLAAIKEKeipFVRRKIGVVFQDFK 89
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---YPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LlPKLTVFENVAFALEVIGEQpsVIKKrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIADEPTGNLD 169
Cdd:cd03233 95 F-PTLTVRETLDFALRCKGNE--FVRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 170 PDTSWEVMKTLEEINN--RGTTVVMATH-NKEIVNTMKKrVIAIEDGIIV 216
Cdd:cd03233 151 SSTALEILKCIRTMADvlKTTTFVSLYQaSDEIYDLFDK-VLVLYEGRQI 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-195 |
1.69e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI-----YRE---EKPTKGQILinhkdlaaikekeipFVRRKigv 83
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGSgriGMPEGEDLL---------------FLPQR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 vfqdfKLLPKLTVFENVAFALEvigeqpsvikkrvlevldlvqlkhkarqfpDQLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:cd03223 73 -----PYLPLGTLREQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 504478437 164 PTGNLDPDTSWEVMKTLEEinnRGTTVVMATH 195
Cdd:cd03223 118 ATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-195 |
1.76e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIyREEKPTKGQILINHKDLAAIKEKEIPFVRrkiGVVFQDFKLLPKLTVFENV 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 101 AFALEViGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSI-----VNNPD--VVIADEPTGNLDPDTS 173
Cdd:PRK03695 91 TLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|..
gi 504478437 174 WEVMKTLEEINNRGTTVVMATH 195
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSH 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-169 |
2.99e-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: 72.44 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEF-----VYVVGPSGAGKSTFIKMIYREEKPTKGQIlinhkdlaaikEKEIPFVRRKIGVVF 85
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------EIELDTVSYKPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 QDFkllpKLTVFENVAFALEVIGEQPSvIKKRVLEVLDLVQLKHkaRQFPDqLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:cd03237 72 ADY----EGTVRDLLSSITKDFYTHPY-FKTEIAKPLQIEQILD--REVPE-LSGGELQRVAIAACLSKDADIYLLDEPS 143
|
....
gi 504478437 166 GNLD 169
Cdd:cd03237 144 AYLD 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-216 |
6.20e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 24 AIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhKDLAAIK-EKEIPfvRRKIGVVFqDFkllpkltVFENVAF 102
Cdd:PRK11147 25 HIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARlQQDPP--RNVEGTVY-DF-------VAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 103 ALEV----------IGEQPS--VIKK--RVLEVLD--------------LVQLKHKARQFPDQLSGGEQQRVSIARSIVN 154
Cdd:PRK11147 94 QAEYlkryhdishlVETDPSekNLNElaKLQEQLDhhnlwqlenrinevLAQLGLDPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 155 NPDVVIADEPTGNLDPDT-SWevmktLEEI--NNRGtTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETiEW-----LEGFlkTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-194 |
9.06e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL------AAIKEKeIPFV---RRKIGvvfq 86
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprDAIRAG-IAYVpedRKGEG---- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 dfkLLPKLTVFENVAFA-LEVIGE----QPSVIKKRVLEVLDLVQLKHKARQFP-DQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:COG1129 341 ---LVLDLSIRENITLAsLDRLSRggllDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190
....*....|....*....|....*....|....
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAT 194
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS 451
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-195 |
1.10e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YP-NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQdfk 89
Cdd:PRK10789 323 YPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW---RSRLAVVSQ--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 lLPKL---TVFENVAFAlevigeQPSVIKKRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIARSIVNN 155
Cdd:PRK10789 397 -TPFLfsdTVANNIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLN 469
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEInNRGTTVVMATH 195
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-213 |
1.58e-14 |
|
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: 69.67 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 8 YKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdLAAIKEKEIPFVRRKIGVVFQD 87
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 88 FK-LLPKLTVFENVAFalevigEQPsVIKKRVLEVLDLVQLKHKARQFP--DQ---------LSGGEQQRVSIARSIVNN 155
Cdd:cd03290 86 QKpWLLNATVEENITF------GSP-FNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKT--LEEINNRGTTVVMATHNKEIVnTMKKRVIAIEDG 213
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-192 |
2.72e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 12 PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL-----AAIKEKEIPFV---RRKIGV 83
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VfqdfkllPKLTVFENvaFALEVIGEQPsvIKKRVLevLDLVQLKHKARQ----F------PDQ----LSGGEQQRVSIA 149
Cdd:COG3845 348 V-------PDMSVAEN--LILGRYRRPP--FSRGGF--LDRKAIRAFAEElieeFdvrtpgPDTparsLSGGNQQKVILA 414
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVM 192
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-195 |
3.01e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 20 GVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKeipfvrrkigvvFQDfKLL-------- 91
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE------------YHQ-DLLylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 -PKLTVFENVAFALEVIGEQPSvikKRVLEVLDLVQLkhkaRQFPD----QLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PRK13538 86 kTELTALENLRFYQRLHGPGDD---EALWEALAQVGL----AGFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 504478437 167 NLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
4.35e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpnGVKAL-NGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINhkdlaaikekeiPFVrrK 80
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG------------ETV--K 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDFKLL-PKLTVFENVAFALEVIgeqpsVIKKRvlEVldlvqlkhKARQF--------PDQ------LSGGEQQR 145
Cdd:PRK11819 389 LAYVDQSRDALdPNKTVWEEISGGLDII-----KVGNR--EI--------PSRAYvgrfnfkgGDQqkkvgvLSGGERNR 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 146 VSIARSIVNNPDVVIADEPTGNLDPDTswevMKTLEE--INNRGTTVV----------MATH 195
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEalLEFPGCAVVishdrwfldrIATH 511
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-213 |
4.73e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQI-----LINHK-----DLAAIKEKEIPFVR-RKIGV 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRsrqviELSEQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQD--FKLLPKLTVFENVAFALE----VIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPD 157
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRlhqgASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 158 VVIADEPTGNLDPDTSWEVM---KTLEEINNRGttVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILqliKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQG 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-224 |
8.16e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 8.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipFVRRKIGVVFQDFK---LLPKL 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLANGIVYISEDRKrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 95 TVFENVAF-ALEVIGEQPSVIKKR--VLEVLDLVQLKHKARQFPDQ----LSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK10762 346 SVKENMSLtALRYFSRAGGSLKHAdeQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMathnkeiVNTMKKRVIAIEDGIIVRDESR--GEY 224
Cdd:PRK10762 426 VDVGAKKEIYQLINQFKAEGLSIIL-------VSSEMPEVLGMSDRILVMHEGRisGEF 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-195 |
1.04e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIyrEEKPTKGQI-----LINHKDLAAikekeiPFVRRkIGVVFQDFKLLP 92
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVItggdrLVNGRPLDS------SFQRS-IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVigEQPSVIKKR-----VLEVLDLVQLkhkaRQFPDQLSG--GE------QQRVSIARSIVNNPDVV 159
Cdd:TIGR00956 850 TSTVRESLRFSAYL--RQPKSVSKSekmeyVEEVIKLLEM----ESYADAVVGvpGEglnveqRKRLTIGVELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*..
