|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
1.40e-131 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 369.38 E-value: 1.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
1.41e-100 |
|
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: 290.30 E-value: 1.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
7.81e-94 |
|
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: 273.51 E-value: 7.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-223 |
2.70e-89 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 262.12 E-value: 2.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGdGEAGQ 223
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
1.08e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 253.04 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG---LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:COG1136 4 LLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQ-IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMrHRMLTLQRGRLIGD 218
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELAARA-DRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.48e-80 |
|
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: 239.70 E-value: 1.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVG---LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQ-IPFL 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLaLIARMRHRMLTLQRGRL 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-220 |
2.96e-77 |
|
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: 232.09 E-value: 2.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHEL---SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINReLGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
1.51e-76 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 233.82 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG---HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:COG1135 1 MIELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
4.33e-74 |
|
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: 223.75 E-value: 4.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIPFLRRQI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQN--HQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:COG1122 78 GLVFQNpdDQL-FAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
1.27e-70 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 218.90 E-value: 1.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG---HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:PRK11153 1 MIELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINReLGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-219 |
6.99e-67 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 205.98 E-value: 6.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPL-QILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDeLGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
9.36e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 205.68 E-value: 9.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNI---ALP----LQ-ILGL-SKAEIAkRVDSALERVSLSDKgELFPAD-LSTGQQQRVGIAR 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGrtstWRsLLGLfPPEDRE-RALEALERVGLADK-AYQRADqLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.86e-65 |
|
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: 210.53 E-value: 1.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG----LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPF 76
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQN--HQLLFDRTVFNNIALPLQILG-LSKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAI 152
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
1.24e-62 |
|
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: 194.22 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQN--HQLLFDrTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03225 78 GLVFQNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
5.40e-61 |
|
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: 190.97 E-value: 5.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPL--------QILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKeDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
1.42e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 189.82 E-value: 1.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGqISNAQIPFLRRQ 80
Cdd:COG1126 1 MIEIENLHKSFGDLEV-LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIAL-PLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
5.06e-60 |
|
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: 188.03 E-value: 5.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG----HVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIS-NAQIP 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTI-LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDeDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLRRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEiaKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMrHRMLTLQRGRLIGDGEA 221
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAA 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
6.37e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.85 E-value: 6.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisNAQIPFlRRQ 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 161 ADEPTGNLDPRL----AAEIMGVFEdinRLGTTVLIASHDL--ALiaRMRHRMLTLQRGRLI 216
Cdd:COG3842 159 LDEPLSALDAKLreemREELRRLQR---ELGITFIYVTHDQeeAL--ALADRIAVMNDGRIE 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
2.23e-58 |
|
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: 183.49 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQI 81
Cdd:cd03259 1 LELKGLSKTYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
2.97e-58 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 184.52 E-value: 2.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYP---NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgqisnaQIPFL 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK--------PVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDL 197
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDV 199
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
3.34e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.73 E-value: 3.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQI 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-219 |
1.65e-57 |
|
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: 182.00 E-value: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPL--------QILGL-SKAEIAKRVdSALERVSLSDKGELFPADLSTGQQQRVGIARAI 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLfPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-219 |
2.51e-57 |
|
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: 181.55 E-value: 2.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQI 81
Cdd:cd03261 1 IELRGLTKSFGGRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPL-QILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-215 |
2.57e-56 |
|
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: 178.58 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKeLGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-220 |
5.06e-55 |
|
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: 176.87 E-value: 5.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY----PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQN--HQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQQRVGIARAIVH 154
Cdd:TIGR04521 81 RKKVGLVFQFpeHQL-FEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-219 |
9.17e-55 |
|
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: 174.62 E-value: 9.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG---HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFD--RTVFNNIALPLQILGL--SKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQQRVGIARAI 152
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-215 |
1.03e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 178.34 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQ 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 161 ADEPTGNLDPRLA----AEIMGVFEdinRLGTTVLIASHDL--ALiaRMRHRMLTLQRGRL 215
Cdd:COG3839 157 LDEPLSNLDAKLRvemrAEIKRLHR---RLGTTTIYVTHDQveAM--TLADRIAVMNDGRI 212
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-215 |
1.61e-54 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 173.75 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG---LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFL 77
Cdd:NF038007 1 MLNMQNAEKCYITKTIKtkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQ-IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQP 156
Cdd:NF038007 81 RRElIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASH-DLAliARMRHRMLTLQRGRL 215
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHsDEA--STYGNRIINMKDGKL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-218 |
1.67e-54 |
|
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: 173.81 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG---HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqipflr 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTL--QRGRLIGD 218
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
2.16e-54 |
|
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: 173.10 E-value: 2.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQiSNAQIPFLRRQI 81
Cdd:cd03262 1 IEIKNLHKSFGDFHV-LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIAL-PLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-222 |
2.44e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 174.22 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG---LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfL 77
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFD--RTVFNNIALPLQILGLskAEIAKRVDSALERVSLSDkgEL---FPADLSTGQQQRVGIARAI 152
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPP--SFldrYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAG 222
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
3.74e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 172.97 E-value: 3.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDK--GELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 159 LLADEPTGNLDP----RLAAEIMgvfeDINR-LGTTVLIASHDL--ALiaRMRHRMLTLQRGRLI 216
Cdd:COG1125 158 LLMDEPFGALDPitreQLQDELL----RLQReLGKTIVFVTHDIdeAL--KLGDRIAVMREGRIV 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
3.88e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.96 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQ--DLGQ-ISNAQIPFLR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFDRTVFNN-IALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
7.35e-53 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.19 E-value: 7.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQ--DLGQISNA-QIPFLR 78
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFDRTVFNN-IALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
4.00e-52 |
|
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: 166.21 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPFLRRQI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-TDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPlqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-210 |
6.12e-52 |
|
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: 166.64 E-value: 6.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQI-PFLRRQIGV 83
Cdd:TIGR03608 2 KNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAsKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 84 VFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 164 PTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLAlIARMRHRMLTL 210
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPE-VAKQADRVIEL 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-215 |
6.34e-52 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 167.69 E-value: 6.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 6 QVAKRYPNGHVG---LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLR-RQI 81
Cdd:PRK11629 10 NLCKRYQEGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLALIARMrHRMLTLQRGRL 215
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
1.35e-51 |
|
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: 167.14 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV-LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIAL---PLQ--ILGLSKAEIAKrVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
4.26e-51 |
|
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: 165.05 E-value: 4.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLL-----LAMERPTSGKLLLAGQDLGQISNAQIPf 76
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQnHQLLFDRTVFNNIALPLQILG-LSKAEIAKRVDSALERVSLSD--KGELFPADLSTGQQQRVGIARAIV 153
Cdd:cd03260 79 LRRRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
1.03e-50 |
|
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: 164.78 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKG--ELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
6.44e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.52 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqIPFLRRQI 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLlFDRTVFNNIALPLQILGLSKAEiaKRVDSALERVSLS----DKGelfPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG4619 77 AYVPQEPAL-WGGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPpdilDKP---VERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFED-INRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
6.89e-50 |
|
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: 169.70 E-value: 6.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHV-GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPT---SGKLLLAGQDLGQISNAQipf 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQNHQLLFDR-TVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
4.23e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.64 E-value: 4.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQiSNAQIPFLRRQ 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIAL-PLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-216 |
7.11e-49 |
|
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: 160.89 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 16 VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ-IGVVFQNHQLLFDR 94
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499850989 175 EIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:cd03294 198 EMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-219 |
2.12e-47 |
|
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: 156.06 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPflRRQIGVV 84
Cdd:cd03219 4 RGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQNHQLLFDRTVFNNIALPLQILGLS----------KAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVH 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
2.57e-47 |
|
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: 155.11 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQI 81
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQqRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
2.60e-47 |
|
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: 156.17 E-value: 2.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQ 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
1.42e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 151.77 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQlLFDRTVFNNIalplqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03228 78 IAYVPQDPF-LFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDInRLGTTVLIASHDLALIARMrHRMLTLQRGR 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-219 |
3.74e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 162.31 E-value: 3.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYP-NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:COG2274 474 IELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLlFDRTVFNNIALplqilGLSKAEIAkRVDSALERVSLSDKGELFP-----------ADLSTGQQQRVGIA 149
Cdd:COG2274 551 IGVVLQDVFL-FSGTIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDG 691
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
4.21e-46 |
|
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: 153.74 E-value: 4.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHV-GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqISNAQIPFLRRQ 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQN--HQLLfDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:TIGR04520 79 VGMVFQNpdNQFV-GATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDL--ALIArmrHRMLTLQRGRLIGDG 219
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMeeAVLA---DRVIVMNKGKIVAEG 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-220 |
1.66e-45 |
|
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: 153.80 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEI 114
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 115 AKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIA 193
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqLGITFVFV 157
|
170 180
....*....|....*....|....*..
gi 499850989 194 SHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
2.69e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.76 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisNAQIPFLRRQI 81
Cdd:COG1118 3 IEVRNISKRFGSFTL-LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
1.45e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaqipfLRRQ 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQllFDR----TVFNNIALPLQ----ILGLSKAEIAKRVDSALERVSLSDK-----GELfpadlSTGQQQRVG 147
Cdd:COG1121 77 IGYVPQRAE--VDWdfpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLadrpiGEL-----SGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 148 IARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-223 |
3.57e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.59 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVglhELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflrRQ 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQI-LGLSKAEIAkRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV-HQPAL 158
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRPgLKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 159 LLaDEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG3840 152 LL-DEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-220 |
4.54e-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: 147.48 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNaqIPFLRRQIGVVFQNHQLLFDRTVF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKD---ITN--LPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM 177
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499850989 178 GVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:cd03299 170 EELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
4.96e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 148.69 E-value: 4.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 10 RYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPFLRRQIGVVFQN-H 88
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 QLLFDRTVFNNIAL-PLQiLGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGN 167
Cdd:PRK13639 89 DQLFAPTVEEDVAFgPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 168 LDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
7.09e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 144.33 E-value: 7.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqIPFLRRQIGVVFQNHQLLFDRTVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 98 NNIALPLQILGLSKAEIAKRVDSALERVSLSDKGE----LFPADLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-219 |
3.91e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 148.94 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQI 81
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDL--ALIarMRHRMLTLQRGRLIGDG 219
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRkLGITFVFVTHDQeeALT--MSDRIVVMRDGRIEQDG 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
6.06e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 151.83 E-value: 6.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQlLFDRTVFNNIAlplqiLGLSKAEIAkRVDSALERVSLSDKGELFPADLST-----------GQQQRVGIAR 150
Cdd:COG4988 414 AWVPQNPY-LFAGTIRENLR-----LGRPDASDE-ELEAALEAAGLDEFVAALPDGLDTplgeggrglsgGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQA-DRILVLDDGRIVEQG 553
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 |
7.95e-43 |
|
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: 142.95 E-value: 7.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 11 YPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQiSNAQIPFLRRQIGVVFQN-HQ 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-SRKGLLERRQRVGLVFQDpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 90 LLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD 169
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 499850989 170 PRLAAEIMGVFEDINRLGTTVLIASHDLALI 200
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-202 |
8.66e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.94 E-value: 8.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISN--------- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEV-LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 72 -AQIPFLRRQIGVVFQNHQLLFDRTVFNN-IALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIA 149
Cdd:COG4598 87 rRQLQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALiAR 202
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGF-AR 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
1.02e-42 |
|
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: 141.77 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaQIPFLRRQI 81
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIalplqilglskaeiakrvdsalervslsdkgelfpaDLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-220 |
1.65e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 144.81 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 16 VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQiSNAQIPFLRRQIGVVFQ--NHQLlFD 93
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQypEYQL-FE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNNIALPLQILGLSKAEIAKRVDSALERVSLS-----DKGelfPADLSTGQQQRVGIARAIVHQPALLLADEPTGNL 168
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyedykDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 169 DPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13637 176 DPKGRDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-216 |
2.58e-42 |
|
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: 145.20 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERP---TSGKLLLAGQDLGQISNAQIPFLR-RQIGVVFQNHQLLFD--R 94
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQMIFQDPMTSLNpvM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQI-LGLSKAEIAKRVDSALERVSLSDKGEL---FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP 170
Cdd:COG0444 104 TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 171 RLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:COG0444 184 TIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-221 |
2.64e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 145.64 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQNHQLLFD--RTVFNN 99
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPYASLNprMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 IALPLQILGL-SKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM 177
Cdd:COG4608 118 IAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 178 GVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRL--IGDGEA 221
Cdd:COG4608 198 NLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIveIAPRDE 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-219 |
4.14e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQlLFDRTVFNNIAlplqiLGLSKAEIAkRVDSALERVSLSDKGELFP-----------ADLSTGQQQRVGIAR 150
Cdd:COG1132 417 GVVPQDTF-LFSGTIRENIR-----YGRPDATDE-EVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
8.35e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.85 E-value: 8.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpflRRQ 80
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV---RRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK13635 83 VGMVFQNPDNQFvGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEG 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.21e-41 |
|
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: 141.32 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQI 81
Cdd:cd03296 3 IEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-----TDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQI----LGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-219 |
2.77e-41 |
|
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: 139.59 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIsnaqipflRRQIG 82
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNHQLLFDR--TVFNNIALPLQ-----ILGLSKAEIAKrVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:cd03235 72 YVPQRRSIDRDFpiSVRDVVLMGLYghkglFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRgRLIGDG 219
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
3.49e-41 |
|
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: 137.38 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIG 82
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQnhqllfdrtvfnnialplqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499850989 163 EPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-222 |
1.03e-40 |
|
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: 140.60 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 9 KRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqISNAQIpfLRRQIGVVFQNH 88
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRK--VRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 QLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNL 168
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 169 DPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAG 222
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-196 |
1.53e-40 |
|
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: 141.71 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAqiPFLRRQIGVV 84
Cdd:TIGR03265 8 DNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRD---ITRL--PPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190
....*....|....*....|....*....|...
