|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
2.63e-136 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 381.32 E-value: 2.63e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGGEELG 222
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-218 |
7.13e-115 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 327.22 E-value: 7.13e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGG 218
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
3.72e-103 |
|
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: 297.24 E-value: 3.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 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 |
4.42e-93 |
|
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: 271.97 E-value: 4.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-220 |
4.08e-89 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 262.29 E-value: 4.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQ---KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:COG1136 4 LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRD-IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKyRTLTLKQGRMIGGEE 220
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARAD-RVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
1.07e-84 |
|
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: 250.48 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG---QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIK-RGHVPYL 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKyRTLTLKQGR 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYAD-RIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.30e-71 |
|
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: 217.83 E-value: 1.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK---ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMIggeELGT 223
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV---EEGT 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
2.81e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 220.72 E-value: 2.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK---ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHD 196
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-216 |
6.34e-66 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 203.33 E-value: 6.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagiKRGHVPYLRRDI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQS--HHLLMDrSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG1122 78 GLVFQNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-223 |
4.55e-65 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 205.03 E-value: 4.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK---ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:PRK11153 1 MIELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggeELGT 223
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINrELGLTIVLITHEMDVVKRICDRVAVIDAGRLV---EQGT 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
8.28e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.05 E-value: 8.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNV---------ALPLVIEGFTLGEIRkRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARA 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLiARmKY--RTLTLKQGRMI 216
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDL-AR-RYadRIIGLRDGRVV 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
4.51e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 197.23 E-value: 4.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYA---GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvpyL 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 158 LLLADEPTGNLDP--KLSM--DILRLFEtfnDAGTSVLIATHDL 197
Cdd:COG1116 159 VLLMDEPFGALDAltRERLqdELLRLWQ---ETGKTVLFVTHDV 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
5.27e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 199.94 E-value: 5.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYlRRD 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSH----HLlmdrSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:COG3842 79 VGMVFQDYalfpHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDPKL--SM--DILRLFETFndaGTSVLIATHD 196
Cdd:COG3842 155 RVLLLDEPLSALDAKLreEMreELRRLQREL---GITFIYVTHD 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
9.74e-61 |
|
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: 189.65 E-value: 9.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-----GVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 162 DEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd03259 155 DEPLSALDAKLREELREELkELQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
2.70e-60 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 188.44 E-value: 2.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQ--SHHLLMDRsVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03225 78 GLVFQnpDDQFFGPT-VEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
6.89e-60 |
|
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: 188.26 E-value: 6.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLvIEGFTLG--EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPL-REHTDLSeaEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
2.14e-58 |
|
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: 184.17 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKA---LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRD-IGMIFQSHHLLMDRSVFDNVALPLVIEGftLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRL-FETFNDAGTSVLIATHDLGLIARMKyRTLTLKQGRMIGGE 219
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLlFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRLVEDT 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
4.67e-58 |
|
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: 191.27 E-value: 4.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIY----AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPY 76
Cdd:COG1123 260 LLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQ--SHHLLMDRSVFDNVALPLVIEG-FTLGEIRKRVAGALDMVGLYGK--ERHnPIMLSGGEQQRVGIARA 151
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDlaDRY-PHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMIggeELGTS 224
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV---EDGPT 489
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
6.11e-58 |
|
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: 183.54 E-value: 6.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLV---------IEGFTLGEIRKRVAgALDMVGLYGKERHNPIMLSGGEQQRVGIARAI 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLgrrstwrslFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-197 |
1.04e-56 |
|
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: 179.59 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ---KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIkrghvpylR 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640581988 159 LLADEPTGNLDP--KLSM--DILRLFEtfnDAGTSVLIATHDL 197
Cdd:cd03293 153 LLLDEPFSALDAltREQLqeELLDIWR---ETGKTVLLVTHDI 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
2.66e-56 |
|
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: 178.85 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDI 81
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLViEGFTLGE--IRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLR-EHTRLSEeeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
2.48e-55 |
|
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: 176.92 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIY---AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyL 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMD--RSVFDNVALPLVIEGftLGEIRKRVAGALDMVGLYGKERHN-PIMLSGGEQQRVGIARAIVN 154
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggEELGTSPMSA 228
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV--EELTVADLLA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-202 |
1.26e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.80 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIaGIKRGHVPYLRRD 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVAL-PLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLiAR 202
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGF-AR 200
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-210 |
1.63e-54 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 173.57 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD-IGM 83
Cdd:TIGR03608 2 KNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLgLIARMKYRTLTL 210
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
2.53e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 177.57 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRD 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSH----HLlmdrSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:COG3839 77 IAMVFQSYalypHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDPKL--SM--DILRLFETFndaGTSVLIATHD 196
Cdd:COG3839 153 KVFLLDEPLSNLDAKLrvEMraEIKRLHRRL---GTTTIYVTHD 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
4.17e-54 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 173.19 E-value: 4.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 162 DEPTGNLDPKLSMDI-LRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMiggEELGT 223
Cdd:cd03300 155 DEPLGALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI---QQIGT 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
2.34e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 2.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEM-AFLtGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRD 80
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIfGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
7.25e-53 |
|
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: 168.52 E-value: 7.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIkRGHVPYLRRDI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPlviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFND-AGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
2.06e-52 |
|
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: 168.84 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQ---KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMD--RSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERH---NPIMLSGGEQQRVGIARAI 152
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-215 |
5.38e-52 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 168.07 E-value: 5.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKIYAGGQ---KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLR-RDI 81
Cdd:PRK11629 10 NLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKyRTLTLKQGRM 215
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-216 |