gi 504478437 160 I-ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-170 |
1.66e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY---RKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQDFKLLPKLtvfenvafaLEVIGEQPSviKKRVLEVLDLVQLKHKAR----QFPD-QLSGGEQQRVSIARSIVNNP 156
Cdd:PRK10522 400 SAVFTDFHLFDQL---------LGPEGKPAN--PALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEER 468
|
170
....*....|....
gi 504478437 157 DVVIADEPTGNLDP 170
Cdd:PRK10522 469 DILLLDEWAADQDP 482
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-217 |
1.92e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVyKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI--YREEKPTKGQILINHKDlaaIKEKEiPFVR 78
Cdd:CHL00131 7 ILEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGES---ILDLE-PEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGV--VFQ-----------DFKLLP--------KLTVFENVAFaLEVIGEQpsvikkrvlevLDLVQLKHK--ARQFP 135
Cdd:CHL00131 82 AHLGIflAFQypieipgvsnaDFLRLAynskrkfqGLPELDPLEF-LEIINEK-----------LKLVGMDPSflSRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 136 DQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAI-EDGI 214
Cdd:CHL00131 150 EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVmQNGK 229
|
...
gi 504478437 215 IVR 217
Cdd:CHL00131 230 IIK 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-196 |
2.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDL-AAIKEKEIPFVRRK 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 ------IGVVFQDFKLLPKltvFENVAFaLEVIGEQPSVIKKRVLEVLDLVQLKHkaRQFpDQLSGGEQQRVSIARSIVN 154
Cdd:PRK15056 87 eevdwsFPVLVEDVVMMGR---YGHMGW-LRRAKKRDRQIVTAALARVDMVEFRH--RQI-GELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504478437 155 NPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-216 |
4.02e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 20 GVSVAIHPGEFVYVVGPSGAGKS----TFIKMIYREEKPTKGQILINHKDLAAIKekeipfVR-RKIGVVFQD----FKl 90
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA------LRgRKIATIMQNprsaFN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 lPKLTVFENVAFALEVIGEQPSVikKRVLEVLDLVQLKHKAR---QFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK10418 94 -PLHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 168 LDPDTSWEVMKTLEEI-NNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIV 216
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-228 |
5.24e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfVRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDFKLLPKltvfeNVAFALEVIGEQPSVikkRVLEVLDLVQLKHKARQFP-----------DQLSGGEQQRVSI 148
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-----TVRFNIDPFSEHNDA---DLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTmkKRVIAIEDGIIVRDESRGEYGSYD 228
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC--DKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-195 |
5.25e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQilinhkdlaAIKEKEIpfvrrKIGV 83
Cdd:PRK11819 9 MNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE---------ARPAPGI-----KVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFKLLPKLTVFENV-------------------AFAL------EVIGEQPSVIKKrvLEVLDLVQLKHK------AR 132
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVeegvaevkaaldrfneiyaAYAEpdadfdALAAEQGELQEI--IDAADAWDLDSQleiamdAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 133 QFPD------QLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT-SWevmktLEE--INNRGtTVVMATH 195
Cdd:PRK11819 153 RCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvAW-----LEQflHDYPG-TVVAVTH 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-220 |
5.99e-13 |
|
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: 66.42 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVKA-LNGVSVAIHPGEFVYVVGPSGAGKST----FIKMIYreekpTKGQILINHKDLAAIKEKEIpf 76
Cdd:cd03289 3 MTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDGVSWNSVPLQKW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 vRRKIGVVFQdfkllpKLTVFE-NVAFALEVIGEQPSvikKRVLEVLDLVQLKHKARQFPDQL-----------SGGEQQ 144
Cdd:cd03289 76 -RKAFGVIPQ------KVFIFSgTFRKNLDPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 145 RVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEiNNRGTTVVMATHNKEIVNTMkKRVIAIEDGIIVRDES 220
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLEC-QRFLVIEENKVRQYDS 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-169 |
8.55e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 6 EVYKAYPNGVKALNGVSV-----AIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaaIKEKeiPfvrrk 80
Cdd:PRK13409 338 ETLVEYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISYK--P----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 igvvfQDFKLLPKLTVFENVAFALEVIGEqpSVIKKRVLEVLDLVQLKHKARqfpDQLSGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK13409 407 -----QYIKPDYDGTVEDLLRSITDDLGS--SYYKSEIIKPLQLERLLDKNV---KDLSGGELQRVAIAACLSRDADLYL 476
|
....*....