gi 499850989 165 TGNLDPRLAAEIMGVFEDINR-LGTTVLIASHD 196
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRrLGVTTIMVTHD 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
3.18e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 135.64 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIGVV 84
Cdd:cd03214 3 ENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQnhqllfdrtvfnnialplqilglskaeiakrvdsALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 165 TGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
8.40e-40 |
|
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: 135.68 E-value: 8.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaQIPFLRRQ 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIakRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRH 205
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARV 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
1.83e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.03 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLL------AGQDLGQiSNAQI 74
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQ-QKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 75 PFLRRQIGVVFQNHQLLFDRTVFNN-IALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-219 |
2.12e-39 |
|
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: 142.21 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVG-LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:COG4987 334 LELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLlFDRTVFNNIAL--PlqilGLSKAEIAKrvdsALERVSLSDKGELFPADLST-----------GQQQRVG 147
Cdd:COG4987 411 IAVVPQRPHL-FDTTLRENLRLarP----DATDEELWA----ALERVGLGDWLAALPDGLDTwlgeggrrlsgGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 148 IARAIVHQPALLLADEPTGNLDPRLAAEIMgvfEDINRL--GTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALL---ADLLEAlaGRTVLLITHRLAGLERM-DRILVLEDGRIVEQG 551
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
2.87e-39 |
|
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: 135.55 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPflRRQ 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA--RLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQ----------ILGLSK-----AEIAKRVDSALERVSLSDKGELFPADLSTGQQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 146 VGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-220 |
3.32e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 138.81 E-value: 3.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 13 NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPFLRRQIGVVFQNHQLLF 92
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRL 172
Cdd:PRK11607 105 HMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 173 AAEI-MGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK11607 185 RDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-216 |
4.03e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 136.11 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG----HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL-GQISNAQIPF 76
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQ-NHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQQRVGIARAIVH 154
Cdd:PRK13641 83 LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-219 |
5.23e-39 |
|
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: 134.54 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRRQ 80
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHqLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVS---------LSDKGelfpADLSTGQQQRVGIARA 151
Cdd:cd03252 78 VGVVLQEN-VLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISelpegydtiVGEQG----AGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIaRMRHRMLTLQRGRLIGDG 219
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-214 |
5.61e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 137.67 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflrRQ 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 161 ADEPTGNLDPRLAA----EIMGVFEdinRLGTTVLIASHD------LAliarmrHRMLTLQRGR 214
Cdd:PRK11650 158 FDEPLSNLDAKLRVqmrlEIQRLHR---RLKTTSLYVTHDqveamtLA------DRVVVMNGGV 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-220 |
8.46e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 135.11 E-value: 8.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaQIPFLRRQ 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK13644 79 VGIVFQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIaRMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-219 |
1.49e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.94 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 9 KRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL-------GQISNA---QIPFLR 78
Cdd:PRK10619 13 KRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLKVAdknQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFDRTVFNNI-ALPLQILGLSKAEIAKRVDSALERVSLSDKGEL-FPADLSTGQQQRVGIARAIVHQP 156
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.81e-38 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 132.49 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.75e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.94 E-value: 4.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRRQI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQN-HQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK13647 82 GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-216 |
1.94e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 131.35 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRYPNGHVG--------LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLR 78
Cdd:PRK10419 9 LSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFD--RTVFNNIALPLQ-ILGLSKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQQRVGIARAIVH 154
Cdd:PRK10419 89 RDIQMVFQDSISAVNprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-223 |
2.15e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 136.35 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 9 KRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMErPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQnh 88
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 qllfD--------RTVFNNIALPLQIL--GLSKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG4172 370 ----DpfgslsprMTVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-219 |
2.33e-37 |
|
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: 129.26 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipflRRQI 81
Cdd:cd03268 1 LKTNDLTKTYGKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----LRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKaeiaKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
3.72e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.30 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY----PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL-GQISNAQIPF 76
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQ--NHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDkgELF---PADLSTGQQQRVGIARA 151
Cdd:PRK13634 83 LRKKVGIVFQfpEHQL-FEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPE--ELLarsPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLG--TTVLIaSHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLV-THSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-216 |
3.78e-37 |
|
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: 133.05 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 14 GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRR-QIGVVFQNHQLLF 92
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRL 172
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499850989 173 AAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:TIGR01186 165 RDSMQDELKKLQAtLQKTIVFITHDLDEAIRIGDRIVIMKAGEIV 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-218 |
5.47e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 136.39 E-value: 5.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRYPNGH---VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ-IG 82
Cdd:PRK10535 10 IRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 163 EPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDlALIARMRHRMLTLQRGRLIGD 218
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
18-223 |
9.55e-37 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 128.56 E-value: 9.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpflrRQIGVVFQNHQLLFDRTVF 97
Cdd:TIGR03864 17 LDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAAL----ARLGVVFQQPTLDLDLSVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM 177
Cdd:TIGR03864 93 QNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAIT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 178 G-VFEDINRLGTTVLIASHdlaLIARMRH--RMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR03864 173 AhVRALARDQGLSVLWATH---LVDEIEAsdRLVVLHRGRVLADGAAAE 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-219 |
1.20e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.85 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRY----PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIS-NAQIP 75
Cdd:PRK13643 1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLRRQIGVVFQ-NHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
1.36e-36 |
|
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: 127.40 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGqisnaqiPFLRRQI 81
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-219 |
1.83e-36 |
|
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: 127.73 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNhQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKG---ELFPA--DLSTGQQQRVGIARAIVHQP 156
Cdd:cd03254 80 GVVLQD-TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGydtVLGENggNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIaRMRHRMLTLQRGRLIGDG 219
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-223 |
1.91e-36 |
|
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: 127.55 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 11 YPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpfLRRQIGVVFQNHQL 90
Cdd:cd03224 10 YGKSQI-LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 91 LFDRTVFNNIALPLQILGlsKAEIAKRVDSALErvslsdkgeLFPA----------DLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03224 87 FPELTVEENLLLGAYARR--RAKRKARLERVYE---------LFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
2.16e-36 |
|
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: 126.60 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQipfLRRQIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKE---RRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQN--HQLLFDrTVFNNIALPLQILGLSKAEIAKrvdsALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRG 213
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-169 |
2.31e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 128.44 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG---HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnaQIPFL 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV------TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRqiGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170
....*....|..
gi 499850989 158 LLLADEPTGNLD 169
Cdd:COG4525 155 FLLMDEPFGALD 166
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
2.87e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.81 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPFLRRQ 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQ--NHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:PRK13636 84 VGMVFQdpDNQL-FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 159 LLADEPTGNLDPRLAAEIMG-VFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-215 |
4.54e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.93 E-value: 4.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpflRRQIGVVFQNHQLLF-DRTV 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI---RHKIGMVFQNPDNQFvGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499850989 177 MGVFEDI-NRLGTTVLIASHDLALIArMRHRMLTLQRGRL 215
Cdd:PRK13650 180 IKTIKGIrDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
5.45e-36 |
|
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: 132.41 E-value: 5.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRRQI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQnHQLLFDRTVFNNIALPLqiLGLSKAEIAKrvdsALERVSLSDKGELFP-----------ADLSTGQQQRVGIAR 150
Cdd:TIGR02857 399 AWVPQ-HPFLFAGTIAENIRLAR--PDASDAEIRE----ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMRH 205
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADR 525
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-219 |
9.83e-36 |
|
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: 125.49 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQI--PFLRRQIGVVFQNHQLLFDRTVFNNIALPLQ 105
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-FDSRKKInlPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 106 ilGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDI-N 184
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIkK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 499850989 185 RLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-196 |
1.13e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.68 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflrRQIGVVFQ 86
Cdd:PRK11432 12 ITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 87 NHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTG 166
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190
....*....|....*....|....*....|.
gi 499850989 167 NLDPRLAAEIMGVFEDIN-RLGTTVLIASHD 196
Cdd:PRK11432 166 NLDANLRRSMREKIRELQqQFNITSLYVTHD 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-223 |
3.92e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 126.62 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQN--HQLLFDRTVFNN 99
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 IALPLQI-LGLSKAEIAKRVDSALERVSLsdKGEL---FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAE 175
Cdd:PRK11308 115 LEEPLLInTSLSAAERREKALAMMAKVGL--RPEHydrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 176 IMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK11308 193 VLNLMMDLQQeLGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-222 |
3.94e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 125.18 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLlAGqdlgqisNAQIPFLRRQIGVV 84
Cdd:PRK11247 16 NAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AG-------TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQNHQLLFDRTVFNNIALPLqilglsKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 165 TGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLtlqrgrLIGDGEAG 222
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVL------LIEEGKIG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-223 |
1.61e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 123.30 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNHQLLFDRTVF 97
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE---LARRRAVLPQHSSLAFPFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV-------HQPALLLADEPTGNLDP 170
Cdd:COG4559 94 EVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 171 RLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4559 174 AHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
1.79e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.76 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRRQIGVVFQN-HQLLFDRTV 96
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKFVGLVFQNpDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499850989 177 MGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13652 177 IDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-220 |
3.06e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.00 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPngHVGLHeLSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqisNAQIPFLRRQ 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQI-LGLSKAEIAKRVDSAlERVSLSDKGELFPADLSTGQQQRVGIARAIV-HQPAL 158
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLNPgLKLNAAQREKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVrEQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 159 LLaDEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK10771 152 LL-DEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-176 |
3.55e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 124.81 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflrRQI 81
Cdd:PRK10851 3 IEIANIKKSFGRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILG----LSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVLPrrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170
....*....|....*....
gi 499850989 158 LLLADEPTGNLDPRLAAEI 176
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKEL 175
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-216 |
4.30e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 13 NGHVGLHELSFRARRGEflfVT---GHSGAGKSTLLRLLLAM--ERP---TSGKLLLAGQDlgqISNAQIP--FLRRQIG 82
Cdd:COG1117 22 GDKQALKDINLDIPENK---VTaliGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGED---IYDPDVDvvELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQ--NhqlLFDRTVFNNIALPLQILGL-SKAEIAKRVDSALERVSLSD--KGELF-PA-DLSTGQQQRVGIARAIVHQ 155
Cdd:COG1117 96 MVFQkpN---PFPKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevKDRLKkSAlGLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 156 PALLLADEPTGNLDPRLAAEImgvfED-INRLGT--TVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:COG1117 173 PEVLLMDEPTSALDPISTAKI----EElILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
4.49e-34 |
|
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: 122.12 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGK-LLLAGQDLGQISnaqIPFLRR 79
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED---VWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLLFDRTV----------FNNIALPLQIlglsKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIA 149
Cdd:COG1119 79 RIGLVSPALQLRFPRDEtvldvvlsgfFDSIGLYREP----TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLI-ASHDLA-LIARMRHRMLtLQRGRLIGDGE 220
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHVEeIPPGITHVLL-LKDGRVVAAGP 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-219 |
1.23e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 121.73 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNG-----HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNaqIP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLRRQIGVVFQN--HQLLfDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK13633 82 DIRNKAGMVFQNpdNQIV-ATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASH--DLALIArmrHRMLTLQRGRLIGDG 219
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHymEEAVEA---DRIIVMDSGKVVMEG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
1.29e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.03 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSD-KGELFPAdLSTGQQQRVGIARAIV------ 153
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYPQ-LSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-201 |
1.73e-33 |
|
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: 120.03 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIPFLRRQI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNhQLLFDRTVFNNIAlpLQILGLSKAEI---AKRVDSALERVSLSDK-----GE--LFpadLSTGQQQRVGIARA 151
Cdd:cd03253 78 GVVPQD-TVLFNDTIGYNIR--YGRPDATDEEVieaAKAAQIHDKIMRFPDGydtivGErgLK---LSGGEKQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIAsHDLALIA 201
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIV 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-223 |
1.95e-33 |
|
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: 125.57 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKS----TLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLR-RQIGVVFQN----- 87
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQEpmtsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 88 ---HqllfdrTVFNNIALPLQI-LGLSKAEIAKRVDSALERVSLSDKGEL---FPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG4172 106 nplH------TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
2.06e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 120.09 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpfLRRQ 80
Cdd:COG0410 3 MLEVENLHAGYGGIHV-LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALPLQILGlSKAEIAKRVDSALErvslsdkgeLFP----------ADLSTGQQQRVGIAR 150
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYE---------LFPrlkerrrqraGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
2.07e-33 |
|
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: 118.09 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQlLFDRTVFNNIalplqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03246 78 VGYLPQDDE-LFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMrHRMLTLQRGRL 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
3.47e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGH-VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:PRK13632 84 KIGIIFQNPDNQFiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIA-SHDL--ALIArmrHRMLTLQRGRLIGDGE 220
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMdeAILA---DKVIVFSEGKLIAQGK 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-220 |
3.97e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 120.62 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG----HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIS-NAQIPF 76
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQ-NHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDkgELF---PADLSTGQQQRVGIARAI 152
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISE--SLFeknPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 153 VHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-219 |
5.15e-33 |
|
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: 118.36 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpnGHVGLHeLSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIsnaqiPFLRRQI 81
Cdd:cd03298 1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-----PPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-223 |
6.90e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 119.73 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPFLRRQIGVVFQN-HQLLFDRTVFNNIALPLQILGLSK 111
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDpEQQIFYTDIDSDIAFSLRNLGVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 112 AEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVL 191
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVI 190
|
170 180 190
....*....|....*....|....*....|..
gi 499850989 192 IASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK13638 191 ISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
8.24e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 117.85 E-value: 8.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRY--PNGHV-GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPF- 76
Cdd:cd03266 1 MITADALTKRFrdVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-----VKEPAe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQNHQLlFDR-TVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:cd03266 76 ARRRLGFVSDSTGL-YDRlTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-215 |
1.05e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 121.29 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflrRQIGVVFQNHQLLFDRTVFNNIALPLQIL 107
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGVGMVFQSYALYPHLSVAENMSFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 108 GLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRL----AAEIMGVFEdi 183
Cdd:PRK11000 104 GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALrvqmRIEISRLHK-- 181
|
170 180 190
....*....|....*....|....*....|..