3.87e-51 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 165.93 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLV--------IEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-196 |
4.02e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 165.26 E-value: 4.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRD 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGL----YGKeRHnPIMLSGGEQQRVGIARAIVNKP 156
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeeYRD-RY-PHELSGGQQQRVGVARALAADP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDP----KLSMDILRLFETFndaGTSVLIATHD 196
Cdd:COG1125 156 PILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHD 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
8.36e-48 |
|
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: 164.31 E-value: 8.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASA---GRVWINGHDIAGIKrghVPY 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELS---EAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQSH-HLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNK 155
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
9.15e-48 |
|
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: 156.96 E-value: 9.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLI-----TVIERASAGRVWINGHDIAGIkRGHVPY 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDL-DVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQSHHLLmDRSVFDNVALPLVIEGFTLG-EIRKRVAGALDMVGL--YGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAgTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-225 |
2.00e-47 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 157.42 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRR-DIGMIFQSHHLLMDRS 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 96 VFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP--KLS 173
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPliRRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 174 M--DILRLFETFNDagTSVLIaTHDLGLIARMKYRTLTLKQGRMI---GGEELGTSP 225
Cdd:cd03294 199 MqdELLRLQAELQK--TIVFI-THDLDEALRLGDRIAIMKDGRLVqvgTPEEILTNP 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
2.59e-47 |
|
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: 156.74 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:COG1120 1 MLEAENLS-VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVAL---PLVIEGFTLGEI-RKRVAGALDMVGLYGKeRHNPIM-LSGGEQQRVGIARAIVNK 155
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEdREAVEEALERTGLEHL-ADRPVDeLSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
3.25e-47 |
|
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: 152.80 E-value: 3.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDIGMIFQSHHLLMDRSVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 98 DNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKE----RHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-216 |
4.86e-47 |
|
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: 156.46 E-value: 4.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG----QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGL---YgKERhNPIMLSGGEQQRVGIARAIV 153
Cdd:TIGR04521 81 RKKVGLVFQfPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdeeY-LER-SPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
5.03e-47 |
|
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: 155.54 E-value: 5.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRDI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKE--RHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 160 LADEPTGNLDP----KLSMDILRLFETFndaGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03295 158 LMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
7.52e-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: 154.33 E-value: 7.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghVPYLRRDI 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD-----LPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 162 DEPTGNLDPKL--SM--DILRLFEtfnDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd03301 155 DEPLSNLDAKLrvQMraELKRLQQ---RLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.80e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.05 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIkrgHVPYLRRDI 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDrSVFDNVALPLVIEGFTLGeiRKRVAGALDMVGLygkerhNPIM-------LSGGEQQRVGIARAIVN 154
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGL------PPDIldkpverLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-215 |
1.76e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.40 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhVPYLRRD 80
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVAL-PLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-198 |
1.79e-45 |
|
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: 150.76 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRgHVPYLRRDI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK-NINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLV-IEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLG 198
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
3.80e-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: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDiAGIkrgHVPYLRRDI 81
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFT---NLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQsHHLL---MdrSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG1118 78 GFVFQ-HYALfphM--TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 159 LLADEPTGNLDPKLSMDILR-LFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMiggEELGT 223
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI---EQVGT 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-214 |
6.21e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvpyLRRD 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLlmDR----SVFDNVALPLVIE-GFTLG---EIRKRVAGALDMVGLYGKeRHNPI-MLSGGEQQRVGIARA 151
Cdd:COG1121 77 IGYVPQRAEV--DWdfpiTVRDVVLMGRYGRrGLFRRpsrADREAVDEALERVGLEDL-ADRPIgELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
4.54e-44 |
|
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: 147.87 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDI 81
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-----DVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVI----EGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 158 LLLADEPTGNLDPKLSMDILR-LFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMiggEELGT 223
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRwLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI---EQVGT 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-216 |
6.83e-44 |
|
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: 147.20 E-value: 6.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYL--RRDIG 82
Cdd:cd03219 4 RGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----PHEiaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQSHHLLMDRSVFDNVALPLVI---EGFTLG-------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAI 152
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQArtgSGLLLArarreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-172 |
1.47e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.10 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEmaFLT--GHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRR 79
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGE--FLTllGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170
....*....|...
gi 640581988 160 LADEPTGNLDPKL 172
Cdd:PRK09452 167 LLDESLSALDYKL 179
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
6.42e-43 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 142.52 E-value: 6.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpYLRRD 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHlLMDRSVFDNValplviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03228 78 IAYVPQDPF-LFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIaTHDLGLIARMKyRTLTLKQGR 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRDAD-RIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-214 |
2.06e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 143.36 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYagGQKALSdVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRD 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----ALPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALplvieGFTLG-----EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNK 155
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-225 |
2.74e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 143.23 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI---AGIKRGHVPYLR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDN-VALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI--GGEELGTSP 225
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIeqGDASHFTQP 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
3.42e-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: 141.00 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRDI 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNvalplviegftlgeirkrvagaldmvglygkerhnpIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVREN------------------------------------LKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-197 |
1.13e-41 |
|
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: 142.57 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgiKRGHVPYLRRD 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDL 197
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNkEEGITVISITHDM 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.58e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.92 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGG---QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvPYL 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRdiGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 158 LLLADEPTGNLDP--KLSMDILrLFETFNDAGTSVLIATHD 196
Cdd:COG4525 155 FLLMDEPFGALDAltREQMQEL-LLDVWQRTGKGVFLITHS 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
1.59e-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: 138.53 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRDIG 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQshhllmdrsvfdnvalplviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640581988 163 EPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-196 |
1.00e-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: 142.48 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDIGMIFQSHHLLMDRSV 96
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT-----RLPPQKRDYGIVFQSYALFPNLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK----L 172
Cdd:TIGR03265 94 ADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARvrehL 173
|
170 180
....*....|....*....|....