gi 504478437 161 ADEPTGNLD 169
Cdd:PRK13409 477 LDEPSAHLD 485
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-201 |
8.93e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILIN----HKDLAAIkEKEIPFVRRKIGVVfqdfkllPK 93
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqsiKKDLCTY-QKQLCFVGHRSGIN-------PY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVigeqpSVIKKRVLEVLDLVQLKHKArQFP-DQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDT 172
Cdd:PRK13540 89 LTLRENCLYDIHF-----SPGAVGITELCRLFSLEHLI-DYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*....
gi 504478437 173 SWEVMKTLEEINNRGTTVVMATHNKEIVN 201
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQDLPLN 191
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-199 |
1.39e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.41 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEvykaypNGV-----KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIyrEEKPTKGQILINHKdLAAIKEKEIPFV 77
Cdd:PLN03140 882 EMKE------QGVtedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIEGDIR-ISGFPKKQETFA 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 78 RRKiGVVFQDFKLLPKLTVFENVAFAL------EVIGEQPSVIKKRVLEVLDLVQLKHKARQFP--DQLSGGEQQRVSIA 149
Cdd:PLN03140 953 RIS-GYCEQNDIHSPQVTVRESLIYSAflrlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIA 1031
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEI 199
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-213 |
1.67e-12 |
|
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: 66.00 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYRE-EKPTKGQILINHKDLAAIKEKEIpfVRRKIGVVFQDFK---L 90
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQA--IRAGIAMVPEDRKrhgI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 LPKLTVFENVAFA-LEVIGEQPSVIKKRVLEVLD--LVQLKHKARQfPD----QLSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:TIGR02633 351 VPILGVGKNITLSvLKSFCFKMRIDAAAELQIIGsaIQRLKVKTAS-PFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-130 |
1.70e-12 |
|
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: 65.97 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPN----GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI---YReekPTKGQILInhkDLAAIKEKEI 74
Cdd:COG4615 328 LELRGVTYRYPGedgdEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLtglYR---PESGEILL---DGQPVTADNR 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 75 PFVRRKIGVVFQDFKLlpkltvFEnvafalEVIGEQPSVIKKRVLEVLDLVQLKHK 130
Cdd:COG4615 402 EAYRQLFSAVFSDFHL------FD------RLLGLDGEADPARARELLERLELDHK 445
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-198 |
2.56e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 65.70 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNG---------VK-------ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKpTKGQILINHK 64
Cdd:TIGR01271 1202 VIENPHAQKCWPSGgqmdvqgltAKyteagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGV 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 65 DLAAIKEKEIpfvRRKIGVVFQdfkllpKLTVFENVaFALEVIG-EQPSviKKRVLEVLDLVQLKHKARQFPDQL----- 138
Cdd:TIGR01271 1281 SWNSVTLQTW---RKAFGVIPQ------KVFIFSGT-FRKNLDPyEQWS--DEEIWKVAEEVGLKSVIEQFPDKLdfvlv 1348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 139 ------SGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEiNNRGTTVVMATHNKE 198
Cdd:TIGR01271 1349 dggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVE 1413
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-218 |
2.74e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKM---IYreekPT---KGQILINHKDLA--AIKEK 72
Cdd:NF040905 1 ILEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVlsgVY----PHgsyEGEILFDGEVCRfkDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 73 EipfvRRKIGVVFQDFKLLPKLTVFENVaFalevIGEQPS---VI-----KKRVLEVLDLVQLKHKARQFPDQLSGGEQQ 144
Cdd:NF040905 76 E----ALGIVIIHQELALIPYLSIAENI-F----LGNERAkrgVIdwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 145 RVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHN-KEI---------------VNTMKKRVI 208
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIrrvadsitvlrdgrtIETLDCRAD 226
|
250
....*....|
gi 504478437 209 AIEDGIIVRD 218
Cdd:NF040905 227 EVTEDRIIRG 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-221 |
2.90e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLA------AIKeKEIPFV---RRKIGvvfq 86
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVK-KGMAYItesRRDNG---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 87 dfkLLPKLTVFENVAFA--LEVIGEQ-------PSVIKKRVLEVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:PRK09700 352 ---FFPNFSIAQNMAISrsLKDGGYKgamglfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMathnkeiVNTMKKRVIAIEDGIIVRDESR 221
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM-------VSSELPEIITVCDRIAVFCEGR 486
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-182 |
3.62e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAY-PNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRK 80
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL---RKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 IGVVFQDfkllPKLtvFE-NVAFALEVIGEQPSVikkRVLEVLDLVQLKHKARQFP-----------DQLSGGEQQRVSI 148
Cdd:PLN03130 1315 LGIIPQA----PVL--FSgTVRFNLDPFNEHNDA---DLWESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSL 1385
|
170 180 190
....*....|....*....|....*....|....
gi 504478437 149 ARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEE 182
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-193 |
4.94e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMI----YREEKPTKGQILINHKDLAAIKekeiPFVRRKIGVVFQDFKLLPK 93
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIK----KHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENVAFALEVIGEQpsvikKRVLEVLDLVQLKHKA------------------RQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQ-----NRPDGVSREEYAKHIAdvymatyglshtrntkvgNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINN-RGTTVVMA 193
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVA 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-198 |
7.85e-12 |
|
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: 64.26 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYP-NGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAikekEIPFVRR 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDFKLLPKLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVV 159
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190
....*....|....*....|....*....|....*....