gi 499850989 184 nRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:PRK11000 182 -RLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
1.43e-32 |
|
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: 117.54 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG------LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQ----DLGQIS 70
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 71 NAQIPFLRRQ-IGVVFQnhqllFDRTV-----FNNIALPLQILGLSKAEIAKRVDSALERVSLSDK-GELFPADLSTGQQ 143
Cdd:COG4778 84 PREILALRRRtIGYVSQ-----FLRVIprvsaLDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 144 QRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-219 |
2.83e-32 |
|
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: 116.53 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDrTVFNNIAlplqiLGLSKAEIAkRVDSALERVSLSDKGELFP-----------ADLSTGQQQRVGIA 149
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNIT-----LGAPLADDE-RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEimgVFEDINRL--GTTVLIASHDLALIArMRHRMLTLQRGRLIGDG 219
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEER---LKERLRQLlgDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
3.15e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 118.75 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNgHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaQIPFLRRQI 81
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-223 |
3.31e-32 |
|
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: 117.01 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMER-----PTSGKLLLAGQDLGQiSNAQIPF 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEA-LKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYD-KKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQnHQLLFDRTVFNNIALPLQILGL-SKAEIAKRVDSALERVSL----SDKGELFPADLSTGQQQRVGIARA 151
Cdd:TIGR00972 80 LRRRVGMVFQ-KPNPFPMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDInRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQ 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
3.59e-32 |
|
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: 116.14 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVtGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQI 81
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 162 DEPTGNLDPrlaAEIMGVFEDINRLGT--TVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03264 155 DEPTAGLDP---EERIRFRNLLSELGEdrIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-217 |
4.44e-32 |
|
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: 116.41 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnaQIPFLRRQigVVFQNHQLLFDRTVF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI------TEPGPDRM--VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQIL--GLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP----R 171
Cdd:TIGR01184 73 ENIALAVDRVlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499850989 172 LAAEIMGVFEDinrLGTTVLIASHDL--ALIARMRHRMLTLQRGRLIG 217
Cdd:TIGR01184 153 LQEELMQIWEE---HRVTVLMVTHDVdeALLLSDRVVMLTNGPAANIG 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-215 |
4.79e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.42 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 26 RRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLR-RQIGVVFQNHQLLFDRTVFNNIALPL 104
Cdd:PRK10584 34 KRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 105 QILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDIN 184
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
|
170 180 190
....*....|....*....|....*....|..
gi 499850989 185 R-LGTTVLIASHDLALIARMRHRmLTLQRGRL 215
Cdd:PRK10584 194 ReHGTTLILVTHDLQLAARCDRR-LRLVNGQL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
4.97e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.90 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGE-FLFVtGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPF--- 76
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEiFGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 ---LRRQIGVVfqnHQLLFdrtvfnnIAlplQILGLSKAEIAKRVDSALERVSLSD----KGElfpaDLSTGQQQRVGIA 149
Cdd:COG4152 79 ergLYPKMKVG---EQLVY-------LA---RLKGLSKAEAKRRADEWLERLGLGDrankKVE----ELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 150 RAIVHQPALLLADEPTGNLDPrLAAEIM-GVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDP-VNVELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
1.11e-31 |
|
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: 121.08 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNhQLLFDRTVFNNIAL--PlqilGLSKAEIAKRVDSA-LER--VSLSDK-----GE--LfpaDLSTGQQQRVGIA 149
Cdd:COG5265 435 GIVPQD-TVLFNDTIAYNIAYgrP----DASEEEVEAAARAAqIHDfiESLPDGydtrvGErgL---KLSGGEKQRVAIA 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVDA-DEILVLEAGRIV 571
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-223 |
2.09e-31 |
|
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: 117.51 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEFLF----------VT---GHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIpFL---RRQIGV 83
Cdd:COG4148 4 EVDFRLRRGGFTLdvdftlpgrgVTalfGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGI-FLpphRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 84 VFQNHQLLFDRTVFNNIALplqilGLSKAEIAKRVDSALERVSLSDKGEL---FPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLY-----GRKRAPRAERRISFDEVVELLGIGHLldrRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-200 |
3.56e-31 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 114.17 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPN--GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIPFLRR 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERV-SLSDKGELFPAD----LSTGQQQRVGIARAIVH 154
Cdd:cd03249 78 QIGLVSQEPVL-FDGTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLVGErgsqLSGGQKQRIAIARALLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDInRLGTTVLIASHDLALI 200
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTI 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
8.22e-31 |
|
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: 112.60 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisNAQIPFLRRQ 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQnHQLLFDR-TVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03263 77 LGYCPQ-FDALFDElTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDInRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-220 |
8.68e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.80 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNA---------------------QIPF 76
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQ--NHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKG-ELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK13651 103 IRRRVGVVFQfaEYQL-FEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-219 |
1.87e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLRLL-----LAMERPTSGKLLLAGQDlgqISNAQIPFLRRQIGVVFQNHQLLFDRTVFNNIALPLQI- 106
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQD---IFKMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLKLn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 107 -LGLSKAEIAKRVDSALERVSLSD--KGEL-FPA-DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFE 181
Cdd:PRK14247 111 rLVKSKKELQERVRWALEKAQLWDevKDRLdAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFL 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 499850989 182 DINRLGTTVLIaSHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK14247 191 ELKKDMTIVLV-THFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-219 |
1.98e-30 |
|
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: 112.43 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 16 VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQIGVVF-QNHQLLFDR 94
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK----FLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILGLSKAEIAKRVDsalERVSLSDKGELF--PA-DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPR 171
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLD---ELSELLDLEELLdtPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 172 LAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-219 |
2.01e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.90 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 16 VGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQ-IGVVFQNHQLLFDR 94
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 175 EIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK10070 202 EMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-219 |
1.36e-29 |
|
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: 110.01 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPN-GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIPFLRRQ 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTVFNNIALPLqiLGLSKAEI--AKRVDSALERVSLSDKG-ELFPAD----LSTGQQQRVGIARAIV 153
Cdd:cd03251 78 IGLVSQD-VFLFNDTVAENIAYGR--PGATREEVeeAARAANAHEFIMELPEGyDTVIGErgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMgvfEDINRL--GTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQ---AALERLmkNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-214 |
2.23e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 111.72 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQN--HQLLFDRTVFNN 99
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 IALPLQIL--GLSKAEIAKRVDSALERVSL-SDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:PRK15079 121 IAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190
....*....|....*....|....*....|....*....
gi 499850989 177 MGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:PRK15079 201 VNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-221 |
5.83e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.26 E-value: 5.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 9 KRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKST----LLRLLlamerPTSGKLLLAGQDLGQISNAQIPFLRRQIGVV 84
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQ--NHQLLFDRTVFNNIALPLQI--LGLSKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK15134 368 FQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-219 |
6.77e-29 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 108.75 E-value: 6.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNHQLLFDRTVFNNIALP----LQILG 108
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRA---RARRVALVEQDSDTAVPLTVRDVVALGriphRSLWA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 109 LSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGT 188
Cdd:TIGR03873 109 GDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGV 188
|
170 180 190
....*....|....*....|....*....|.
gi 499850989 189 TVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:TIGR03873 189 TVVAALHDLNLAASYCDHVVVLDGGRVVAAG 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
3.55e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.76 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLagqdLGQISNAQIPFLRRQI 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-169 |
4.37e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.71 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnaQIPFLRRq 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 iGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*....
gi 499850989 161 ADEPTGNLD 169
Cdd:PRK11248 152 LDEPFGALD 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-219 |
4.74e-28 |
|
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: 105.69 E-value: 4.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVG---------------------LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLL 60
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwaLKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 61 LAGQDLGQISnaqipflrrqIGVVFQNHQllfdrTVFNNIALPLQILGLSKAEIAKRVDsalERVSLSDKGELFpaDL-- 138
Cdd:cd03220 81 VRGRVSSLLG----------LGGGFNPEL-----TGRENIYLNGRLLGLSRKEIDEKID---EIIEFSELGDFI--DLpv 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 139 ---STGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03220 141 ktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
....
gi 499850989 216 IGDG 219
Cdd:cd03220 221 RFDG 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-223 |
8.42e-28 |
|
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: 107.89 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEF---------------LFvtGHSGAGKSTLLRLLLAMERPTSGKLLLAG---QDLGQisNAQIPFLRRQI 81
Cdd:TIGR02142 2 SARFSKRLGDFsldadftlpgqgvtaIF--GRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRK--GIFLPPEKRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIalplqILGLSKAEIAKRV---DSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:TIGR02142 78 GYVFQEARLFPHLSVRGNL-----RYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-216 |
1.02e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 105.69 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQipFLRRQIGVVFQNHQllfdrTVF 97
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK--YRCKHIRMIFQDPN-----TSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 N---NIAlplQIL--------GLSKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:COG4167 101 NprlNIG---QILeeplrlntDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499850989 166 GNLDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:COG4167 178 AALDMSVRSQIINLMLELQeKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-219 |
1.24e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRRQIGVVFQNHQLLF-DRTV 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQNPDNQFvGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499850989 177 MGVFEDI-NRLGTTVLIASHDLALIARmRHRMLTLQRGRLIGDG 219
Cdd:PRK13642 180 MRVIHEIkEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-223 |
1.26e-27 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 104.55 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 23 FRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaqipfLRRQIGVVFQNHQLLFD------RTV 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK--------GWRHIGYVPQRHEFAWDfpisvaHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 177 MGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQrGRLIGDGEAGQ 223
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQ 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
2.78e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.19 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPfLRRQ 80
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDA-IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQnHQLLFDR-TVFNNIAL---PLQILGLSKAEIAKRVDSALERVSLsdkgELFP----ADLSTGQQQRVGIARAI 152
Cdd:COG3845 82 IGMVHQ-HFMLVPNlTVAENIVLglePTKGGRLDRKAARARIRELSERYGL----DVDPdakvEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 153 VHQPALLLADEPTGNLDPrlaAEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG3845 157 YRGARILILDEPTAVLTP---QEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-216 |
3.45e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.40 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQNHQLLFD--RTVFN 98
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDprQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 99 NIALPLQILGLSKAEIA-KRVDSALERVSLSDKGEL-FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEI 176
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAAaARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499850989 177 MGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK10261 503 INLLLDLQRdFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-220 |
6.39e-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: 102.86 E-value: 6.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgqisnaqiPFLRR---QI 81
Cdd:TIGR03740 4 KNLSKRFGKQTA-VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH----------PWTRKdlhKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIakrvDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
6.75e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRR 79
Cdd:PRK13648 7 IIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:PRK13648 84 HIGIVFQNPDNQFvGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIA-SHDLALIARMRHrMLTLQRGRLIGDG 219
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAMEADH-VIVMNKGTVYKEG 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-223 |
6.83e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.53 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVG-LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLlFDRTVFNNIAlplqilGLSKAEIAKRVDSAlERVSLSDKGELFP-----------ADLSTGQQQRVGIA 149
Cdd:COG4618 408 IGYLPQDVEL-FDGTIAENIA------RFGDADPEKVVAAA-KLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMrHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDE 552
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-223 |
9.35e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.60 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpfLRRQIGVVFQNHQLLFDRTVF 97
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQILGLSKAEIAKRVdsalervslsdkGELFPA----------DLSTGQQQRVGIARAIVHQPALLLADEPTGN 167
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEI------------YELFPVlkemlgrrggDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 168 LDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-223 |
1.30e-26 |
|
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: 102.24 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIpFLRRQI 81
Cdd:cd03218 1 LRAENLSKRYGKRKV-VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD---ITKLPM-HKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVF--QNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03218 76 GIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
1.41e-26 |
|
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: 101.78 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPN--GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPAD-----LSTGQQQRVGIARAIVH 154
Cdd:cd03248 89 KVSLVGQEPVL-FARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGekgsqLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRL 215
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-219 |
1.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHV-GLHELSFRARRGEFLFVTGHSGAGKSTLLRL----LLAMERPTSgKLLLAGQDLGQISNAQIpf 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLinglLLPDDNPNS-KITVDGITLTAKTVWDI-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 lRRQIGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:PRK13640 83 -REKVGIVFQNPDNQFvGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALiARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQG 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-222 |
2.17e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNhQLLFDRTVFNNIALPLQilGLSKAEIAKrvdsALERVSLSD----KGELFPAD-------LSTGQQQRVGIAR 150
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNIRVGRP--DATDEEMRA----AAERAQAHDfierKPDGYDTVvgergrqLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIAsHDLALIaRMRHRMLTLQRGRLIgdgEAG 222
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA-HRLSTV-RNADRILVFDNGRVV---ESG 551
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
2.55e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVG---------------------LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKL 59
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 60 LLAgqdlGQISnaqiPFLrrQIGVVFQNhqllfDRTVFNNIALPLQILGLSKAEIAKRVDSALErvsLSDKGELFpaDL- 138
Cdd:COG1134 84 EVN----GRVS----ALL--ELGAGFHP-----ELTGRENIYLNGRLLGLSRKEIDEKFDEIVE---FAELGDFI--DQp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 139 ----STGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:COG1134 144 vktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*..
gi 499850989 215 LIGDGEA 221
Cdd:COG1134 224 LVMDGDP 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
2.83e-26 |
|
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: 105.65 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAME--RPTSGKLL----------------LAG 63
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 64 Q--------------DLGQISNAQIPFLRRQIGVVFQNHQLLF-DRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLS 128
Cdd:TIGR03269 80 EpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRTFALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 129 DKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM-GVFEDINRLGTTVLIASHDLALIARMRHRM 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|...