gi 640581988 173 SMDILRLFETFndaGTSVLIATHD 196
Cdd:TIGR03265 174 RTEIRQLQRRL---GVTTIMVTHD 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
2.49e-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: 137.23 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRD 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIrkRVAGALDMVGLYGKErHNPI-MLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLA-DLPVrQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARmkYRTLTLKQGR 214
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDLGDFK 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-203 |
3.29e-40 |
|
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: 140.19 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERA---SAGRVWINGHDIAGIKRGHVPYLR-RDIGMI 84
Cdd:COG0444 12 PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 85 FQshhllmD--------RSVFDNVALPLVI-EGFTLGEIRKRVAGALDMVGLYGKERHN---PIMLSGGEQQRVGIARAI 152
Cdd:COG0444 92 FQ------DpmtslnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARM 203
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEI 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-216 |
5.09e-40 |
|
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: 145.36 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG-GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHlLMDRSVFDNVALPLviEGFTLGEIRK--RVAGALDMV-----GLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:COG2274 551 IGVVLQDVF-LFSGTIRENITLGD--PDATDEEIIEaaRLAGLHDFIealpmGYDTVVGEGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFnDAGTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLAD-RIIVLDKGRIV 688
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-198 |
9.72e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.10 E-value: 9.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQshhllmD-- 93
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ------Dpy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 ------RSVFDNVALPLVIEG-FTLGEIRKRVAGALDMVGLygKERH---NPIMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:COG4608 106 aslnprMTVGDIIAEPLRIHGlASKAERRERVAELLELVGL--RPEHadrYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLG 198
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-223 |
1.14e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.38 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghvPYLRRDI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL---ESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLmDRSVFDNVALPLviEGFTLGEIRK--RVAGALD-----------MVGlygkERHnpIMLSGGEQQRVGI 148
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYGR--PDATDEEVEEaaKAAQAHEfiealpdgydtVVG----ERG--VNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 149 ARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIARMKyRTLTLKQGRMIggeELGT 223
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA-HRLSTIRNAD-RILVLDDGRIV---EQGT 557
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-224 |
1.64e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 136.30 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI---AGIKRGHVPYLR 78
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDN-VALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggeELGTS 224
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV---EQGDA 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-216 |
1.80e-39 |
|
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: 136.14 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRD 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPIM-LSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGeLSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
3.24e-39 |
|
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: 134.31 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghvpylRRDIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQS--HHLLMDrSVFDNVALPLVIegftLGEIRKRVAGALDMVGLYG-KERHnPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGLKE----LDAGNEQAETVLKDLDLYAlKERH-PLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 160 LADEPTGNLDPKlSMDIL-RLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQG 213
Cdd:cd03226 149 IFDEPTSGLDYK-NMERVgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-200 |
6.71e-39 |
|
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: 133.81 E-value: 6.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrghvpYLRRDIG 82
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQSHHLLMDR--SVFDNVALPLVIEGFTLGEIRK----RVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:cd03235 72 YVPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKadkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLI 200
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLV 195
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.26e-38 |
|
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: 131.79 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghvPYLRRDIGMI 84
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP---KELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 85 FQshhllmdrsvfdnvalplviegftlgeirkrvagALDMVGLYGKeRHNPIM-LSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHL-ADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-215 |
1.41e-38 |
|
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: 136.08 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 33 LTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLG 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 113 EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDI-LRLFETFNDAGTSVL 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITFV 155
|
170 180
....*....|....*....|....
gi 640581988 192 IATHDLGLIARMKYRTLTLKQGRM 215
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
17-216 |
1.60e-38 |
|
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: 132.62 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQ-----------RGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikrGHVPYLRRDIGMIF 85
Cdd:cd03298 2 RLDKIRFSYGeqpmhfdltfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----TAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 QSHHLLMDRSVFDNVALPLViEGFTLGEI-RKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLS-PGLKLTAEdRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640581988 165 TGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03298 156 FAALDPALRAEMLDLVlDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
5.73e-38 |
|
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: 132.47 E-value: 5.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYLRRD 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP----PHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMI--FQSHHLLMDRSVFDNVALPLVI---EGFTLG------------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQ 143
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLVAAHArlgRGLLAAllrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-196 |
9.90e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 130.68 E-value: 9.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLI--TVIERASA-GRVWINGHDIAgikrgHVPYL 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagTLSPAFSAsGEVLLNGRRLT-----ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNV--ALPlviEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNK 155
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRL-FETFNDAGTSVLIATHD 196
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHD 193
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-216 |
1.02e-37 |
|
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: 131.30 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIkrghvPYLRRDIGMIFQSHHLLMDRSVF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL-----PPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 98 DNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDIL 177
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 178 RLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03299 170 EELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 |
1.03e-37 |
|
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: 129.85 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 11 YAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhVPYLRRDIGMIFQS-HH 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKG-LLERRQRVGLVFQDpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 90 LLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 640581988 170 PKLSMDILRLFETFNDAGTSVLIATHDLGLI 200
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.54e-37 |
|
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: 137.59 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDNvaLPLVIEGFTLGEIRKrvagALDMVGLYGKERHNP-----------IMLSGGEQQRVGIA 149
Cdd:COG4987 411 IAVVPQRPHLFDT-TLREN--LRLARPDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 150 RAIVNKPPLLLADEPTGNLDPKLSMDILR-LFETFndAGTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLAdLLEAL--AGRTVLLITHRLAGLERMD-RILVLEDGRIV 548
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-215 |
2.20e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 130.28 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLR-RDIGMIFQSHHLLMDRSV 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDI 176
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 177 LRLFETFN-DAGTSVLIATHDLGLIARMKyRTLTLKQGRM 215
Cdd:PRK10584 186 ADLLFSLNrEHGTTLILVTHDLQLAARCD-RRLRLVNGQL 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-196 |
5.67e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 132.54 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDIGMIFQSHHLLM 92
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-----HRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKL 172
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180
....*....|....*....|....*...