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKE 198
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-195 |
8.89e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYPNGVKALNGVSV-----AIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIlinHKDLA-AIKEKEIPf 76
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKiSYKPQYIS- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 77 vrrkigvvfQDFkllpKLTVFENVAfalevigeqpSVIKKRV------LEVLDLVQLKHKARQFPDQLSGGEQQRVSIAR 150
Cdd:COG1245 412 ---------PDY----DGTVEEFLR----------SANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504478437 151 SIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEI-NNRGTTVVMATH 195
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDH 514
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-227 |
9.85e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIlinhkdlaaiKEKEipfvRRKI 81
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSE----NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 82 GVVFQD----FKllPKLTVFENVA-FALEVIGEQpSV--IKKRVLEVLDlvQLKHKARQfpdqLSGGEQQRVSIARSIVN 154
Cdd:PRK15064 385 GYYAQDhaydFE--NDLTLFDWMSqWRQEGDDEQ-AVrgTLGRLLFSQD--DIKKSVKV----LSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 155 NPDVVIADEPTGNLDpdtswevMKTLEEINN-----RGtTVVMATHNKEIVNTMKKRVIAI-EDGIIvrdESRGEYGSY 227
Cdd:PRK15064 456 KPNVLVMDEPTNHMD-------MESIESLNMalekyEG-TLIFVSHDREFVSSLATRIIEItPDGVV---DFSGTYEEY 523
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-227 |
1.23e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILinhkdlaaiKEKEIPFVRRKIGVVfqdfkllpKLTVF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYVPQQAWIM--------NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEvigEQPSvikkRVLEVLDLVQLKHKARQFPD-----------QLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PTZ00243 739 GNILFFDE---EDAA----RLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504478437 167 NLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVnTMKKRVIAIEDGiivRDESRGEYGSY 227
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDG---RVEFSGSSADF 868
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-215 |
1.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEkeIPFVRRKigvvfqdfkllpklTVF 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQ--VSWIFNA--------------TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVIGEqpsvikkRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PLN03232 697 ENILFGSDFESE-------RYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504478437 167 NLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKrVIAIEDGII 215
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR-IILVSEGMI 817
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-171 |
2.23e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 25 IHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILIN-HKDLAAIKEKEIPFVRRKIGvvfqdfkLLPKLTVFENVAFA 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFMAYLGHLPG-------LKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 104 LEVIGEQPsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:PRK13543 107 CGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-202 |
2.47e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 3 EMKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaaikeKEIPFvrrkig 82
Cdd:PRK11147 321 EMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------LEVAY------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 83 vvFQDFK--LLPKLTVFENVAfalevIGEQPSVIKKRVLEVLDLVQ--LKH--KARQFPDQLSGGEQQRVSIARSIVNNP 156
Cdd:PRK11147 387 --FDQHRaeLDPEKTVMDNLA-----EGKQEVMVNGRPRHVLGYLQdfLFHpkRAMTPVKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 157 DVVIADEPTGNLDPDTswevMKTLEE-INNRGTTVVMATHNKEIV-NT 202
Cdd:PRK11147 460 NLLILDEPTNDLDVET----LELLEElLDSYQGTVLLVSHDRQFVdNT 503
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-196 |
3.35e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.23 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 27 PGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQI--------LINH-------KDLAAIKEKEIPFVRRKigvvfQDFKLL 91
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEfrgselqNYFTKLLEGDVKVIVKP-----QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 92 PKlTVFENVAFALEVIGEqpsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:cd03236 100 PK-AVKGKVGELLKKKDE-----RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*
gi 504478437 172 TSWEVMKTLEEINNRGTTVVMATHN 196
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-226 |
3.73e-11 |
|
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: 62.27 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQDFKLLP----- 92
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFSgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVF-----ENVAFALEVigeqpSVIKKRVLEVLDlvQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:TIGR00957 1379 NLDPFsqysdEEVWWALEL-----AHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMkkRVIAIEDGIIvrdesrGEYGS 226
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT--RVIVLDKGEV------AEFGA 1502
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-228 |
7.05e-11 |
|
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: 60.31 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYPNGVK-ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAaikekEIPF--VR 78
Cdd:cd03288 20 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-----KLPLhtLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKltvfeNVAFALEvigEQPSVIKKRVLEVLDLVQLKHKARQFP-----------DQLSGGEQQRVS 147
Cdd:cd03288 95 SRLSIILQDPILFSG-----SIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 148 IARSIVNNPDVVIADEPTGNLDpdtswevMKTlEEINNRgttVVMATHNKEIVNTMKKRVIAIEDGIIVRDESRGEYGSY 227
Cdd:cd03288 167 LARAFVRKSSILIMDEATASID-------MAT-ENILQK---VVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVEC 235
|
.