gi 499850989 208 LTLQRGRLIGDGE 220
Cdd:TIGR03269 240 IWLENGEIKEEGT 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-223 |
2.95e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPN--GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQnHQLLFDRTVFNNIALPL------QILGLSKAEIAKRVDSALERVSLSDKGELfPADLSTGQQQRVGIARAIV 153
Cdd:TIGR00958 556 QVALVGQ-EPVLFSGSVRENIAYGLtdtpdeEIMAAAKAANAHDFIMEFPNGYDTEVGEK-GSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 154 HQPALLLADEPTGNLDPRLAAeimGVFEDINRLGTTVLIASHDLALIARMrHRMLTLQRGRLIGDGEAGQ 223
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMGTHKQ 699
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
7.91e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.86 E-value: 7.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLR----LLLAMERPTSGKLLLAG--QDLGQISNaQI 74
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRtvQREGRLAR-DI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 75 PFLRRQIGVVFQNHQLLFDRTVFNNIAL------PLQILGLS--KAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRV 146
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 147 GIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
9.10e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISN---AQipfl 77
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSprdAQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RRQIGVVFQNHQLLFDRTVFNNIALPLQILG---LSKAEIAKRVDSALERVSLsdkgELFP----ADLSTGQQQRVGIAR 150
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGL----DIDPdtpvGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 151 AIVHQPALLLADEPTGNLDPRlaaEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG1129 154 ALSRDARVLILDEPTASLTER---EVERLFRIIRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-221 |
1.64e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.92 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLR-----LLLAMERPTSGKLLLAGQDLGQISNAQIPfLRRQIGVVFQNHQLLFDRTVFNNIALPLQIL 107
Cdd:PRK14267 35 LMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPFPHLTIYDNVAIGVKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 108 GL--SKAEIAKRVDSALERVSLSD--KGEL--FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFE 181
Cdd:PRK14267 114 GLvkSKKELDERVEWALKKAALWDevKDRLndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499850989 182 DINRLGTTVLIaSHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK14267 194 ELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-197 |
2.51e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.84 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 27 RGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQNHQLLFDRTVFNNIALPL-Q 105
Cdd:PRK11831 32 RGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLrE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 106 ILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR 185
Cdd:PRK11831 112 HTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNS 191
|
170
....*....|...
gi 499850989 186 -LGTTVLIASHDL 197
Cdd:PRK11831 192 aLGVTCVVVSHDV 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-218 |
2.79e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 96.73 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL--GQISNAQipflRR 79
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfASPRDAR----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQnhqllfdrtvfnnialplqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGD 218
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-222 |
3.08e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYPNGHvGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQ-----DLGQISNAQIPFL-R 78
Cdd:PRK11701 10 RGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLlR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQ--LLFDRTVFNNIALPLQILG--------------LSKAEI-AKRVDSAlervslsdkgelfPADLSTG 141
Cdd:PRK11701 89 TEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGarhygdiratagdwLERVEIdAARIDDL-------------PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 142 QQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFED-INRLGTTVLIASHDLAlIARM-RHRMLTLQRGRLIgdg 219
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLA-VARLlAHRLLVMKQGRVV--- 231
|
...
gi 499850989 220 EAG 222
Cdd:PRK11701 232 ESG 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
3.13e-25 |
|
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: 98.33 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTVFNNIAlPLQIlgLSKAEIAkrvdSALERVSLSDKGELFP-----------ADLSTGQQQRVGIA 149
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLD-PFGE--YSDEELW----QALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDiNRLGTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
1.32e-24 |
|
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: 95.46 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYP-NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipfLRRQ 80
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTVFNNIALPlqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLL 160
Cdd:cd03247 77 ISVLNQR-PYLFDTTLRNNLGRR----------------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-219 |
1.45e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 8 AKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL--GQISNAQIPFLRRQIGVVF 85
Cdd:PRK13645 17 AKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 86 Q--NHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSL-SDKGELFPADLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:PRK13645 97 QfpEYQL-FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 163 EPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-196 |
2.71e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 13 NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNhQLLF 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQT-PTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 DRTVFNNIALPLQILGlsKAEIAKRVDSALERVSLSDKGELFP-ADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDpr 171
Cdd:PRK10247 94 GDTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-- 169
|
170 180
....*....|....*....|....*....
gi 499850989 172 lAAEIMGVFEDINRL----GTTVLIASHD 196
Cdd:PRK10247 170 -ESNKHNVNEIIHRYvreqNIAVLWVTHD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-208 |
2.90e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 10 RYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGqdlgqisNAQIPFLRRQIGVVFQnhq 89
Cdd:NF040873 1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------GARVAYVPQRSEVPDS--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 90 llFDRTVFNNIAL----PLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:NF040873 70 --LPLTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499850989 166 GNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRML 208
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
3.04e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIAL---P-LQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQP 156
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-219 |
3.73e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.76 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpflRRQIGVVFQNHQLLFDRTVF 97
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIAL---P-LQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLA 173
Cdd:PRK09536 96 QVVEMgrtPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 174 AEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-219 |
5.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 12 PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKL----LLAGQDLGQISNAQIPF---------LR 78
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYskkiknfkeLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQ--NHQLlFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKG-ELFPADLSTGQQQRVGIARAIVHQ 155
Cdd:PRK13631 116 RRVSMVFQfpEYQL-FKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 156 PALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-223 |
5.10e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.68 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLrLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNHQLLFDRTVFNNI 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLL-ARMAGLLPGQGEILLNGRPLSDWSAAE---LARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ALPLQiLGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAI--VH-----QPALLLADEPTGNLDPRLA 173
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499850989 174 AEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG4138 170 AALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-215 |
1.31e-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: 92.88 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 14 GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflRRQIGVVF-----QNH 88
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD----AIRAGIAYvpedrKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 QLLFDRTVFNNIALPLQilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLLADEPTGNL 168
Cdd:cd03215 88 GLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 169 DPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-219 |
1.71e-23 |
|
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: 94.51 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGhVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQD-----LGQISNAQIP 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FL-RRQIGVVFQNHQ--LLFDRTVFNNIALPLQILGLSK-AEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIAR 150
Cdd:TIGR02323 82 RLmRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRdLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-223 |
1.81e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 11 YPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAM------ERPTSGKLLLAGQDLGQISNAQipfLRRQIGVV 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIK---LRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 85 FQNHQLLFDRTVFNNIALPLQILGLS-KAEIAKRVDSALERVSL----SDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-203 |
1.95e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLRLLLAM-----ERPTSGKLLLAGQDLGQiSNAQIPFLRRQIGVVFQNHQLlFDRTVFNNIALPLQIL 107
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNRLRRQVSMVHPKPNL-FPMSVYDNVAYGVKIV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 108 GL-SKAEIAKRVDSALERVSLSD--KGELFPA--DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFED 182
Cdd:PRK14258 116 GWrPKLEIDDIVESALKDADLWDeiKHKIHKSalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQS 195
|
170 180
....*....|....*....|..
gi 499850989 183 IN-RLGTTVLIASHDLALIARM 203
Cdd:PRK14258 196 LRlRSELTMVIVSHNLHQVSRL 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-221 |
2.04e-23 |
|
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: 97.42 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRRQ 80
Cdd:TIGR01842 317 LSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE---TFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLlFDRTVFNNIAL------PLQILGLSKAEIAKRVDSALER---VSLSDKGelfpADLSTGQQQRVGIARA 151
Cdd:TIGR01842 394 IGYLPQDVEL-FPGTVAENIARfgenadPEKIIEAAKLAGVHELILRLPDgydTVIGPGG----ATLSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMrHRMLTLQRGRLIGDGEA 221
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCV-DKILVLQDGRIARFGER 537
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-219 |
2.30e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.54 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFL-FVtGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqisnaqiPFLRR-----QIGVVF-QNHQL 90
Cdd:COG4586 38 VDDISFTIEPGEIVgFI-GPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---------PFKRRkefarRIGVVFgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 91 LFDrtvfnniaLPLQ--------ILGLSKAEIAKRVDSALERVSLSDKgelfpAD-----LSTGQQQRVGIARAIVHQPA 157
Cdd:COG4586 108 WWD--------LPAIdsfrllkaIYRIPDAEYKKRLDELVELLDLGEL-----LDtpvrqLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-219 |
1.67e-22 |
|
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: 90.30 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRlLLAMERP---TSGKLLLAGQDLGQISnaqipfLRRQIGVVFQNHQLLFDR 94
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLN-ALAGRRTglgVSGEVLINGRPLDKRS------FRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILGlskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:cd03213 98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 175 EIMGVFEDINRLGTTVLIASHDL-ALIARMRHRMLTLQRGRLIGDG 219
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
1.74e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRY----PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipf 76
Cdd:COG1101 1 MLELKNLSKTFnpgtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 lR-RQIGVVFQNHQL--LFDRTVFNNIALPL---QILGLSKAEIAKRVDSALERVS---------LSDKGELfpadLSTG 141
Cdd:COG1101 78 -RaKYIGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFRELLAtlglglenrLDTKVGL----LSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 142 QQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDL--ALiaRMRHRMLTLQRGRLIGD 218
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRIILD 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
1.87e-22 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 94.73 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQN-HqlLFDRTVFNNIALPLQilGLSKAEIAKrvdsALERVSLSDKGELFP-----------ADLSTGQQQRVGIA 149
Cdd:TIGR02868 412 SVCAQDaH--LFDTTVRENLRLARP--DATDEELWA----ALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDL 197
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-220 |
3.64e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 93.71 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGL----HELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKL-LLAGQDLGQISNAQiP 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPG-P 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLR----RQIGVVFQNHQLLFDRTVFNNI--ALPLQI---LGLSKAEIAKRVDSALER--VSLSDKgelFPADLSTGQQQ 144
Cdd:TIGR03269 358 DGRgrakRYIGILHQEYDLYPHRTVLDNLteAIGLELpdeLARMKAVITLKMVGFDEEkaEEILDK---YPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 145 RVGIARAIVHQPALLLADEPTGNLDP----RLAAEIMGVFEDINRlgtTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-219 |
9.36e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 12 PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMeRPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNHQLl 91
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPES---WRKHLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 92 FDRTVFNNIALplqilGLSKAEIAkRVDSALERVSLSDKGELFP-----------ADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK11174 435 PHGTLRDNVLL-----GNPDASDE-QLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIaSHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMV-THQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-195 |
1.17e-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: 88.18 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaQIPFLRRQIGVVFQNHQLLFDRTVFNNI 100
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ALPLQILGLSKAEIakrvDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVF 180
Cdd:TIGR01189 95 HFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*
gi 499850989 181 EDINRLGTTVLIASH 195
Cdd:TIGR01189 171 RAHLARGGIVLLTTH 185
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
1.47e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQN-HqlLFDRTVFNNIALplqilGLSKAEIAKRVDsALERVSLS-----DKG-ELFPAD----LSTGQQQRVGIA 149
Cdd:PRK11160 416 ISVVSQRvH--LFSATLRDNLLL-----AAPNASDEALIE-VLQQVGLEklledDKGlNAWLGEggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-221 |
7.69e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.63 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 12 PNGHV-GLHELSFRARRGEFLFVTGHSGAGKS-TLLRL--LLAMERPTSGKLLLAGQDLGQISNAQIPFLR-RQIGVVFQ 86
Cdd:PRK09473 25 PDGDVtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELNKLRaEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 87 NHQllfdrTVFNnialP--------LQIL----GLSKAEIAKRVDSALERVSLSD---KGELFPADLSTGQQQRVGIARA 151
Cdd:PRK09473 105 DPM-----TSLN----PymrvgeqlMEVLmlhkGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-216 |
9.78e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG----HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL-GQISNAQIPF 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRRQIGVVFQ-NHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLS-DKGELFPADLSTGQQQRVGIARAIVH 154
Cdd:PRK13646 83 VRKRIGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDIN-RLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-195 |
1.29e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 13 NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqisnAQIPFLRRQIgvVFQNHQ--- 89
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEAC--HYLGHRnam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 90 --LLfdrTVFNNIALPLQILGLSKAEIAkrvdSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGN 167
Cdd:PRK13539 85 kpAL---TVAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*...
gi 499850989 168 LDPRLAAEIMGVFEDINRLGTTVLIASH 195
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-219 |
2.55e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPflrrQIGVV--FQNHQLLFDRTVFNN 99
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA----RMGVVrtFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 --IALPLQ-----ILGL--------SKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:PRK11300 101 llVAQHQQlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 165 TGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-217 |
2.74e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 17 GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQ-----IPFL---RRQIGvvfqnh 88
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagIAYVpedRKGEG------ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 qLLFDRTVFNNIALP-LQILG----LSKAEIAKRVDSALERVSLSDKGELFPA-DLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:COG1129 341 -LVLDLSIRENITLAsLDRLSrgglLDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 163 EPTGNLDPRLAAEImgvFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIG 217
Cdd:COG1129 420 EPTRGIDVGAKAEI---YRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-222 |
3.05e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.88 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRLLLAMERP----TSGKLLLAGQDLGQISNAQI-PFLRRQIGVVFQNHQLLFD--RTVFNNI 100
Cdd:COG4170 33 GEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrKIIGREIAMIFQEPSSCLDpsAKIGDQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 --ALPLQILGLS----KAEIAKRVDSALERVSLSDKGEL---FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPR 171
Cdd:COG4170 113 ieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDHKDImnsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMEST 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499850989 172 LAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIgdgEAG 222
Cdd:COG4170 193 TQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTV---ESG 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
35-202 |
3.95e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRL------LLAMERpTSGKLLLAGQDL--GQISNAQIpflRRQIGVVFQNHQLlFDRTVFNNIALPLQI 106
Cdd:PRK14243 43 GPSGCGKSTILRCfnrlndLIPGFR-VEGKVTFHGKNLyaPDVDPVEV---RRRIGMVFQKPNP-FPKSIYDNIAYGARI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 107 LGLsKAEIAKRVDSALERVSL----SDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPrlaAEIMGVFED 182
Cdd:PRK14243 118 NGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP---ISTLRIEEL 193
|
170 180
....*....|....*....|..