gi 640581988 173 --SM--DILRLFETFNDagTSvLIATHD 196
Cdd:PRK11432 172 rrSMreKIRELQQQFNI--TS-LYVTHD 196
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-216 |
6.65e-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: 132.67 E-value: 6.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRR-DIGMIFQSHHLL 91
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK 171
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640581988 172 LSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR01186 164 IRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIV 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
7.25e-37 |
|
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: 135.66 E-value: 7.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDrSVFDNVAL--PlvieGFTLGEIRK--RVAGALDMV-----GLygkerHNPI-----MLSGGEQQRVG 147
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLgrP----DASDEELEAalEAAGLDEFVaalpdGL-----DTPLgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 148 IARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNdAGTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQAD-RILVLDDGRIV 550
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
7.76e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.51 E-value: 7.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:PRK13548 2 MLEARNLS-VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYG-KERHNPiMLSGGEQQRVGIARAIV------ 153
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-216 |
8.37e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 132.65 E-value: 8.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRDIGMIFQSHHLLMD 93
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 174 MDI-LRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11607 186 DRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
3.10e-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: 133.57 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQsHHLLMDRSVFDNVALPLviEGFTLGEIRK--RVAGALDMVGLYGKERHNPI-----MLSGGEQQRVGIARAIVN 154
Cdd:TIGR02857 399 AWVPQ-HPFLFAGTIAENIRLAR--PDASDAEIREalERAGLDEFVAALPQGLDTPIgeggaGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFNDaGTSVLIATHDLGLIARMKY 205
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADR 525
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-197 |
3.24e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 127.89 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKIYA--GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvPYLRRdiGM 83
Cdd:PRK11248 3 QISHLYAdyGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAER--GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 640581988 164 PTGNLDP--KLSMDILrLFETFNDAGTSVLIATHDL 197
Cdd:PRK11248 155 PFGALDAftREQMQTL-LLKLWQETGKQVLLITHDI 189
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-223 |
5.05e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 127.61 E-value: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGH----------VPYLRRDIG 82
Cdd:COG4598 19 GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqLQRIRTRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQSHHLLMDRSVFDNVAL-PLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:COG4598 99 MVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMiggEELGT 223
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI---EEQGP 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-216 |
1.02e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.47 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG----QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGiKRGHVPYL 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGL-YG--KERhNPIMLSGGEQQRVGIARAIV 153
Cdd:PRK13637 82 RKKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdYEdyKDK-SPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.38e-35 |
|
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: 125.00 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGeMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRDI 81
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNdAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-216 |
2.49e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.16 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 7 VSKIYAGGQ---KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD-IG 82
Cdd:PRK10535 10 IRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 163 EPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDlGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
3.20e-35 |
|
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: 124.25 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagiKRGHVPYLRrdI 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY---QKNIEALRR--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNvalpLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
3.34e-35 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 124.47 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYA----GGQK--ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGH----DIAGIK 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 71 RGHVPYLRRD-IGmiFQSHHL-LMDR-SVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLygKER--HN-PIMLSGGEQQ 144
Cdd:COG4778 84 PREILALRRRtIG--YVSQFLrVIPRvSALDVVAEPLLERGVDREEARARARELLARLNL--PERlwDLpPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 145 RVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
4.96e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.51 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKiYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikrGHVPYLRRDI 81
Cdd:PRK10851 3 IEIANIKK-SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVI----EGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 158 LLLADEPTGNLDPKLSMDILR----LFETFNdaGTSVLIaTHDLGLIARMKYRTLTLKQGRMiggEELGT 223
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRwlrqLHEELK--FTSVFV-THDQEEAMEVADRVVVMSQGNI---EQAGT 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-214 |
5.30e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.61 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRDIGMIFQS-HHLLMDRSV 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDI 176
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 640581988 177 LRLFETFNDA-GTSVLIATHDLGLIArMKYRTLTLKQGR 214
Cdd:PRK13650 180 IKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
6.12e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGgQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIK-----RGHVP 75
Cdd:PRK11264 3 AIEVKNLVKKFHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLRRDIGMIFQSHHLLMDRSVFDNVAL-PLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-222 |
9.44e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 124.31 E-value: 9.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIK----------RGHVPYLRRDIG 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQSHHLLMDRSVFDNV-ALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHN-PIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMiggEELG 222
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI---EEEG 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-200 |
1.14e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.85 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQSHH--LLMD 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYgsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALPLVIE-GFTLGEIRKRVAGALDMVGL----YGKERHnpiMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:PRK11308 109 KKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrpehYDRYPH---MFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190
....*....|....*....|....*....|...
gi 640581988 169 DPKLSMDILRLFETF-NDAGTSVLIATHDLGLI 200
Cdd:PRK11308 186 DVSVQAQVLNLMMDLqQELGLSYVFISHDLSVV 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
1.83e-34 |
|
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: 122.61 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRD 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKeRHNPI-MLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRArTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNdAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
1.92e-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: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:COG4559 1 MLEAENLS-VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYG-KERHNPiMLSGGEQQRVGIARAIV------ 153
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQ-TLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 154 -NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-218 |
2.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 11 YAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPyLRRDIGMIFQ-SHH 89
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE-VRKTVGIVFQnPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 90 LLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK13639 90 QLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640581988 170 PKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGG 218
Cdd:PRK13639 170 PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-216 |
2.69e-34 |
|
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: 122.79 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLI-----TVIERASAGRVWINGHDIAGiKRGHVPYLRRDIGM 83
Cdd:TIGR00972 8 NLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIYD-KKIDVVELRRRVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLmDRSVFDNVALPLVIEGF-TLGEIRKRVAGALDMVGLYG--KER--HNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:TIGR00972 87 VFQKPNPF-PMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDevKDRlhDSALGLSGGQQQRLCIARALAVEPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAGTsVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR00972 166 LLLDEPTSALDPIATGKIEELIQELKKKYT-IVIVTHNMQQAARISDRTAFFYDGELV 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-216 |
8.75e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.68 E-value: 8.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK----LITVIERASA-GRVWINGHDIAGiKRGHVPY 76
Cdd:COG1117 12 IEVRNLN-VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrMNDLIPGARVeGEILLDGEDIYD-PDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQshhllmdR------SVFDNVALPLVIEGFTL-GEIRKRVAGALDMVGLYG--KER--HNPIMLSGGEQQR 145