gi 504478437 228 D 228
Cdd:cd03288 236 D 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-228 |
7.26e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkdlaaikekeipfVRRKIGVVFQdFKLLPKLTVF 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IRGTVAYVPQ-VSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVigeQPSvikkRVLEVLDLVQLKHKARQFP--DQ---------LSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:PLN03130 697 DNILFGSPF---DPE----RYERAIDVTALQHDLDLLPggDLteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 167 NLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMkKRVIAIEDGIIvrdesrGEYGSYD 228
Cdd:PLN03130 770 ALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMI------KEEGTYE 824
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
1.66e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 4 MKEVYKAYPnGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRKIGV 83
Cdd:PRK10982 1 MSNISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 VFQDFKLLPKLTVFENVAfalevIGEQPS----VIKKRVLE----VLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNN 155
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMW-----LGRYPTkgmfVDQDKMYRdtkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 156 PDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-179 |
2.50e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIliNHKDlaaikekeipfvrrKIGVVFQDFKLLPK 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSG--------------RISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 lTVFENVAFALevigeqpSVIKKRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:cd03291 113 -TIKENIIFGV-------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
170
....*....|....*..
gi 504478437 163 EPTGNLDPDTSWEVMKT 179
Cdd:cd03291 185 SPFGYLDVFTEKEIFES 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
3.36e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEipfvRRKIGVVF-----QDFKLLPKLT 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAfALeVIGEQPSVIK----KRVLE----VLDlVQLKHkARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK15439 358 LAWNVC-AL-THNRRGFWIKpareNAVLEryrrALN-IKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-179 |
3.46e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQIliNHKDlaaikekeipfvrrKIGVVFQDFKLLPK 93
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSG--------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 lTVFENVAFALevigeqpSVIKKRVLEVLDLVQLKHKARQFPDQ-----------LSGGEQQRVSIARSIVNNPDVVIAD 162
Cdd:TIGR01271 502 -TIKDNIIFGL-------SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLD 573
|
170
....*....|....*..
gi 504478437 163 EPTGNLDPDTSWEVMKT 179
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFES 590
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-218 |
6.20e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfvRRKIGVVFQDfkllPKL--- 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQD----PVLfdg 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 95 TVFENV-AF----------ALEVIGEQPSV------IKKRVLEvldlvqlkhkarqFPDQLSGGEQQRVSIARSIVN-NP 156
Cdd:PTZ00243 1399 TVRQNVdPFleassaevwaALELVGLRERVasesegIDSRVLE-------------GGSNYSVGQRQLMCMARALLKkGS 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 157 DVVIADEPTGNLDPDTSWEVMKTleeinnrgttvVMATHNKEIVNTMKKRV--IAIEDGIIVRD 218
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQAT-----------VMSAFSAYTVITIAHRLhtVAQYDKIIVMD 1518
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-213 |
9.94e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKdlaaikekeipfvrrkIGVVFQDFKLLPKLTV 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 97 FENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEV 176
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 504478437 177 MKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-218 |
2.41e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 115 KKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMAT 194
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT 201
|
90 100
....*....|....*....|....
gi 504478437 195 HNKEIVNTMKKRVIAIEDGIIVRD 218
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-195 |
3.51e-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: 55.95 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 27 PGEFVYVVGPSGAGKSTFIKMIYREEKPT-----------------KGQILINHkdLAAIKEKEIPfVRRKIgvvfQDFK 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELQDY--FKKLANGEIK-VAHKP----QYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKltVFE-NVAFALEVIGEqpsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:COG1245 171 LIPK--VFKgTVRELLEKVDE-----RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*..
gi 504478437 169 DPDTSWEVMKTLEEINNRGTTVVMATH 195
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-221 |
4.41e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 21 VSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRKIGVVFQDFK---LLPKLTVF 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA--IRAGIMLCPEDRKaegIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAfalevIGEQPSVIKKRVLevLDLVQLKHKARQF----------PDQ----LSGGEQQRVSIARSIVNNPDVVIADE 163
Cdd:PRK11288 350 DNIN-----ISARRHHLRAGCL--INNRWEAENADRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 164 PTGNLDPDTSWEVMKTLEEINNRGTTVVMathnkeiVNTMKKRVIAIEDGIIVRDESR 221
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLF-------VSSDLPEVLGVADRIVVMREGR 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-194 |
4.93e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 15 VKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIpfVRRKIGVVFQDF--KLLP 92
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA--VCPRIAYMPQGLgkNLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 93 KLTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLkhkaRQFPD----QLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGV 167
|
170 180 190
....*....|....*....|....*....|
gi 504478437 169 DPdTS----WEVMKTLEEiNNRGTTVVMAT 194
Cdd:NF033858 168 DP-LSrrqfWELIDRIRA-ERPGMSVLVAT 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-215 |
1.05e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIY-----REEkptkGQILINHKDLAAIKEKEIpfVRRKIGVVFQDF 88
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgRWE----GEIFIDGKPVKIRNPQQA--IAQGIAMVPEDR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 89 K---LLPKLTVFENVAFALEVIGEQPSVIKKrVLEVLDLVQ----LKHKARQfPDQ----LSGGEQQRVSIARSIVNNPD 157
Cdd:PRK13549 348 KrdgIVPVMGVGKNITLAALDRFTGGSRIDD-AAELKTILEsiqrLKVKTAS-PELaiarLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 158 VVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDGII 215
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-195 |
1.39e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 16 KALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIKEKEIPFVRRKIGVvfqdfKLlpKLT 95
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGL-----KL--EMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGEqpsvikkrvLEVLDLVQLKHKARQFPDQ----LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPD 171
Cdd:PRK13541 87 VFENLKFWSEIYNS---------AETLYAAIHYFKLHDLLDEkcysLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180
....*....|....*....|....*....