gi 499850989 183 INRLGT--TVLIASHDLALIAR 202
Cdd:PRK14243 194 MHELKEqyTIIIVTHNMQQAAR 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-213 |
6.15e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLlA---------MERPTSGKLLLAGQD--LGQI 69
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AglwpygsgrIARPAGARVLFLPQRpyLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 70 SnaqipfLRRQIgvvfqnhqllfdrtvfnniALPLQILGLSKAEIAKrvdsALERVSLS------DKGELFPADLSTGQQ 143
Cdd:COG4178 441 T------LREAL-------------------LYPATAEAFSDAELRE----ALEAVGLGhlaerlDEEADWDQVLSLGEQ 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 144 QRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDinRL-GTTVLIASHDLALIArMRHRMLTLQRG 213
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELpGTTVISVGHRSTLAA-FHDRVLELTGD 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-210 |
6.19e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 14 GHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnaqipflrRQIGVVFqNHQLLF- 92
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI------------RRQRDEY-HQDLLYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 --------DRTVFNNIALPLQILGLSKAEiakRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:PRK13538 80 ghqpgiktELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 165 TGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTL 210
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-197 |
6.56e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQI 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDL 197
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
1.06e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpfLRRQ 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQA-LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNIALplqilGLSKAEiAKRVDSALERVSlsdkgELFP----------ADLSTGQQQRVGIAR 150
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAM-----GGFFAE-RDQFQERIKWVY-----ELFPrlherriqraGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-222 |
1.30e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 19 HELSFRARRGEFLFVTGHSGAGKS----TLLRLLLAMERPTSGKLLLAGQDLGQISnaqipfLR-RQIGVVFQNhqllfD 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA------LRgRKIATIMQN-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNnialPLQ---------ILGLSKAEIAKRVDSALERVSLSDKG---ELFPADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK10418 89 RSAFN----PLHtmhtharetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 162 DEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAG 222
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-221 |
1.73e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMeRPTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQNHQLLFDRTVFNNI 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAE---LARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ALPLQIlGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAI--VHQPA-----LLLADEPTGNLDPRLA 173
Cdd:PRK03695 91 TLHQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPDInpagqLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499850989 174 AEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEA 221
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-223 |
2.04e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPnghvGLHELSFRARRGEFLFVTGHSGAGKS-TLLRLLLAMERP----TSGKLLLAGQ-----DLGQISN 71
Cdd:PRK10261 20 IAFMQEQQKIA----AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRsrqviELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 72 AQIPFLR-RQIGVVFQNHQLLFDR--TVFNNIALPLQI-LGLSKAEIAKRVDSALERVSLSDKGEL---FPADLSTGQQQ 144
Cdd:PRK10261 96 AQMRHVRgADMAMIFQEPMTSLNPvfTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 145 RVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-216 |
2.43e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 11 YPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAM-----ERPTSGKLLLAGQDLGQiSNAQIPFLRRQIGVVF 85
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 86 QNHQLlFDRTVFNNIALPLQILGL-SKAEIAKRVDSALERVSLSD--KGELFPA--DLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK14239 93 QQPNP-FPMSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWDevKDRLHDSalGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDInRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-223 |
2.46e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.41 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKS----TLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflRRQI-----GVVFQNHQLL 91
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE----RRNLvgaevAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 92 FD--RTVFNNIALPLQI-LGLSKAEIAKRVDSALERVSLSD---KGELFPADLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:PRK11022 102 LNpcYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 166 GNLDPRLAAEIMGVFEDINRLGTTVLI-ASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVlITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-195 |
3.29e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIpFLRRQ 80
Cdd:COG1137 3 TLEAENLVKSYGKRTV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---ITHLPM-HKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGV--------VFQNhqlLfdrTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSD----KGELfpadLSTGQQQRVGI 148
Cdd:COG1137 78 LGIgylpqeasIFRK---L---TVEDNILAVLELRKLSKKEREERLEELLEEFGITHlrksKAYS----LSGGERRRVEI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 149 ARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASH 195
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-216 |
3.84e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 81.69 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIPFLRRQ 80
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID---ISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTVFNNialpLQILG-LSKAEIakrvdsaLERVSLSDKGElfpaDLSTGQQQRVGIARAIVHQPALL 159
Cdd:cd03369 84 LTIIPQD-PTLFSGTIRSN----LDPFDeYSDEEI-------YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 160 LADEPTGNLDPRLAAEIMGVF-EDINrlGTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIrEEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-219 |
5.53e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.07 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 12 PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisNAQIPFLRRQIGVVFQNHQLL 91
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 92 FDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPR 171
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499850989 172 LAAEIMGVFEDInRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:TIGR01257 1096 SRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-170 |
5.69e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.79 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGE---FLfvtGHSGAGKSTLLRLLLAMERPTSGKLLLAGQ--DLGQISnaqipfLRRQIGVVFQNHQLLFDRTV 96
Cdd:NF033858 286 SFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIA------TRRRVGYMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 97 FNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP 170
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-200 |
6.31e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLG--QISNaqipfLR 78
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLAS-----LR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQN-HqlLFDRTVFNNIALPLQILgLSKAEI--AKRVDSALERVSLSDK------GElFPADLSTGQQQRVGIA 149
Cdd:PRK11176 417 NQVALVSQNvH--LFNDTIANNIAYARTEQ-YSREQIeeAARMAYAMDFINKMDNgldtviGE-NGVLLSGGQRQRIAIA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 150 RAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDI--NRlgtTVLIASHDLALI 200
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTI 542
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
6.48e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYpNGHVGLHELSFRARRGEflfVT---GHSGAGKSTLL----RLLlameRPTSGKLLLAGQDLGQISNAQ 73
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGG---ITaliGPNGAGKSTLLsmisRLL----PPDSGEVLVDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 74 ipfLRRQIGVVFQNhqllfdrtvfNNIALPLQILGL--------SK----AEIAKRVDSALERVSLSDKGELFPADLSTG 141
Cdd:COG4604 73 ---LAKRLAILRQE----------NHINSRLTVRELvafgrfpySKgrltAEDREIIDEAIAYLDLEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 142 QQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
...
gi 499850989 221 AGQ 223
Cdd:COG4604 220 PEE 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-219 |
1.83e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipFLRRQI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDrTVFNNIAlplqiLGLSKAEiaKRVDSALERVSLSDKGELFPA-----------DLSTGQQQRVGIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVT-----LGRDISE--EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 151 AIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIAsHDLALIARMRHrMLTLQRGRLIGDG 219
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVEADT-ILVLHRGQAVEQG 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-219 |
2.04e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGlHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPflrRQI 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIA---LPLQILGLS-KAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPA 157
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVArgrYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-223 |
3.22e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPflrRQIG 82
Cdd:PRK10575 13 ALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNHQLLFDRTVFNNIAL---PLQ-ILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIgryPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINRL-GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-216 |
3.28e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgQISNAQIPfLRRQIG 82
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAA-LAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNHQLLFDRTVFNNI---ALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 160 LADEPTGNLDPRlaaEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK11288 163 AFDEPTSSLSAR---EIEQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-220 |
3.57e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHvGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLrrQ 80
Cdd:PRK09700 5 YISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVFNNI---ALPL-QILGLSK---AEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 154 HQPALLLADEPTGNLDprlAAEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK09700 162 LDAKVIIMDEPTSSLT---NKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-195 |
3.64e-18 |
|
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: 79.07 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQisnaQIPFLRRQIGVVFQNHQLLFDRTVFNNI 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ALPLQILGLSKaeiakrVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVF 180
Cdd:cd03231 95 RFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*
gi 499850989 181 EDINRLGTTVLIASH 195
Cdd:cd03231 169 AGHCARGGMVVLTTH 183
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-219 |
7.10e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNA-QIPFLRRQIGVVFQNHQLL---------------FDRTVFN 98
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEKRRIGYVFQDARLFphykvrgnlrygmakSMVAQFD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 99 NIalpLQILGLskaeiakrvDSALERvslsdkgelFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD-PRlAAEIM 177
Cdd:PRK11144 111 KI---VALLGI---------EPLLDR---------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPR-KRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 178 GVFE----DINrlgTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK11144 169 PYLErlarEIN---IPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-214 |
1.68e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 19 HELSFRARRGEFLFVTGHSGAGKS-TLLRLLLAMERP----TSGKLLLAGQDLGQISNAQIPFLR-RQIGVVFQNHQLLF 92
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 DrtvfnnialPLQILGLSKAEI----------AKRVD--SALERVSLSD-KGEL--FPADLSTGQQQRVGIARAIVHQPA 157
Cdd:PRK15134 106 N---------PLHTLEKQLYEVlslhrgmrreAARGEilNCLDRVGIRQaAKRLtdYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 158 LLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGR 214
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-220 |
3.54e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRRQIGVVFQNHQL-LFDRTVFN 98
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSYRSQRIRMIFQDPSTsLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 99 NIA-LPLQI-LGLSKAEIAKRVDSALERVSL-SDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAE 175
Cdd:PRK15112 108 QILdFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 176 IMGV-FEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK15112 188 LINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-223 |
8.14e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 12 PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflRRQIGVVF-----Q 86
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRLGVAYipedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 87 NHQLLFDRTVFNNIAL------PLQILG-LSKAEIAKRVDSALERVSLSDKGELFPAD-LSTGQQQRVGIARAIVHQPAL 158
Cdd:COG3845 344 GRGLVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 159 LLADEPTGNLDPRLAAEIMgvfediNRL------GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIH------QRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-219 |
9.24e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.09 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLgqisnAQIPF---LRRQI 81
Cdd:PRK10895 7 KNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-----SLLPLharARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFDRTVFNNIALPLQIL-GLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 161 ADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-223 |
1.49e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.08 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 99 NIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMG 178
Cdd:NF000106 106 NLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWD 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499850989 179 VFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:NF000106 186 EVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-215 |
1.72e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.32 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLRRQI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQlLFDRTvfnnialplqILGLSKAEIAKRVDSALERVSLSDK-----GELFPADLSTGQQQRVGIARAIVHQP 156
Cdd:PRK10522 400 SAVFTDFH-LFDQL----------LGPEGKPANPALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIaRMRHRMLTLQRGRL 215
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQeMGKTIFAISHDDHYF-IHADRLLEMRNGQL 527
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-195 |
2.37e-16 |
|
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: 74.61 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERP---TSGKLLLAGQdlgQISNAQIpflRRQIGVVFQNHQLLFDR 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ---PRKPDQF---QKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILG---LSKAEIAKRV-DSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP 170
Cdd:cd03234 97 TVRETLTYTAILRLprkSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*
gi 499850989 171 RLAAEIMGVFEDINRLGTTVLIASH 195
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIH 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-216 |
2.56e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 4 FEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgqisnaqipfLRrqIGV 83
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 84 VFQNHQLLFDRTVFNNIALPLQILGLSKAEIAK--------------------------------RVDSALERVSLSDKG 131
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 132 ELFP-ADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDprlaaeIMGV--FED-INRLGTTVLIASHDLALIARMRHRM 207
Cdd:COG0488 146 LDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIewLEEfLKNYPGTVLVVSHDRYFLDRVATRI 219
|
....*....
gi 499850989 208 LTLQRGRLI 216
Cdd:COG0488 220 LELDRGKLT 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-161 |
2.73e-16 |
|
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: 76.76 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG------HVGLHELSFRarRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIP 75
Cdd:COG4615 328 LELRGVTYRYPGEdgdegfTLGPIDLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLRRQIGVVFQNHQlLFDRtvfnnialplqILGLSKAEIAKRVDSALERVSLSDK-----GELFPADLSTGQQQRVgiar 150
Cdd:COG4615 403 AYRQLFSAVFSDFH-LFDR-----------LLGLDGEADPARARELLERLELDHKvsvedGRFSTTDLSQGQRKRL---- 466
|
170
....*....|.