Cdd:COG1117 90 LRRRVGMVFQ-------KpnpfpkSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAALWDevKDRlkKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 146 VGIARAIVNKPPLLLADEPTGNLDPKLSMDI----LRLFETFndagtSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIeeliLELKKDY-----TIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-216 |
2.17e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 121.07 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGG--------QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRG 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 73 HVPYLRRDIGMIFQSHHLLMD--RSVFDNVALPLV-IEGFTLGEIRKRVAGALDMVGLYGKE-RHNPIMLSGGEQQRVGI 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNprMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 149 ARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
4.92e-33 |
|
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: 118.63 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpyLRRDI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPI-MLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-196 |
5.53e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 121.87 E-value: 5.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYlRRD 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE----PA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 161 ADEPTGNLDPKL--SM--DILRLFETFndaGTSVLIATHD 196
Cdd:PRK11650 158 FDEPLSNLDAKLrvQMrlEIQRLHRRL---KTTSLYVTHD 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
9.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhVPYLRRD 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPI-MLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPThCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-216 |
9.82e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.93 E-value: 9.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG----QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA------GIKR 71
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 72 ghvpyLRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLygKER---HNPIMLSGGEQQRVG 147
Cdd:PRK13641 83 -----LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL--SEDlisKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 148 IARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-216 |
1.18e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 123.64 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 12 AGGQKALSDVSFHLQRGEMAFLTGHSGAGKS----TLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLR-RDIGMIFQ 86
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 87 ----SHHLLMdrSVFDNVALPLVI-EGFTLGEIRKRVAGALDMVGLYGKERH---NPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG4172 100 epmtSLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
1.44e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagiKRGHVPYLRRDI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK13647 82 GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI--GGEELGTSP 225
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLaeGDKSLLTDE 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-223 |
1.98e-32 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 117.72 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRDI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDrSVFDNVAL-------PLVIEGFTLGEIRKRVAGALD----MVGlygkERHnpIMLSGGEQQRVGIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYgrpdatdEEVIEAAKAAQIHDKIMRFPDgydtIVG----ERG--LKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 151 AIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIARMKyRTLTLKQGRMIggeELGT 223
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVNAD-KIIVLKDGRIV---ERGT 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-216 |
4.10e-32 |
|
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: 118.65 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYaGGQKALSDVSFHLQRGE-MAFLtGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpyLRRDIGMIFQS 87
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEvFGFL-GPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:TIGR01188 75 ASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640581988 168 LDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
6.66e-32 |
|
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: 116.72 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT-VIERASAGRVWINGHdiagiKRGH--VPYL 77
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGE-----RRGGedVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDR--SVFDnvalpLVIEGF--TLG-------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRV 146
Cdd:COG1119 77 RKRIGLVSPALQLRFPRdeTVLD-----VVLSGFfdSIGlyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 147 GIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAG-TSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-216 |
7.21e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 121.33 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTL----LKLItvierASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQshhll 91
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQ----- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 mD--------RSVFDNVALPLVI--EGFTLGEIRKRVAGALDMVGLYGKERHN-PIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG4172 370 -DpfgslsprMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-195 |
1.03e-31 |
|
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: 115.72 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVP-YLRRD 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-----KLPmHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIF--QSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYgKERHNP-IMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHIT-HLRKSKaSSLSGGERRRVEIARALATNPK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-217 |
1.44e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 115.93 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVwinghdIAGikRGHVPYLRRDIGMI 84
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAG--TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 85 FQSHHLLMDRSVFDNVALPLViegftlGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 165 TGNLDPKLSMDILRLFET-FNDAGTSVLIATHDLGLIARMKYRTLTLKQGRmIG 217
Cdd:PRK11247 161 LGALDALTRIEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-223 |
1.49e-31 |
|
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: 115.41 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG-GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRD 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDNVALPLviEGFTLGEIRK--RVAGALDMV-----GLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGR--PGATREEVEEaaRAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIARMKyRTLTLKQGRMIggeELGT 223
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLSTIENAD-RIVVLEDGKIV---ERGT 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-216 |
2.08e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.94 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 7 VSKIYAGG--------QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLR 78
Cdd:PRK10419 9 LSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMD--RSVFDNVALPLV-IEGFTLGEIRKRVAGALDMVGL-YGKERHNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK10419 89 RDIQMVFQDSISAVNprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFND-AGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-216 |
2.85e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.99 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAG----GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGI-KRGHVP 75
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKE--RHNPIMLSGGEQQRVGIARAI 152
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL-ADEfwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-214 |
3.47e-31 |
|
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: 114.07 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPY--LRRDIGMIFQSHHL 90
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP----PHerARAGIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 91 LMDRSVFDNvaLPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03224 87 FPELTVEEN--LLLGAYARRRAKRKARLERVYELFPRLKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640581988 170 PKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-216 |
4.14e-31 |
|
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: 114.12 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG-GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpYLRRD 80
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQShHLLMDRSVFDNVAlpLVIEGFTLGEIRK--RVAGALDMVgLYGKERHNPIM------LSGGEQQRVGIARAI 152
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIA--LADPGMSMERVIEaaKLAGAHDFI-SELPEGYDTIVgeqgagLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIaRMKYRTLTLKQGRMI 216
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIA-HRLSTV-KNADRIIVMEKGRIV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
5.54e-31 |
|
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: 113.14 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDI 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GmifqshhLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03269 80 G-------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 162 DEPTGNLDP---KLSMDILRlfeTFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03269 153 DEPFSGLDPvnvELLKDVIR---ELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagiKRGHVPYLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIA-THDL--GLIARmkyRTLTLKQGRMI 216
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMdeAILAD---KVIVFSEGKLI 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-223 |
2.07e-30 |
|
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: 112.32 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLmDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMV-----GLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:cd03254 80 GVVLQDTFLF-SGTIMENIRLGRPNATDEEVIEAAKEAGAHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIaRMKYRTLTLKQGRMIggeELGT 223
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTI-KNADKILVLDDGKII---EEGT 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-197 |
1.08e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.40 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQSHHLLM 92
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVALPLViEGFTLGE--IRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK11831 98 DMNVFDNVAYPLR-EHTQLPAplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*....