gi 504478437 172 T-----SWEVMKTleeinNRGTTVVMATH 195
Cdd:PRK13541 158 NrdllnNLIVMKA-----NSGGIVLLSSH 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-202 |
2.33e-08 |
|
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: 51.94 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 6 EVYKAYpngVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIyreekptkgqilinhkdLAAIKEKEIPfvrrkigvvf 85
Cdd:cd03238 2 TVSGAN---VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLI---------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 qdfKLLPK----LTVFenvafalevIGEQPSVIKKRvlevLDLVQLKHKArqfpDQLSGGEQQRVSIARSIVNNPD--VV 159
Cdd:cd03238 52 ---SFLPKfsrnKLIF---------IDQLQFLIDVG----LGYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLF 111
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504478437 160 IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNT 202
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-216 |
2.36e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 57 GQILINHKDLAAIKEKEIpfvRRKIGVVFQDfKLLPKLTVFENVAFALEvigeqpSVIKKRVLEVLDLVQLKHKARQFPD 136
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDL---RNLFSIVSQE-PMLFNMSIYENIKFGKE------DATREDVKRACKFAAIDEFIESLPN 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 137 Q-----------LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGttvvmathNKEIVnTMKK 205
Cdd:PTZ00265 1347 KydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA--------DKTII-TIAH 1417
|
170
....*....|...
gi 504478437 206 RVIAIE--DGIIV 216
Cdd:PTZ00265 1418 RIASIKrsDKIVV 1430
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-169 |
6.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 27 PGEFVYVVGPSGAGKSTFIKMIYREEKPT-----------------KGQILINHkdLAAIKEKEIPFVRrKIgvvfQDFK 89
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQNY--FKKLYNGEIKVVH-KP----QYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKltVFE-NVAFALEVIGEqpsviKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:PRK13409 171 LIPK--VFKgKVRELLKKVDE-----RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 504478437 169 D 169
Cdd:PRK13409 244 D 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-204 |
6.70e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIY-REE-KPTKGQILINHKDLAAIKEKEipfvrRKIGVVFQDFKLLPKLT 95
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREDyEVTGGTVEFKGKDLLELSPED-----RAGEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGeqpSVIKKRVLEVL------DLVQLKHKARQFPDQL---------SGGEQQRVSIARSIVNNPDVVI 160
Cdd:PRK09580 92 GVSNQFFLQTALN---AVRSYRGQEPLdrfdfqDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504478437 161 ADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNTMK 204
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIK 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-169 |
7.62e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkdlaaikEKEIPFVRRKigvvfqdfKLLPKLTVF 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM---------KGSVAYVPQQ--------AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 98 ENVAFALEVigeQPSVIKKRV--------LEVL---DLVQLKHKARQfpdqLSGGEQQRVSIARSIVNNPDVVIADEPTG 166
Cdd:TIGR00957 717 ENILFGKAL---NEKYYQQVLeacallpdLEILpsgDRTEIGEKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
...
gi 504478437 167 NLD 169
Cdd:TIGR00957 790 AVD 792
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-213 |
1.12e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 17 ALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILIN-HKDLAAIKEkeipfvrrkigvvfqdfKLLPKLT 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKgSAALIAISS-----------------GLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 96 VFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWE 175
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 504478437 176 VMKTLEEINNRGTTVVMATHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
1.19e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 27 PGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILInhkdlaaikekeipfvrrkigvvfqdfkllpkltvfenvaFALEV 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------------------IDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 107 IgeqpsvikkrvLEVLDLVQLKHKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLE----- 181
Cdd:smart00382 41 I-----------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|...
gi 504478437 182 -EINNRGTTVVMATHNKEIVNTM 203
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-211 |
2.45e-07 |
|
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: 49.11 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEF-----VYVVGPSGAGKSTFIKMIYREEKPTKGQIlinhkdlaaikekEIPFVRrkigvvf 85
Cdd:cd03222 3 YPDCVKRYGVFFLLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGIT------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 86 qdfkllpkltvfenvafalevIGEQPSVIKkrvlevldlvqlkhkarqfpdqLSGGEQQRVSIARSIVNNPDVVIADEPT 165
Cdd:cd03222 63 ---------------------PVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504478437 166 GNLDPDTSWEVMKTLEEINNRGT-TVVMATHNKEIVNTMKKRVIAIE 211
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-171 |
3.14e-07 |
|
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: 50.52 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKmIYREEKPTKGQILINHKDLAAIKEKEIPFVRRK 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 81 igvVFQDFKLLPKlTVFEnvaFALEVIGEQpsvikkRVLEVLDLVQLKH---------KARQFPDQLSGGEQQRVSIARS 151
Cdd:TIGR00954 530 ---TLRDQIIYPD-SSED---MKRRGLSDK------DLEQILDNVQLTHilereggwsAVQDWMDVLSGGEKQRIAMARL 596
|
170 180
....*....|....*....|
gi 504478437 152 IVNNPDVVIADEPTGNLDPD 171
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVD 616
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-213 |
4.14e-07 |
|