gi 499850989 151 aivhqpALLLA 161
Cdd:COG4615 467 ------ALLVA 471
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-223 |
2.79e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 33 VTGHSGAGKSTLLRLLLAMERPTSG-----KLLLAGQDLgqISNAQIPFLRRQIGVVFQNHQLlFDRTVFNNIALPLQIL 107
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNP-FPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 108 GL-SKAEIAKRVDSALERVSL----SDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFED 182
Cdd:PRK14271 129 KLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499850989 183 I-NRLgtTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK14271 209 LaDRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-214 |
5.05e-16 |
|
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: 73.27 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAgqdlGQIS-NAQIPFLrrqigvvfQNhqllfdRTV 96
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP----GSIAyVSQEPWI--------QN------GTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIalplqILGlsKAEIAKRVDSALERVSLSDKGELFPA-----------DLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:cd03250 83 RENI-----LFG--KPFDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 166 GNLDPRLAAEImgvFED-IN---RLGTTVLIASHDLALIARMrHRMLTLQRGR 214
Cdd:cd03250 156 SAVDAHVGRHI---FENcILgllLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-195 |
5.60e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEFLFVTGHSGAGKSTLLRLLLAmerptsgkLLLAGQDLGQISNAQIPFLRrqigvvfqnhqllfDRTVFNN 99
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDNQFGR--------------EASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 IALPLQILglSKAEIakrvdsaLERVSLSDKGELF--PADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM 177
Cdd:COG2401 106 IGRKGDFK--DAVEL-------LNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 499850989 178 GVFEDINR-LGTTVLIASH 195
Cdd:COG2401 177 RNLQKLARrAGITLVVATH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-212 |
9.73e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgqisnaqipfLRrq 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQnhQLLFDRTvfnniaLPLQIL-------GLSKAEIAkrvdSALERVSLSDKGELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK09544 69 IGYVPQ--KLYLDTT------LPLTVNrflrlrpGTKKEDIL----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 154 HQPALLLADEPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQR 212
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
4.77e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLaGQDLgqisnaqipflrrQ 80
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLL-FDRTVFNNIAlplqilGLSKAEIAKRVDSALERVslsdkgeLFPAD--------LSTGQQQRVGIARA 151
Cdd:COG0488 380 IGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRF-------LFSGDdafkpvgvLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 152 IVHQPALLLADEPTGNLDPrlaaEIMGVFED-INRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI----ETLEALEEaLDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
1.26e-14 |
|
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: 68.72 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLL--------AMERPTSGKLLLAgqdlgqisnAQ 73
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLFL---------PQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 74 IPF-----LRRQIgvvfqnhqllfdrtvfnniALPLQILglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGI 148
Cdd:cd03223 72 RPYlplgtLREQL-------------------IYPWDDV------------------------------LSGGEQQRLAF 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 149 ARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDinrLGTTVLIASH 195
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-217 |
1.75e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAM--ERPTSGKLLLAGQDL--GQISNAQipflRRQIGVVFQNHQLLFD 93
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTE----RAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNNIALPLQILG----LSKAEIAKRVDSALERVSLSDKGELFP-ADLSTGQQQRVGIARAIVHQPALLLADEPTGNL 168
Cdd:TIGR02633 93 LSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 169 DPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIG 217
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-216 |
2.95e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqIPFLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYrPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNhQLLFDRTVFNNIAlPL---QILGLSKAEIAKRVDSALERVSLSDKGELFPA--DLSTGQQQRVGIARAIVH 154
Cdd:PLN03232 1311 VLSIIPQS-PVLFSGTVRFNID-PFsehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 155 QPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFK-SCTMLVIAHRLNTIIDC-DKILVLSSGQVL 1448
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-217 |
4.64e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.46 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 17 GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipflRRQIGVVF-----QNHQLL 91
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 92 FDRTVFNNIA------LPLQILGLSKAEIAKRVDSALErVSLSDKGElfPA-DLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:PRK15439 354 LDAPLAWNVCalthnrRGFWIKPARENAVLERYRRALN-IKFNHAEQ--AArTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 165 TGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIG 217
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4-195 |
8.22e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 4 FEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRlLLAMERPT----SGKLLLAGQDLGQisnaqiPFLRR 79
Cdd:TIGR00955 28 RGCFCRERPRKHL-LKNVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGMPIDA------KEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLLFDRTVFNNIA------LPLQilgLSKAEIAKRVDSALERVSLSD------------KGelfpadLSTG 141
Cdd:TIGR00955 100 ISAYVQQDDLFIPTLTVREHLMfqahlrMPRR---VTKKEKRERVDEVLQALGLRKcantrigvpgrvKG------LSGG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499850989 142 QQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASH 195
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-223 |
1.82e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 17 GLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipFLRRQIGVVFQNHQ---LLFD 93
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLANGIVYISEDRKrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNNIALPlQILGLSKAeiAKRVDSALERVSLSDKGELF----PA------DLSTGQQQRVGIARAIVHQPALLLADE 163
Cdd:PRK10762 345 MSVKENMSLT-ALRYFSRA--GGSLKHADEQQAVSDFIRLFniktPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 164 PTGNLDPRLAAEImgvFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PRK10762 422 PTRGVDVGAKKEI---YQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-223 |
4.04e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.82 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 10 RYP-NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQIsnaQIPFLRRQIGVVFQNh 88
Cdd:PRK10789 322 TYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 89 QLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERV---------SLSDKGELfpadLSTGQQQRVGIARAIVHQPALL 159
Cdd:PRK10789 398 PFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDIlrlpqgydtEVGERGVM----LSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 160 LADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMRHrMLTLQRGRLIGDGEAGQ 223
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEASE-ILVMQHGHIAQRGNHDQ 535
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
28-216 |
4.22e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRLLLAME----RPTSGKLLLAGQDLGQISNAQipfLRRQIG----VVFQNHQLLFD------ 93
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRE---RRKLVGhnvsMIFQEPQSCLDpservg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNNIalP--------LQILGLSKaeiaKRVDSALERVSLSDKGEL---FPADLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:PRK15093 110 RQLMQNI--PgwtykgrwWQRFGWRK----RRAIELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 163 EPTGNLDPRLAAEIMGVFEDINR-LGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-216 |
5.91e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQ 80
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTV-FNnialplqilgLSKAEIAKRVD--SALERVSLSD---------KGELFPA--DLSTGQQQRV 146
Cdd:PLN03130 1315 LGIIPQA-PVLFSGTVrFN----------LDPFNEHNDADlwESLERAHLKDvirrnslglDAEVSEAgeNFSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 147 GIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRlGTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK-SCTMLIIAHRLNTIIDC-DRILVLDAGRVV 1451
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-196 |
6.78e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLaGQDLgqisnaqipflrrQI 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFD-RTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFpADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:TIGR03719 388 AYVDQSRDALDPnKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKV-GQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190
....*....|....*....|....*....|....*..
gi 499850989 161 ADEPTGNLDprlaAEIMGVFED-INRLGTTVLIASHD 196
Cdd:TIGR03719 467 LDEPTNDLD----VETLRALEEaLLNFAGCAVVISHD 499
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-199 |
9.92e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQ---ISNAQIPFLRRQIGVvfqNHQLLFDR 94
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlcTYQKQLCFVGHRSGI---NPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPLQILGLSkaeiakrvdsalERVSLSDKGEL--FPAD-LSTGQQQRVGIARAIVHQPALLLADEPTGNLDPR 171
Cdd:PRK13540 94 NCLYDIHFSPGAVGIT------------ELCRLFSLEHLidYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*....
gi 499850989 172 LAAEIMGVFEDINRLGTTVLIASH-DLAL 199
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-200 |
1.00e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.24 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLagqdlgqISNAQIPFLrrqi 81
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------GSTVKIGYF---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 gvvfqnHQLlfdrtvfnnialplqilglskaeiakrvdsalervslsdkgelfpadlSTGQQQRVGIARAIVHQPALLLA 161
Cdd:cd03221 69 ------EQL------------------------------------------------SGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499850989 162 DEPTGNLDP--RLAAEimgvfEDINRLGTTVLIASHDLALI 200
Cdd:cd03221 95 DEPTNHLDLesIEALE-----EALKEYPGTVILVSHDRYFL 130
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-218 |
1.14e-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: 66.39 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEFLFVTGHSGAGKSTLLRLLL-AMERPTSGKLLLAGQDLGQISNAQIpfLRRQIGVVFQN---HQLLFDRT 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFgAYPGKFEGNVFINGKPVDIRNPAQA--IRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 96 VFNNIALPL-----QILGLSKAEIAKRVDSALERVSLSDKGELFP-ADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD 169
Cdd:TIGR02633 356 VGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 170 PRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGD 218
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-200 |
1.60e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 20 ELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLagQDLGQISNAQIPFLRRQIGVVFQNhQLLFDRTVFNN 99
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 100 IALPLQIL------------------------GLSKAEIAKRV-----------------------DSALERVS------ 126
Cdd:PTZ00265 480 IKYSLYSLkdlealsnyynedgndsqenknkrNSCRAKCAGDLndmsnttdsneliemrknyqtikDSEVVDVSkkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 127 -----LSDKGELF----PADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRlaAEIMgVFEDINRLG-----TTVLI 192
Cdd:PTZ00265 560 dfvsaLPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK--SEYL-VQKTINNLKgnenrITIII 636
|
....*...
gi 499850989 193 AsHDLALI 200
Cdd:PTZ00265 637 A-HRLSTI 643
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-217 |
2.79e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMeRPT---SGKLLLAGQDL--GQISNAQipflRRQIGVVFQNHQLLF 92
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 93 DRTVFNNIALPLQILG---LSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD 169
Cdd:PRK13549 96 ELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499850989 170 PRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIG 217
Cdd:PRK13549 176 ESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-202 |
7.77e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 4 FEQVAKRYPNG-HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQipfLRRQIG 82
Cdd:PTZ00243 1311 FEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNhQLLFDRTVFNNIALPLQIlglSKAEiakrVDSALERVSLSDK----GELFPA-------DLSTGQQQRVGIARA 151
Cdd:PTZ00243 1388 MIPQD-PVLFDGTVRQNVDPFLEA---SSAE----VWAALELVGLRERvaseSEGIDSrvleggsNYSVGQRQLMCMARA 1459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 152 IVHQ-PALLLADEPTGNLDPRL----AAEIMGVFEdinrlGTTVLIASHDLALIAR 202
Cdd:PTZ00243 1460 LLKKgSGFILMDEATANIDPALdrqiQATVMSAFS-----AYTVITIAHRLHTVAQ 1510
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-216 |
8.52e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 27 RGEFLFVTGHSGAGKSTLLRLLlAMERP-TSGKLLLAgQDLgQISNAQIPFLRRQIGVVF---------------QNHQL 90
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKIL-NGEVLlDDGRIIYE-QDL-IVARLQQDPPRNVEGTVYdfvaegieeqaeylkRYHDI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 91 LFD------RTVFNNIAL---PLQILGLSKAEiaKRVDSALERVSLSDKGELfpADLSTGQQQRVGIARAIVHQPALLLA 161
Cdd:PRK11147 105 SHLvetdpsEKNLNELAKlqeQLDHHNLWQLE--NRINEVLAQLGLDPDAAL--SSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499850989 162 DEPTGNLDprlaaeimgvFEDINRL--------GTTVLIaSHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK11147 181 DEPTNHLD----------IETIEWLegflktfqGSIIFI-SHDRSFIRNMATRIVDLDRGKLV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-213 |
1.31e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.49 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYP-NGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQD-LGQISNaqipfLR 78
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD-----VH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 RQIGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPAL 158
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRG 213
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-213 |
6.30e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 6 QVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqiPFLRRQIGV-- 83
Cdd:PRK15439 16 SISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQLGIyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 84 VFQNHQLLFDRTVFNNIALPLQilglSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADE 163
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499850989 164 PTGNLDPrlaAEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRG 213
Cdd:PRK15439 167 PTASLTP---AETERLFSRIRELlaqGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-223 |
8.19e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRLLLAMERPTS--GKLLLAGQDLGQisnaqiPFLRRqIGVVFQNHQLLFDRTVFNNIA---- 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK------QILKR-TGFVTQDDILYPHLTVRETLVfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 102 --LPLQILGLSKAEIAKRVDSALERVSLSDK--GELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM 177
Cdd:PLN03211 167 lrLPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499850989 178 GVFEDINRLGTTVLIASHD-LALIARMRHRMLTLQRGRLIGDGEAGQ 223
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-218 |
9.31e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 19 HELSFRARRGEFLFVTGHSGAGKSTLLRLLL-AMERPTSGKLLLAGQDLgQISNAQiPFLRRQIGVVFQN---HQLLFDR 94
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPV-KIRNPQ-QAIAQGIAMVPEDrkrDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIALPL--QILGLSKAEIAKRVDSALERVS-LSDKG---ELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNL 168
Cdd:PRK13549 357 GVGKNITLAAldRFTGGSRIDDAAELKTILESIQrLKVKTaspELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499850989 169 DPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGD 218
Cdd:PRK13549 437 DVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-218 |
9.39e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 17 GLHE-LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDL-----GQISNAQI---PFLRRQIGVVFQn 87
Cdd:PRK11288 267 GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRDAIRAGImlcPEDRKAEGIIPV- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 88 hqllfdRTVFNNIALP---------LQILGLSKAEIAKRVDSALeRVSLSDKGELFpADLSTGQQQRVGIARAIVHQPAL 158
Cdd:PRK11288 346 ------HSVADNINISarrhhlragCLINNRWEAENADRFIRSL-NIKTPSREQLI-MNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 159 LLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGD 218
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-211 |
9.54e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAqipflrRQIGVVFQNHQLLFDRTVFNNI 100
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS------RFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ALplqILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVF 180
Cdd:PRK13543 104 HF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170 180 190
....*....|....*....|....*....|.
gi 499850989 181 EDINRLGTTVLIASHDLALIARMRHRMLTLQ 211
Cdd:PRK13543 181 SAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-170 |
1.15e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAmERPT--SGKLLLAGQDLGqiSNAQIPFLRRQIGVVfqNHQLLFD-- 93
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRRRG--SGETIWDIKKHIGYV--SSSLHLDyr 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 -----RTV-----FNNIALPLQIlglSKAEiAKRVDSALERVSLSDKGELFP-ADLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:PRK10938 351 vstsvRNVilsgfFDSIGIYQAV---SDRQ-QKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILD 426
|
....*...
gi 499850989 163 EPTGNLDP 170
Cdd:PRK10938 427 EPLQGLDP 434
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
1.52e-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: 60.31 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLllagQDLGQIS-NAQIPFlrrqigvvfqnhqlLFDRTV 96
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----KHSGRISfSPQTSW--------------IMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIalplqILGLSKAEIakRVDSALERVSLSDKGELFPAD-----------LSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:TIGR01271 504 KDNI-----IFGLSYDEY--RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170
....*....|.
gi 499850989 166 GNLDPRLAAEI 176
Cdd:TIGR01271 577 THLDVVTEKEI 587
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-213 |
2.21e-10 |
|
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: 57.64 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLlaMERPTS----GKLLLAGQDLGqisnaqiPFLRRQIGVVFQNHQLLFD 93
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAgvitGEILINGRPLD-------KNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVfnnialplqilglskaeiakrvdsaleRVSLsdkgeLFPA---DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP 170
Cdd:cd03232 94 LTV---------------------------REAL-----RFSAllrGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499850989 171 RLAAEIMGVFEDINRLGTTVLIASHD-LALIARMRHRMLTLQRG 213
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-202 |
2.51e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 56 SGKLLLAGQDlgqISNAQIPFLRRQIGVVFQnHQLLFDRTVFNNIALPLQILGLSKAEIAKR---VDSALErvSLSDKGE 132
Cdd:PTZ00265 1276 SGKILLDGVD---ICDYNLKDLRNLFSIVSQ-EPMLFNMSIYENIKFGKEDATREDVKRACKfaaIDEFIE--SLPNKYD 1349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 133 L----FPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDI-NRLGTTVLIASHDLALIAR 202
Cdd:PTZ00265 1350 TnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRIASIKR 1424
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-215 |
6.89e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 10 RYPNGHVglHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISN--------AQIPFLRRQI 81
Cdd:PRK09700 273 SRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmAYITESRRDN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVvFQNhqllFDrtVFNNIALPLQI--------LGL-SKAEIAKRVDSALERVSLSDKG-ELFPADLSTGQQQRVGIARA 151
Cdd:PRK09700 351 GF-FPN----FS--IAQNMAISRSLkdggykgaMGLfHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRL 215
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-195 |
7.36e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 32 FVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQdlgQISNAQIPFLrrqiGVVFQNHQLLFDRTVFNNIALPLQILglsk 111
Cdd:PRK13541 30 YIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC---NINNIAKPYC----TYIGHNLGLKLEMTVFENLKFWSEIY---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 112 aEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVL 191
Cdd:PRK13541 99 -NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVL 177
|
....