gi 640581988 171 kLSMDIL-RLFETFNDA-GTSVLIATHDL 197
Cdd:PRK11831 177 -ITMGVLvKLISELNSAlGVTCVVVSHDV 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-218 |
1.31e-29 |
|
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: 109.69 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 22 SFHLQ-----RGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWING---HDiaGIKRGHVPYLRRDIGMIFQSHHLLMD 93
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFD--SRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALPLviEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:cd03297 90 LNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640581988 174 MDILR-LFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGG 218
Cdd:cd03297 168 LQLLPeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-223 |
1.31e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQShHLLMDRSVFDNvaLPLVIEGFTLGEIRK--RVAGALD-----------MVGlygkERHNpiMLSGGEQQRVGI 148
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDN--IRVGRPDATDEEMRAaaERAQAHDfierkpdgydtVVG----ERGR--QLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 149 ARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIaRMKYRTLTLKQGRMIggeELGT 223
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA-HRLSTV-RNADRILVFDNGRVV---ESGS 552
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
1.97e-29 |
|
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: 108.07 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKA-LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA----GIKRGHVPY 76
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIgmifqshhLLMDRSVFDNValplviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKP 156
Cdd:cd03246 81 LPQDD--------ELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKyRTLTLKQGRM 215
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-195 |
2.67e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK-----ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrgHVP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLRRDIGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFND-AGTSVLIATH 195
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITH 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-216 |
2.71e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.12 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 20 DVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGH-VPYLRRDIGMIFQSHHLLMDRSVFD 98
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIfLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 99 NVAlplviegFTL-----GEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:COG4148 97 NLL-------YGRkraprAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 174 MDILRLFETFND-AGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4148 170 AEILPYLERLRDeLDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-197 |
3.06e-29 |
|
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: 109.09 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA--GIKRGhvpylrrdigMIFQSHHLLMDRS 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDRM----------VVFQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 96 VFDNVALPL--VIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDpKLS 173
Cdd:TIGR01184 71 VRENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD-ALT 149
|
170 180
....*....|....*....|....*.
gi 640581988 174 MDIL--RLFETFNDAGTSVLIATHDL 197
Cdd:TIGR01184 150 RGNLqeELMQIWEEHRVTVLMVTHDV 175
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
6.89e-29 |
|
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: 106.36 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVpyLRRDI 81
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA--RRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQshhllmdrsvfdnvalplviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-214 |
9.30e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaggQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRRD 80
Cdd:PRK10771 1 MLKLTDITWLY---HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT-----TTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLViEGFTL-GEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLN-PGLKLnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-192 |
1.01e-28 |
|
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: 107.76 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPY--LR 78
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP----PHriAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDNvalpLVIEGFTLGEiRKRVAGALDMVglYG-----KERHNPI--MLSGGEQQRVGIARA 151
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEEN----LLLGAYARRD-RAEVRADLERV--YElfprlKERRRQRagTLSGGEQQMLAIGRA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLI 192
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-216 |
1.16e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagiKRGHVPYLRRD 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---SEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGT-SVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQAD-RVIVMNKGEIL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
3.77e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghVPYLRRD 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHL-LMDRSVFDNVAL-PlviEGFTLG--EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFgP---ENLCLPpiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIaRMKYRTLTLKQGRMI 216
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIV 214
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
17-216 |
5.60e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.85 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRDIGMIFQshhllmdrsv 96
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE---YGDYKYRCKHIRMIFQ---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 fD-NVAL-PlvieGFTLGEI----------------RKRVAGALDMVGLYGKERH-NPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG4167 95 -DpNTSLnP----RLNIGQIleeplrlntdltaeerEERIFATLRLVGLLPEHANfYPHMLSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4167 170 IIIADEALAALDMSVRSQIINLMlELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-197 |
7.74e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 7.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGE-MAfLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI------AGIKRGh 73
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEvHA-LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprDAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 vpylrrdIGMIFQSHHLLMDRSVFDNVALPLVIEGFTL---GEIRKRVAGALDMVGLygkerhnPI-------MLSGGEQ 143
Cdd:COG1129 81 -------IAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGL-------DIdpdtpvgDLSVAQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLDPKlsmDILRLFE---TFNDAGTSVLIATHDL 197
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTER---EVERLFRiirRLKAQGVAIIYISHRL 200
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-215 |
1.57e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKA-LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRG----HVPY 76
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGmifqshhlLMDRSVFDNVALplviegftLGEIRK-------RVAGALDM-----------VGlygkerHNPIML 138
Cdd:COG4618 411 LPQDVE--------LFDGTIAENIAR--------FGDADPekvvaaaKLAGVHEMilrlpdgydtrIG------EGGARL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 139 SGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKyRTLTLKQGRM 215
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVD-KLLVLRDGRV 544
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.83e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.32 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ----KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGH---- 73
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 -----------------VPYLRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGL---YGKEr 132
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesYLQR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 133 hNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQ 212
Cdd:PRK13651 162 -SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....