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: 48.76 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 33 VVGPSGAGKSTFI---KMIYREEKPTKGQILINHKDLAAIKEkeipfVRRKIGVVFQ-----DFKLLPKLTVFENVAFAL 104
Cdd:cd03240 27 IVGQNGAGKTTIIealKYALTGELPPNSKGGAHDPKLIREGE-----VRAQVKLAFEnangkKYTITRSLAILENVIFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 105 EviGEqpsvIKKRVLEVldlvqlkhkarqfPDQLSGGEQQ------RVSIARSIVNNPDVVIADEPTGNLDPDTSW---- 174
Cdd:cd03240 102 Q--GE----SNWPLLDM-------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEesla 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504478437 175 EVMKTLEEINNRGTTVVmaTHNKEIVNTMKK--RVIAIEDG 213
Cdd:cd03240 163 EIIEERKSQKNFQLIVI--THDEELVDAADHiyRVEKDGRQ 201
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
6-200 |
5.57e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 6 EVYKAYPNGVKalnGVSVAIHPGEFVYVVGPSGAGKSTF-IKMIYRE--------------------EKPTKGQIlinhK 64
Cdd:cd03270 2 IVRGAREHNLK---NVDVDIPRNKLVVITGVSGSGKSSLaFDTIYAEgqrryveslsayarqflgqmDKPDVDSI----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 65 DLA---AIKEKEI-PFVRRKIGVVFQDFKLLPKLtvfenvaFALEVIGEQPSVIKKRVLEVLDLvqlkhkARQFPdQLSG 140
Cdd:cd03270 75 GLSpaiAIDQKTTsRNPRSTVGTVTEIYDYLRLL-------FARVGIRERLGFLVDVGLGYLTL------SRSAP-TLSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 141 GEQQRVSIARSIVNNPDVV--IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIV 200
Cdd:cd03270 141 GEAQRIRLATQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
1.49e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 2 IEMKEVYKAYpNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIyREEKPtkgQILINHKDLAAIKE---KEIPFVR 78
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHP---QGYSNDLTLFGRRRgsgETIWDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 79 RKIGVVFQDFKLLPKL-TVFENVAFA--LEVIGEQPSV---IKKRVLEVLDLVQLKHKARQFPDQ-LSGGEQQRVSIARS 151
Cdd:PRK10938 336 KHIGYVSSSLHLDYRVsTSVRNVILSgfFDSIGIYQAVsdrQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRA 415
|
170
....*....|....*....
gi 504478437 152 IVNNPDVVIADEPTGNLDP 170
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-202 |
1.73e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFI-----KMIYREEKPTKGQILiNHKDLAAIK--EKEIPFVRRKIGV------- 83
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQPG-NHDRIEGLEhiDKVIVIDQSPIGRtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 84 ----VFQDFKLL---------------------------PKLTVFEnvafALEVIGEQPSVikKRVLEVLDLVQLKH-KA 131
Cdd:cd03271 90 tytgVFDEIRELfcevckgkrynretlevrykgksiadvLDMTVEE----ALEFFENIPKI--ARKLQTLCDVGLGYiKL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 132 RQFPDQLSGGEQQRVSIARSIVN---NPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNT 202
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
145-202 |
2.88e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.88e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 145 RVSIARSIVNNPDVVIADEPTGNLDPDT-SWevmktLEEI-NNRGTTVVMATHNKEIVNT 202
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTiRW-----LEDVlNERNSTMIIISHDRHFLNS 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-171 |
5.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 11 YPNGVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQILINHKDLAAIkekeipFVRRKI-GVVFQDFK 89
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAV------FSQHHVdGLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 90 LLPKLTVFenvafalevigeqPSVIKKRVLEVLDLVQLK-HKARQFPDQLSGGEQQRVSIARSIVNNPDVVIADEPTGNL 168
Cdd:PLN03073 592 LLYMMRCF-------------PGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
...
gi 504478437 169 DPD 171
Cdd:PLN03073 659 DLD 661
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-213 |
5.77e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 1 MIEMKEVYKAYPNGVkALNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQI-LINHKDLAAIKEKEIPFVRR 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 80 KIGVVFQDFKLLPKLTvfenvafalevigEQpsvikkrvlevldlvQLK----------HKARQFPDQLSGGEQQRVSIA 149
Cdd:PRK10636 391 DESPLQHLARLAPQEL-------------EQ---------------KLRdylggfgfqgDKVTEETRRFSGGEKARLVLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504478437 150 RSIVNNPDVVIADEPTGNLDPDTSWEVMKTLeeINNRGTTVVMaTHNKEIVNTMKKRVIAIEDG 213
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVV-SHDRHLLRSTTDDLYLVHDG 503
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-228 |
6.21e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 18 LNGVSVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQI-LINHKDLAAIKEKEIPFVRRKIGVVF---QDFKLLPK 93
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVNQETPALPQPALEYVIdgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFENV-----AFA-----LEVIgeQPSVIKKRVLEVLDLV-----QLKHKARQFpdqlSGGEQQRVSIARSIVNNPDV 158
Cdd:PRK10636 97 QLHDANErndghAIAtihgkLDAI--DAWTIRSRAASLLHGLgfsneQLERPVSDF----SGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 159 VIADEPTGNLDPDTS-WevmktLEE-INNRGTTVVMATHNKEIVNTMKKRVIAIEDGIIVrdESRGEYGSYD 228
Cdd:PRK10636 171 LLLDEPTNHLDLDAViW-----LEKwLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLF--EYTGNYSSFE 235
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-201 |
1.17e-05 |
|
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: 43.89 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 22 SVAIHPGEFVYVVGPSGAGKSTFIKmiyreekptkgQILInhkdlaaikekeipfvrrkigVVFQDFKLLPKLTVF---E 98
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILD-----------AIGL---------------------ALGGAQSATRRRSGVkagC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 99 NVAfalevigeqpsvikkrvLEVLDLVQLKHkarqfpdQLSGGEQQRVSIA-----RSIVNNPDVVIaDEPTGNLDPDTS 173
Cdd:cd03227 63 IVA-----------------AVSAELIFTRL-------QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDG 117
|
170 180
....*....|....*....|....*...