gi 499850989 192 IASH 195
Cdd:PRK13541 178 LSSH 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-216 |
8.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIpfLRRQIGVVFQ 86
Cdd:PRK10982 4 ISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 87 NHQLLFDRTVFNNIAL---PLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADE 163
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 164 PTGNLDPRlaaEIMGVFEDINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:PRK10982 161 PTSSLTEK---EVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-170 |
1.19e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 8 AKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERpTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQN 87
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQT---WRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 88 hQLLFDRTVFNNIALPLQilgLSKAEIAKrvdsALERVSLSDKGELFPADL-----------STGQQQRVGIARAIVHQP 156
Cdd:TIGR01271 1301 -VFIFSGTFRKNLDPYEQ---WSDEEIWK----VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372
|
170
....*....|....
gi 499850989 157 ALLLADEPTGNLDP 170
Cdd:TIGR01271 1373 KILLLDEPSAHLDP 1386
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-200 |
1.93e-09 |
|
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: 56.68 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMeRPTSGKLLLAGQDLGQISNAQIPFLRRQ 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IgvvfqnhqlLFDRTVFNNIALPLQILGLSKAEIAK-----RVDSALER-VSLS---DKGELfpadLSTGQQQRVGIARA 151
Cdd:TIGR00954 530 T---------LRDQIIYPDSSEDMKRRGLSDKDLEQildnvQLTHILEReGGWSavqDWMDV----LSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499850989 152 IVHQPALLLADEPTGNLDPRLAAEImgvFEDINRLGTTVLIASHDLALI 200
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYM---YRLCREFGITLFSVSHRKSLW 642
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-223 |
1.95e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRLLlaMERPTSGkLLLAGQDLGQISNAQIPFLRRqIGVVFQNHQLLFDRTVFNNI---ALPLQILGLSK 111
Cdd:TIGR00956 796 GASGAGKTTLLNVL--AERVTTG-VITGGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTSTVRESLrfsAYLRQPKSVSK 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 112 AEIAKRVDSALERVSLSDKGE----LFPADLSTGQQQRVGIARAIVHQPALLL-ADEPTGNLDPRLAAEIMGVFEDINRL 186
Cdd:TIGR00956 872 SEKMEYVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH 951
|
170 180 190
....*....|....*....|....*....|....*....
gi 499850989 187 GTTVLIASHD-LALIARMRHRMLTLQRG-RLIGDGEAGQ 223
Cdd:TIGR00956 952 GQAILCTIHQpSAILFEEFDRLLLLQKGgQTVYFGDLGE 990
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-197 |
2.29e-09 |
|
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: 55.41 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQNHQLLFDRTVF 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIAL--PLQilglskaeiAKRVDSALERVSLSDKGELFP-----------ADLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:cd03290 97 ENITFgsPFN---------KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*
gi 499850989 165 TGNLDPRLAAEIM--GVFEDINRLGTTVLIASHDL 197
Cdd:cd03290 168 FSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-176 |
7.16e-09 |
|
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: 54.48 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLllagQDLGQIS-NAQIPFlrrqigvvfqnhqlLFDRTV 96
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KHSGRISfSSQFSW--------------IMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNNIalplqILGLSKAEIakRVDSALERVSLSDKGELFPA-----------DLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:cd03291 115 KENI-----IFGVSYDEY--RYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|.
gi 499850989 166 GNLDPRLAAEI 176
Cdd:cd03291 188 GYLDVFTEKEI 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-222 |
8.45e-09 |
|
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: 53.95 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 26 RRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqisnaqIPFLRRQIGVVFQN--HQLLFDRT-------V 96
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------VSYKPQYIKADYEGtvRDLLSSITkdfythpY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 97 FNN-IALPLQIlglskaeiakrvDSALERvslsdkgELfpADLSTGQQQRVGIArAIVHQPA-LLLADEPTGNLD--PRL 172
Cdd:cd03237 95 FKTeIAKPLQI------------EQILDR-------EV--PELSGGELQRVAIA-ACLSKDAdIYLLDEPSAYLDveQRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499850989 173 -AAEIMGVFEDINRlgTTVLIASHDLALIARMRHRMLTLqrgrligDGEAG 222
Cdd:cd03237 153 mASKVIRRFAENNE--KTAFVVEHDIIMIDYLADRLIVF-------EGEPS 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-213 |
3.07e-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: 53.41 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRY-PNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISnaqIPFLRRQ 80
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNhQLLFDRTVFNNialpLQILGLSKAEiakRVDSALERVSLSDKGELFPA-----------DLSTGQQQRVGIA 149
Cdd:TIGR00957 1362 ITIIPQD-PVLFSGSLRMN----LDPFSQYSDE---EVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLA 1433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499850989 150 RAIVHQPALLLADEPTGNLDPR----LAAEIMGVFEDinrlgTTVLIASHDLALIarMRH-RMLTLQRG 213
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLEtdnlIQSTIRTQFED-----CTVLTIAHRLNTI--MDYtRVIVLDKG 1495
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-223 |
3.70e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAmeRPT----SGKLLLAGQDLGQISNAQIPFLRRQIGV----VFQNHQ 89
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKKQETFARISGYCEQNDIhspqVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 90 LLFdrTVFnnIALPLQIlglSKAEIAKRVDSALERV---SLSDKGELFPA--DLSTGQQQRVGIARAIVHQPALLLADEP 164
Cdd:PLN03140 974 LIY--SAF--LRLPKEV---SKEEKMMFVDEVMELVeldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 165 TGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLAL-IARMRHRMLTLQR-GRLIGDGEAGQ 223
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRgGQVIYSGPLGR 1107
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-219 |
4.11e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRypnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRlLLAMERPTS---------GKLLLAGQDLGQISNAQIPFL 77
Cdd:PRK13547 9 VARR---HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLK-ALAGDLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 78 RrqiGVVFQNHQLLFDRTVFNNIALPLQILGLSKAEIAKR----VDSALERVSLSDKGELFPADLSTGQQQRVGIARAIV 153
Cdd:PRK13547 85 R---AVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 154 H---------QPALLLADEPTGNLDPRLAAEIMGVFEDINR---LGttVLIASHDLALIARMRHRMLTLQRGRLIGDG 219
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnLG--VLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-189 |
4.98e-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: 53.03 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFqNHQLL--FDRT 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILF-GKALNekYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 96 VFNNIALplqilgLSKAEIAKRVDsaleRVSLSDKGelfpADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAE 175
Cdd:TIGR00957 733 VLEACAL------LPDLEILPSGD----RTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180
....*....|....*....|.
gi 499850989 176 I-------MGVFEDINRLGTT 189
Cdd:TIGR00957 799 IfehvigpEGVLKNKTRILVT 819
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-198 |
8.69e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYP-----------------NG--HVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLA 62
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklkdlffrskDGeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 63 GQ-DLGQISNAqipflrrqigvvfQNHQLlfdrTVFNNIALPLQILGLSKAEIAKRVDSALErvsLSDKGELFPADL--- 138
Cdd:PRK13545 85 GSaALIAISSG-------------LNGQL----TGIENIELKGLMMGLTKEKIKEIIPEIIE---FADIGKFIYQPVkty 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 139 STGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLA 198
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
1.02e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYpNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLaGQDLgqisnaqipflrrQI 81
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 82 GVVFQNHQLLFD-RTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFpADLSTGQQQRVGIARAIVHQPALLL 160
Cdd:PRK11819 390 AYVDQSRDALDPnKTVWEEISGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKV-GVLSGGERNRLHLAKTLKQGGNVLL 468
|
170 180 190
....*....|....*....|....*....|....*...
gi 499850989 161 ADEPTGNLDprlaAEIMGVFED--INRLGTTVLIaSHD 196
Cdd:PRK11819 469 LDEPTNDLD----VETLRALEEalLEFPGCAVVI-SHD 501
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-222 |
1.02e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 25 ARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLA------GQDLGQISNAQIPFLRRQIGVVFQNHQLlfdrtvfn 98
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLLRSITDDLGSSYY-------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 99 nialplqilglsKAEIAKRVdsALERvsLSDKgELfpADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD--PRLAAEI 176
Cdd:PRK13409 434 ------------KSEIIKPL--QLER--LLDK-NV--KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveQRLAVAK 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499850989 177 MgvfedINRL----GTTVLIASHDLALIARMRHRMLTLqrgrligDGEAG 222
Cdd:PRK13409 495 A-----IRRIaeerEATALVVDHDIYMIDYISDRLMVF-------EGEPG 532
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-223 |
1.51e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 8 AKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERpTSGKLLLAGQDLGQISNAQipfLRRQIGVVFQN 87
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQK---WRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 88 hQLLFDRTVFNNialpLQILGLSKAEIAKRVdsaLERVSLSDKGELFPADL-----------STGQQQRVGIARAIVHQP 156
Cdd:cd03289 86 -VFIFSGTFRKN----LDPYGKWSDEEIWKV---AEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 157 ALLLADEPTGNLDPRLAAEIMGVFEDiNRLGTTVLIASHDLaliarmrHRMLTLQRGRLIGDGEAGQ 223
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI-------EAMLECQRFLVIEENKVRQ 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-200 |
1.67e-07 |
|
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: 50.94 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 25 ARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLA------GQDLGQISNAQI-PFLRRQIGVVFQNHQLlfdrtvf 97
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPDYDGTVeEFLRSANTDDFGSSYY------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 nnialplqilglsKAEIAKRVDsaLERvsLSDKgELfpADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDprlAAEIM 177
Cdd:COG1245 436 -------------KTEIIKPLG--LEK--LLDK-NV--KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQRL 492
|
170 180
....*....|....*....|....*..
gi 499850989 178 GVFEDINRL----GTTVLIASHDLALI 200
Cdd:COG1245 493 AVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-220 |
3.66e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 3 RFEQVAKrypnghVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLlagqdlGQISNAQIPFLRRQIG 82
Cdd:PTZ00243 667 FFELEPK------VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------AERSIAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 VVFQNHQLLFDRTVFNNIALPLQILGLsKAEIAKrVDSALErVSLSDKGelfpADLSTGQQQRVGIARAIVHQPALLLAD 162
Cdd:PTZ00243 735 ATVRGNILFFDEEDAARLADAVRVSQL-EADLAQ-LGGGLE-TEIGEKG----VNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 163 EPTGNLDPRLAAEIMgvfED--INRL-GTTVLIASHDLALIARMRHrMLTLQRGRLIGDGE 220
Cdd:PTZ00243 808 DPLSALDAHVGERVV---EEcfLGALaGKTRVLATHQVHVVPRADY-VVALGDGRVEFSGS 864
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-195 |
4.59e-07 |
|
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: 48.68 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAME--RPTSGKLLLAGQDLGQISNAQIPflRRQIGVVFQNhqllfdrt 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 96 vfnnialPLQILGLSKAEIAKRVDsalervslsdkgelfpADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP---RL 172
Cdd:cd03217 86 -------PPEIPGVKNADFLRYVN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdalRL 142
|
170 180
....*....|....*....|...
gi 499850989 173 AAEimgVFEDINRLGTTVLIASH 195
Cdd:cd03217 143 VAE---VINKLREEGKSVLIITH 162
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-216 |
5.79e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQ-------------VAKRYPNGHVgLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAgqdlgq 68
Cdd:PRK15064 307 IRFEQdkklhrnalevenLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 69 iSNAqipflrrQIGVVFQNHQLLF--DRTVFNNIAlplQILGLSKAEIAKRvdSALERVslsdkgeLFPAD--------L 138
Cdd:PRK15064 380 -ENA-------NIGYYAQDHAYDFenDLTLFDWMS---QWRQEGDDEQAVR--GTLGRL-------LFSQDdikksvkvL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 139 STGQQQRVGIARAIVHQPALLLADEPTGNLDprlaaeiMgvfEDINRLGT-------TVLIASHDLALIARMRHRMLTLQ 211
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------M---ESIESLNMalekyegTLIFVSHDREFVSSLATRIIEIT 509
|
....*
gi 499850989 212 RGRLI 216
Cdd:PRK15064 510 PDGVV 514
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
88-201 |
5.85e-07 |
|
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: 48.93 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 88 HQLLFDRTVFNNIALPLQILGLSKAEIAKRVDSALERVSLSDKGELFPADLSTGQQQ---RVGIARAIVHQPALLLADEP 164
Cdd:pfam13304 187 RLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEP 266
|
90 100 110
....*....|....*....|....*....|....*..