gi 640581988 213 GRMI 216
Cdd:PRK13651 241 GKII 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-223 |
2.29e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG-GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRD 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQsHHLLMDRSVFDNVALPlVIEGFTLGEIRK--RVAGALDMV-----GLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:TIGR02203 408 VALVSQ-DVVLFNDTIANNIAYG-RTEQADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIARMKyRTLTLKQGRMIggeELGT 223
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLSTIEKAD-RIVVMDDGRIV---ERGT 550
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
2.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.22 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHdiaGIKRGHVPYLRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIA-THDL 197
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDL 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-216 |
3.53e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.22 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK----LITVIERAS-AGRVWINGHDIAGIKrghVPYLRRDIGM 83
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMD---VIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLMDRSVFDNVALPLVIEGF--TLGEIRKRVAGALDMVGLYG--KERHNPIM--LSGGEQQRVGIARAIVNKPP 157
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDevKDRLDAPAgkLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIaTHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKGQIV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-216 |
4.19e-27 |
|
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: 103.44 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ-KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIkrgHVPYLRRD 80
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDNVAL--PLVIEGFTLGEIRkrVAGALDMVGLYGKERHNPI-----MLSGGEQQRVGIARAIV 153
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLgaPLADDERILRAAE--LAGVTDFVNKHPNGLDLQIgergrGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMdilRLFETFND--AGTSVLIATHDLGLIArMKYRTLTLKQGRMI 216
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEE---RLKERLRQllGDKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-202 |
4.48e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 102.31 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvpylrrdigmifqshhLLM 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA---------------------YVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNvALPL-VIEGFTLG-------------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPL 158
Cdd:NF040873 62 QRSEVPD-SLPLtVRDLVAMGrwarrglwrrltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIAR 202
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-215 |
5.53e-27 |
|
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: 102.13 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAG------IKRG--HVPYLRRDIGmif 85
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrsprdaIRAGiaYVPEDRKREG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 qshhLLMDRSVFDNVALPlviegftlgeirkrvagaldmvglygkerhnpIMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:cd03215 89 ----LVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640581988 166 GNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-196 |
6.65e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.88 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 7 VSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGhdiagiKR-GHVPYLRRDIGMIF 85
Cdd:PRK11000 9 VTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE------KRmNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 QSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 640581988 166 GNLDPKL----SMDILRLFETFndaGTSVLIATHD 196
Cdd:PRK11000 162 SNLDAALrvqmRIEISRLHKRL---GRTMIYVTHD 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-216 |
6.88e-27 |
|
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: 103.18 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK--------------------ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWI 61
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 62 NghdiagikrGHVPYLRRD-----IGMIF-QSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNP 135
Cdd:cd03267 81 A---------GLVPWKRRKkflrrIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDL-EELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 136 I-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQG 213
Cdd:cd03267 151 VrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 640581988 214 RMI 216
Cdd:cd03267 231 RLL 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-217 |
6.96e-27 |
|
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: 105.58 E-value: 6.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 20 DVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA-GIKRGHVPYLRRDIGMIFQSHHLLMDRSVFD 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 99 NVALPLvieGFTLGEIRK-RVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDIL 177
Cdd:TIGR02142 95 NLRYGM---KRARPSERRiSFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 178 RLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-197 |
9.85e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 102.48 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHdiagikrghvPYLRRD---I 81
Cdd:TIGR03740 4 KNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH----------PWTRKDlhkI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKrvagALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSHIL 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
1.09e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.55 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK----LITViERASAGRVWINGHDI--AGIKRGHV 74
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITG-DKSAGSHIELLGRTVqrEGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 75 PYLRRDIGMIFQSHHLLMDRSVFDNVAL------PL---VIEGFTLGEiRKRVAGALDMVGLYGKERHNPIMLSGGEQQR 145
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwrtCFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 146 VGIARAIVNKPPLLLADEPTGNLDP---KLSMDILRlfETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPesaRIVMDTLR--DINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
1.34e-26 |
|
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: 100.85 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG-GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpyLRRD 80
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLmDRSVFDNVALPlviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLGRR----------------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 161 ADEPTGNLDPKLSMDILRLFetFNDA-GTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLI--FEVLkDKTLIWITHHLTGIEHMD-KILFLENGKII 175
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-216 |
1.53e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ----KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI-AGIKRGHVPY 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVG----LYGKerhNPIMLSGGEQQRVGIARA 151
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGisesLFEK---NPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-216 |
1.59e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.55 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ----KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI-AGIKR-GHVP 75
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGL---YGKErhNPIMLSGGEQQRVGIARA 151
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpedYVKR--SPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-216 |
1.75e-26 |
|
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: 102.59 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPylrRDI 81
Cdd:TIGR03873 2 LRLSRVS-WSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARA---RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALplviegftlGEIRKR-------------VAGALDMVGLYGKERHNPIMLSGGEQQRVGI 148
Cdd:TIGR03873 78 ALVEQDSDTAVPLTVRDVVAL---------GRIPHRslwagdsphdaavVDRALARTELSHLADRDMSTLSGGERQRVHV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 149 ARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR03873 149 ARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
1.86e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrgHVPYLRRDI 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-224 |
1.96e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.02 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQ----SHHLL 91
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQdplaSLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MdrSVFDNVALPLVI--EGFTLGEIRKRVAGALDMVGLYGK--ERHnPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK15079 115 M--TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNliNRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 168 LDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggeELGTS 224
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV---ELGTY 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-195 |
3.73e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.26 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVP-YLRR 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----HLPmHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGM--------IFQshhllmDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNP-IMLSGGEQQRVGIAR 150
Cdd:COG1137 77 RLGIgylpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKaYSLSGGERRRVEIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640581988 151 AIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
3.94e-26 |
|