gi 504478437 174 WEVMKTLEEINNRGTTVVMATHNKEIVN 201
Cdd:cd03227 118 QALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-192 |
4.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 22 SVAIHPGEFVYVVGPSGAGKSTFIKMIYREEKPTKGQ--------ILINHKDLAAIKEKEipFVRRK---IGVVFQDFKL 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDE--WQRNNtdmLSPGEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 91 lpkltvfenvaFALEVIGEQpsvIKK--RVLEVLDLVQLKHK-ARQFpDQLSGGEQQRVSIARSIVNNPDVVIADEPTGN 167
Cdd:PRK10938 101 -----------TTAEIIQDE---VKDpaRCEQLAQQFGITALlDRRF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180
....*....|....*....|....*
gi 504478437 168 LDPDTSWEVMKTLEEINNRGTTVVM 192
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-213 |
5.11e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 136 DQLSGGEQQRVSIARSIVNNPDVV--IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVnTMKKRVIAIEDG 213
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPG 553
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
94-202 |
5.78e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 94 LTVFEnvafALEVIGEQPSVIKKrvLEVLDLVQLKH-KARQFPDQLSGGEQQRVSIARSI---VNNPDVVIADEPTGNLD 169
Cdd:TIGR00630 791 MTVEE----AYEFFEAVPSISRK--LQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH 864
|
90 100 110
....*....|....*....|....*....|...
gi 504478437 170 PDTSWEVMKTLEEINNRGTTVVMATHNKEIVNT 202
Cdd:TIGR00630 865 FDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT 897
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-203 |
5.96e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 14 GVKALNGVSVAIHPGEFVYVVGPSGAGKSTFIK---MIYREEKPTKGQIL-----INHKDLAAIK-------------EK 72
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymaMHAIDGIPKNCQILhveqeVVGDDTTALQcvlntdiertqllEE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 73 EIPFVRRKIGVVFQDFKLLPKLTvfENVAFALEVIGEQPSVIKKRvLEVLDLVQLKHKA--------------RQFPDQL 138
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGKGA--NKDGVDKDAVSQRLEEIYKR-LELIDAYTAEARAasilaglsftpemqVKATKTF 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 139 SGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTsweVMKTLEEINNRGTTVVMATHNKEIVNTM 203
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-192 |
1.21e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 138 LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVM 192
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-192 |
2.59e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 504478437 138 LSGGEQQRVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVM 192
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-202 |
3.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504478437 138 LSGGEQQRVSIARSIVN---NPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVNT 202
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKV 877
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
31-88 |
3.78e-04 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 40.05 E-value: 3.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504478437 31 VYVVGPSGAGKSTFIKMIYR---EEKPTKGQIlINHKD-----LAAIKEKEIPFVRRKIGVVFQDF 88
Cdd:cd19516 14 VYVAGATGSGKSTLLAAIYRyilENDPPDRKI-ITYEDpiefvYDGIKSKHSIIVQSQIPRHFKSF 78
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
61-201 |
4.23e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 61 INHKDLAAIKEKEIPFVRRKIGVVFQDFKLLPK------LTVFENVAFALEVIGEQPSVIKKRVLEVLDLVQLKHKARQF 134
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKELLQrlvrglKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELP 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 135 PDQLSGGEQQ---RVSIARSIVNNPDVVIADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKEIVN 201
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
26-45 |
1.33e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 1.33e-03
|
| phosphon_PhnN |
TIGR02322 |
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this ... |
28-81 |
2.34e-03 |
|
phosphonate metabolism protein/1,5-bisphosphokinase (PRPP-forming) PhnN; Members of this family resemble PhnN of phosphonate utilization operons, where different such operons confer the ability to use somewhat different profiles of C-P bond-containing compounds (see ), including phosphites as well as phosphonates. PhnN in E. coli shows considerable homology to guanylate kinases (EC 2.7.4.8), and has actually been shown to act as a ribose 1,5-bisphosphokinase (PRPP forming). This suggests an analogous kinase reaction for phosphonate metabolism, converting 5-phosphoalpha-1-(methylphosphono)ribose to methylphosphono-PRPP. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 274078 Cd Length: 179 Bit Score: 37.73 E-value: 2.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504478437 28 GEFVYVVGPSGAGKSTfikmiyreekptkgqiLINHKDLAAIKEKEIPFVRRKI 81
Cdd:TIGR02322 1 GRLIYVVGPSGAGKDT----------------LLDYARARLAGDPRVHFVRRVI 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-45 |
2.71e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.71e-03
10 20
....*....|....*....|....*..
gi 504478437 19 NGVSVAIHPGEFVYVVGPSGAGKSTFI 45
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
53-198 |
4.43e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504478437 53 KPTKGQILINHKDLAAIKEKEIpfvrRKIGVVFQDFKLLPkltvfENVAFALEVIGEqpsvIKKRV---LEV-LDLVQLK 128
Cdd:TIGR00630 417 KPEALAVTVGGKSIADVSELSI----REAHEFFNQLTLTP-----EEKKIAEEVLKE----IRERLgflIDVgLDYLSLS 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504478437 129 HKArqfpDQLSGGEQQRVSIARSIVNNPDVV--IADEPTGNLDPDTSWEVMKTLEEINNRGTTVVMATHNKE 198
Cdd:TIGR00630 484 RAA----GTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED 551
|
|
| |