gi 499850989 165 TGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIA 201
Cdd:pfam13304 267 ESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-217 |
7.67e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDLGQ------ISN--AQIPFLRRQIGVvFQNHQ 89
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINHgfALVTEERRSTGI-YAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 90 LLFDrTVFNNIALPLQILGLSKAEIAKR----VDSALERVSLSDKGELfpADLSTGQQQRVGIARAIVHQPALLLADEPT 165
Cdd:PRK10982 343 IGFN-SLISNIRNYKNKVGLLDNSRMKSdtqwVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499850989 166 GNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIG 217
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-193 |
1.14e-06 |
|
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: 47.26 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLL---LAMERPTSGKLLLAGQDLGQISNaqipFLRRQIGVVFQNHQLLFDR 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAE----KYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 95 TVFNNIalplqilglskaeiakrvdsaleRVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:cd03233 99 TVRETL-----------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180
....*....|....*....|
gi 499850989 175 EIMGVFEDINR-LGTTVLIA 193
Cdd:cd03233 156 EILKCIRTMADvLKTTTFVS 175
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-169 |
1.35e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRLLLAMERPTSGKLLLA-GQDLGQISNAQIPFLRRqigvvfqnhqllfDRTvfnnialPLQILglskAE 113
Cdd:PRK10636 345 GRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRA-------------DES-------PLQHL----AR 400
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 114 IAKRVDSALERVSLS------DKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLD 169
Cdd:PRK10636 401 LAPQELEQKLRDYLGgfgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-216 |
1.72e-06 |
|
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: 48.01 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 7 VAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLA-GQDLGQIsnAQIPFL------RR 79
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYL--PQEPQLdptktvRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 80 QIGVVFQNHQLLFDR--TVFNNIALP---LQILGLSKAEIAKRVDSA--------LERVSlsDKGELFPAD-----LSTG 141
Cdd:TIGR03719 88 NVEEGVAEIKDALDRfnEISAKYAEPdadFDKLAAEQAELQEIIDAAdawdldsqLEIAM--DALRCPPWDadvtkLSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 142 QQQRVGIARAIVHQPALLLADEPTGNLDprlaAEIMGVFED-INRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERhLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-218 |
2.53e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 35 GHSGAGKSTLLRLLLAMERPTSGKLLLagqdLGQISNAQIPFLRRQ--IGVVFQNHQLLFDRTVFNNIAL---PLQILGL 109
Cdd:PRK10762 37 GENGAGKSTMMKVLTGIYTRDAGSILY----LGKEVTFNGPKSSQEagIGIIHQELNLIPQLTIAENIFLgreFVNRFGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 110 SK-AEIAKRVDSALERVSLSDKGELFPADLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRlaaEIMGVFEDINRL-- 186
Cdd:PRK10762 113 IDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT---ETESLFRVIRELks 189
|
170 180 190
....*....|....*....|....*....|...
gi 499850989 187 -GTTVLIASHDLALIARMRHRMLTLQRGRLIGD 218
Cdd:PRK10762 190 qGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
5-200 |
8.34e-06 |
|
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: 45.44 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 5 EQVAKRY-PNGHVgLHELSFrARRGEFLFVTGHSGAGKSTLLRLLlamerptSGKLLlagQDLGQISNAQ-----IPFLR 78
Cdd:cd03236 4 DEPVHRYgPNSFK-LHRLPV-PREGQVLGLVGPNGIGKSTALKIL-------AGKLK---PNLGKFDDPPdwdeiLDEFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 79 rqiGVVFQNHqllFDRTVFNNIA----------LPLQILGlSKAEIAKRVDSALERVSLSDKGELFP------ADLSTGQ 142
Cdd:cd03236 72 ---GSELQNY---FTKLLEGDVKvivkpqyvdlIPKAVKG-KVGELLKKKDERGKLDELVDQLELRHvldrniDQLSGGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499850989 143 QQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALI 200
Cdd:cd03236 145 LQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVL 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-220 |
1.24e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGqdlgqisnaqipflrrQIGVVFQNHQLLFDRTVF 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 98 NNIALPLQILGLSKAEIAKRVDSALErvsLSDKGELF--PA-DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIE---FSELGEFIyqPVkKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499850989 175 EIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLIGDGE 220
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-201 |
1.51e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRFEQVAKRYPNGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGqdlgqisnaqipflRRQ 80
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA--------------KVR 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 81 IGVVFQNHQLLFDRTVfNNIalpLQILGLSKAEIAKRVDSALERVSLSDKGELFPA-DLSTGQQQRVGIARAIVHQPALL 159
Cdd:PLN03073 574 MAVFSQHHVDGLDLSS-NPL---LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499850989 160 LADEPTGNLD-PRLAAEIMG--VFEDinrlgtTVLIASHDLALIA 201
Cdd:PLN03073 650 LLDEPSNHLDlDAVEALIQGlvLFQG------GVLMVSHDEHLIS 688
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-216 |
2.08e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 9 KRYPnGHVGLHELSFRARRGEFLFVTGHSGAGKSTLLRLLLAMeRPT---SGKLLLAGQ--DLGQISNAQipflrrQIGV 83
Cdd:NF040905 9 KTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEvcRFKDIRDSE------ALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 84 VFQnHQLLfdrtvfnniAL-PLqilgLSKAE-------IAK-----------RVDSALERVSLSDKGELFPADLSTGQQQ 144
Cdd:NF040905 81 VII-HQEL---------ALiPY----LSIAEniflgneRAKrgvidwnetnrRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 145 RVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRHRMLTLQRGRLI 216
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-200 |
2.60e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 22 SFRARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSG------KLLLAgqdlgqisnaqipflrrqigvVFQNHQLLFD-- 93
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtKLEVA---------------------YFDQHRAELDpe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 94 RTVFNNialplqiLGLSKAEI-----AKRVDSALERVSLSDKGELFPAD-LSTGQQQRVGIARAIVHQPALLLADEPTGN 167
Cdd:PRK11147 398 KTVMDN-------LAEGKQEVmvngrPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*
gi 499850989 168 LDprlaAEIMGVFEDI--NRLGtTVLIASHDLALI 200
Cdd:PRK11147 471 LD----VETLELLEELldSYQG-TVLLVSHDRQFV 500
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-200 |
3.09e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 3.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499850989 138 LSTGQQQRVGIARAIVHQP--ALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALI 200
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVL 152
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-216 |
3.56e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.36 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 2 IRFEQVAKRYPNG------HVGLHelsfrARRGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGQDlgqISNAQIP 75
Cdd:cd03288 20 IKIHDLCVRYENNlkpvlkHVKAY-----IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID---ISKLPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 76 FLRRQIGVVFQNHQLLFDRTVFN----------NIALPLQILGLSKaeIAKRVDSALERVsLSDKGELFpadlSTGQQQR 145
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNldpeckctddRLWEALEIAQLKN--MVKSLPGGLDAV-VTEGGENF----SVGQRQL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499850989 146 VGIARAIVHQPALLLADEPTGNLDprLAAE------IMGVFEDinrlgTTVLIASHDLALIARMrHRMLTLQRGRLI 216
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASID--MATEnilqkvVMTAFAD-----RTVVTIAHRVSTILDA-DLVLVLSRGILV 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-170 |
4.82e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 38 GAGKSTLLRLLLAMERPTSGKLLLAGQDLGQISN-----AQIPFLRRQIGvvfqnHQLLFDRTVFNNIALPLQILGLSKA 112
Cdd:NF033858 37 GVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrravcPRIAYMPQGLG-----KNLYPTLSVFENLDFFGRLFGQDAA 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499850989 113 EIAKRVDSALERVSLSDkgelF---PA-DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDP 170
Cdd:NF033858 112 ERRRRIDELLRATGLAP----FadrPAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-223 |
2.08e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 18 LHELSFRARRGEFLFVTGHSGAGkstllRLLLAME-------RPTSGKLLLAGQ--DLGQISNA---QIPFL---RRQIG 82
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAG-----RTELAMSvfgrsygRNISGTVFKDGKevDVSTVSDAidaGLAYVtedRKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 83 vvfqnhqLLFDRTVFNNIALPlqilGLSKaeIAKR--VDSALERVSlsdkGELFPAD--------------LSTGQQQRV 146
Cdd:NF040905 351 -------LNLIDDIKRNITLA----NLGK--VSRRgvIDENEEIKV----AEEYRKKmniktpsvfqkvgnLSGGNQQKV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 147 GIARAIVHQPALLLADEPTGNLDPRLAAEIMGVfedINRL---GTTVLIASHDLALIARMRHRMLTLQRGRLIGD---GE 220
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INELaaeGKGVIVISSELPELLGMCDRIYVMNEGRITGElprEE 490
|
...
gi 499850989 221 AGQ 223
Cdd:NF040905 491 ASQ 493
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-169 |
4.80e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 1 MIRfeqVAKRYPNGHVGLHE--LSF--RARRGeflfVTGHSGAGKSTLLRLLLAMERPTSGKLLLAgqdlgqisnaqiPF 76
Cdd:PRK11819 9 MNR---VSKVVPPKKQILKDisLSFfpGAKIG----VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------------PG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 77 LRrqIGVVFQNHQLLFDRTVFNNIALPLQ-ILGLSK--------------------AEIAK-----------RVDSALER 124
Cdd:PRK11819 70 IK--VGYLPQEPQLDPEKTVRENVEEGVAeVKAALDrfneiyaayaepdadfdalaAEQGElqeiidaadawDLDSQLEI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499850989 125 VSlsDKGELFPAD-----LSTGQQQRVGIARAIVHQPALLLADEPTGNLD 169
Cdd:PRK11819 148 AM--DALRCPPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
5.90e-04 |
|
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: 38.89 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 27 RGEFLFVTGHSGAGKSTLLRLLLAMERPTSGKLLLAGqdlGQISNAQIPFLRRQIGVVFQNHQllfdrtvfnnialplqi 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGKKAS----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 107 lglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIM------GVF 180
Cdd:smart00382 61 -------------------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLL 109
|
170 180
....*....|....*....|...
gi 499850989 181 EDINRLGTTVLIASHDLALIARM 203
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-169 |
6.55e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 21 LSFRARRGeflfVTGHSGAGKSTLLRlLLAMER----PTSGKLLLAGQD--------LGQISNAQIP---FLRRQIGVVF 85
Cdd:PLN03073 200 LAFGRHYG----LVGRNGTGKTTFLR-YMAMHAidgiPKNCQILHVEQEvvgddttaLQCVLNTDIErtqLLEEEAQLVA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 86 QNHQLLFDrTVFNNIALPlQILGLSKAEIAKRVDSALERVSLSD------------KGELFPADL--------STGQQQR 145
Cdd:PLN03073 275 QQRELEFE-TETGKGKGA-NKDGVDKDAVSQRLEEIYKRLELIDaytaearaasilAGLSFTPEMqvkatktfSGGWRMR 352
|
170 180
....*....|....*....|....
gi 499850989 146 VGIARAIVHQPALLLADEPTGNLD 169
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLD 376
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
41-195 |
6.59e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 41 KSTLLRLL-LAMERPTSGKLLLAGQDLGQISNAQIPFLRRQIGVVFQNhqllfdrtVFNNIALPLQILGLSKAEIAKRVd 119
Cdd:COG3593 78 GSLLSRLLrLLLKEEDKEELEEALEELNEELKEALKALNELLSEYLKE--------LLDGLDLELELSLDELEDLLKSL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 120 saleRVSLSDKGELFPADLSTGQQQRVGIA--RAIVH-----QPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLI 192
Cdd:COG3593 149 ----SLRIEDGKELPLDRLGSGFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
...
gi 499850989 193 ASH 195
Cdd:COG3593 225 TTH 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-205 |
7.65e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 27 RGEFLFVTGHSGAGKSTLLR---LLLAMERPTSGKLLLAGQdlGQISNAQIPFLrrqIGVVFQnhqllfdrtvfnnialp 103
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKA--GCIVAAVSAEL---IFTRLQ----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 104 lqilglskaeiakrvdsalervslsdkgelfpadLSTGQQQRVGIARAIVHQPA----LLLADEPTGNLDPRLAAEIMGV 179
Cdd:cd03227 78 ----------------------------------LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEA 123
|
170 180
....*....|....*....|....*.
gi 499850989 180 FEDINRLGTTVLIASHDLALIARMRH 205
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPELAELADK 149
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
8.20e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 26 RRGEFLFVTGHSGAGKSTLLRLLlamerptSGKLLlagQDLGQISNA----QIpfLRRQIGVVFQNHqllFDRTVFNNI- 100
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKIL-------SGELI---PNLGDYEEEpswdEV--LKRFRGTELQNY---FKKLYNGEIk 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 101 ---------ALPLQILG-----LSKAEIAKRVDSALERVSLS---DKgELfpADLSTGQQQRVGIARAIVHQPALLLADE 163
Cdd:PRK13409 162 vvhkpqyvdLIPKVFKGkvrelLKKVDERGKLDEVVERLGLEnilDR-DI--SELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*...
gi 499850989 164 PTGNLDPRlaaEIMGVFEDINRL--GTTVLIASHDLAL 199
Cdd:PRK13409 239 PTSYLDIR---QRLNVARLIRELaeGKYVLVVEHDLAV 273
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-219 |
9.44e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 28 GEFLFVTGHSGAGKSTLLRlllAMerptsgklllagqdLGQISNAQIP--FLRRQIGVVFQNhQLLFDRTVFNNIalplq 105
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLIS---AM--------------LGELSHAETSsvVIRGSVAYVPQV-SWIFNATVRENI----- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 106 ILGlSKAEiAKRVDSALERVSLSDKGELFPA-----------DLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAA 174
Cdd:PLN03232 700 LFG-SDFE-SERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499850989 175 EIMGVFEDINRLGTTVLIASHDLALIARMrHRMLTLQRGRLIGDG 219
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
109-207 |
1.27e-03 |
|
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: 38.32 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 109 LSKAEIAKRVDSALERVSLSDKGELFpaDLSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRlaaEIMGVFEDINRL-- 186
Cdd:cd03222 45 LAGQLIPNGDNDEWDGITPVYKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE---QRLNAARAIRRLse 119
|
90 100
....*....|....*....|...
gi 499850989 187 --GTTVLIASHDLALIARMRHRM 207
Cdd:cd03222 120 egKKTALVVEHDLAVLDYLSDRI 142
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-201 |
1.38e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499850989 136 ADLSTGQQQRVGIARaivHQPALLLA-----DEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIA 201
Cdd:PRK00635 475 ATLSGGEQERTALAK---HLGAELIGityilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS 542
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-192 |
6.67e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 36.92 E-value: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499850989 138 LSTGQQQRVGIARAIVHQPALLLADEPTGNLDPRLAAEIMGVFEDINRLGTT-VLI 192
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITlVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-205 |
8.03e-03 |
|
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: 36.47 E-value: 8.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499850989 138 LSTGQQQRVGIARAIVHQ--PALLLADEPTGNLDPRLAAEIMGVFEDINRLGTTVLIASHDLALIARMRH 205
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADH 207
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
24-51 |
8.51e-03 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 36.96 E-value: 8.51e-03
10 20
....*....|....*....|....*...
gi 499850989 24 RARRGEFLFVTGHSGAGKSTLLRLLLAM 51
Cdd:PRK05537 388 RHKQGFTVFFTGLSGAGKSTIAKALMVK 415
|
|
| |