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: 105.52 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVpylRRDI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLmDRSVFDNVALPL----------VIEGFTLGE-IRKRVAGALDMVGLYGKerhnpiMLSGGEQQRVGIAR 150
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLARpdatdeelwaALERVGLADwLRALPDGLDTVLGEGGA------RLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 640581988 151 AIVNKPPLLLADEPTGNLDPKLSMDILR-LFETfnDAGTSVLIATHDL 197
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEdLLAA--LSGRTVVLITHHL 530
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
1.01e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRD 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK13652 80 VGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDA-GTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-216 |
1.16e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKST----LLKLItvierASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQSHHLLM 92
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVfdNVaLPLVIEGF-------TLGEIRKRVAGALDMVGLYGKERHN-PIMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK15134 376 NPRL--NV-LQIIEEGLrvhqptlSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640581988 165 TGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
1.49e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.39 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWING-----HDIAGI---KRGHVpy 76
Cdd:PRK11701 10 RGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseaERRRL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQS--HHLLMDRSVFDNVALPLVIEGFT-LGEIRKRVAGALDMVGLyGKERHN--PIMLSGGEQQRVGIARA 151
Cdd:PRK11701 87 LRTEWGFVHQHprDGLRMQVSAGGNIGERLMAVGARhYGDIRATAGDWLERVEI-DAARIDdlPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGlIARM-KYRTLTLKQGRMI 216
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLA-VARLlAHRLLVMKQGRVV 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
1.58e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 99.90 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVP----- 75
Cdd:TIGR02323 3 LLQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSeaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 -YLRRDIGMIFQSHH--LLMDRSVFDNVA-LPLVIEGFTLGEIRKRVAGALDMVGL-YGKERHNPIMLSGGEQQRVGIAR 150
Cdd:TIGR02323 82 rLMRTEWGFVHQNPRdgLRMRVSAGANIGeRLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 151 AIVNKPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-216 |
1.60e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 10 IYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVI-----ERASAGRVWINGHDIAGIKRGHVPyLRRDIGMI 84
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 85 FQSHHLLmDRSVFDNVALPLVIEGF----TLGE-IRKRVAGA--LDMVglygKER-H-NPIMLSGGEQQRVGIARAIVNK 155
Cdd:PRK14239 92 FQQPNPF-PMSIYENVVYGLRLKGIkdkqVLDEaVEKSLKGAsiWDEV----KDRlHdSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTsVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.91e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.57 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEM-AFLtGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYL-- 77
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIfGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 -RRdigmifqshhLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKeRHNPI-MLSGGEQQRVGIARAIVNK 155
Cdd:COG4152 79 eRG----------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDR-ANKKVeELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 156 PPLLLADEPTGNLDPkLSMDILR--LFEtFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4152 148 PELLILDEPFSGLDP-VNVELLKdvIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-216 |
2.06e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.42 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD-IGMIFQSHHLLMDRS 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 96 VFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMD 175
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 176 IL-RLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10070 203 MQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-230 |
2.10e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEM-AFLtGHSGAGKSTLLKLITVIERASAGRVWINGH--DIAG----IKRGh 73
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIhALL-GENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSprdaIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 vpylrrdIGMIFQsHHLLMDR-SVFDNVAL---PLVIEGFTLGEIRKRVAGALDMVGLygkerhnPI-------MLSGGE 142
Cdd:COG3845 82 -------IGMVHQ-HFMLVPNlTVAENIVLglePTKGGRLDRKAARARIRELSERYGL-------DVdpdakveDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 143 QQRVGIARAIVNKPPLLLADEPTGNLDPKlsmDILRLFET---FNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGge 219
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQ---EADELFEIlrrLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG-- 221
|
250
....*....|.
gi 640581988 220 ELGTSPMSAKE 230
Cdd:COG3845 222 TVDTAETSEEE 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-203 |
8.45e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 99.59 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIE----RASAGRVWINGHDIAGI---KRGHVpyLRRDIGMIFQSH 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLsprERRKI--IGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 HLLMDRS--VFDNvaLPLVIEGFTL--------GEIRKRVAGALDMVGLygkERHNPIM------LSGGEQQRVGIARAI 152
Cdd:COG4170 99 SSCLDPSakIGDQ--LIEAIPSWTFkgkwwqrfKWRKKRAIELLHRVGI---KDHKDIMnsypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFND-AGTSVLIATHDLGLIARM 203
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQW 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-223 |
1.07e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 101.44 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpYLRRDI 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA---SLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDrSVFDNVAL--PlvieGFTLGEIRK--RVAgALD------------MVGlygkERHnpIMLSGGEQQR 145
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYgrP----DASEEEVEAaaRAA-QIHdfieslpdgydtRVG----ERG--LKLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 146 VGIARAIVNKPPLLLADEPTGNLDPKLSMDILrlfETFNDAG---TSVLIAtHDLGLIARMKyRTLTLKQGRMIggeELG 222
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQ---AALREVArgrTTLVIA-HRLSTIVDAD-EILVLEAGRIV---ERG 574
|
.
gi 640581988 223 T 223
Cdd:COG5265 575 T 575
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
1.33e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.05 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDN--VALPLVIEgftlgeirKRVAGALDMVGLY----GKERHNPIM------LSGGEQQRVGI 148
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNllLAAPNASD--------EALIEVLQQVGLEklleDDKGLNAWLgeggrqLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 149 ARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNdAGTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFD-RICVMDNGQII 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
1.58e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 10 IYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT-VIERASA-----GRVWINGHDIAGIKrghVPYLRRDIGM 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrLIEIYDSkikvdGKVLYFGKDIFQID---AIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLMDRSVFDNVALPLVIEGFTLG-EIRKRVAGALDMVGLYgKERHNPI-----MLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLW-KEVYDRLnspasQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIaTHDLGLIARMKYRTLTLKQGRMI---GGEELGTSP 225
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIV-SHNPQQVARVADYVAFLYNGELVewgSSNEIFTSP 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
1.60e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVI-----ERASAGRVWINGHDIAGiKRGHVPY 76
Cdd:PRK14258 8 IKVNNLS-FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQSHHLLmDRSVFDNVALPLVIEGFTLG-EIRKRVAGALDMVGLYGKERH----NPIMLSGGEQQRVGIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHkihkSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLK--QGRMIGGEELGTS 224
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVEFGLT 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-202 |
1.64e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK----LITVIERASA-GRVWINGHDIAGIKRGHVPy 76
Cdd:PRK14243 11 LRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGFRVeGKVTFHGKNLYAPDVDPVE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQSHHLLmDRSVFDNVALPLVIEGFTlGEIRKRVAGALDMVGLYG----KERHNPIMLSGGEQQRVGIARAI 152
Cdd:PRK14243 89 VRRRIGMVFQKPNPF-PKSIYDNIAYGARINGYK-GDMDELVERSLRQAALWDevkdKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTsVLIATHDLGLIAR 202
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAAR 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-215 |
2.20e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 12 AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIK----RGHVPYlrrdigmIFQS 87
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyRQQVSY-------CAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 HHLLMDrSVFDNVALPLVIEGFTLGEirKRVAGALDMVGLYGKERHNPIM-LSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 640581988 167 NLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARM-KYRTLTLKQGRM 215
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHAdKVITLQPHAGEM 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-216 |
3.19e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.45 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK----LITVIERASA-GRVWINGHDIAGIKRGHVPyLRRDIGM 83
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVeGEVRLFGRNIYSPDVDPIE-VRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHLLMDRSVFDNVALPLVIEGF--TLGEIRKRVAGALDMVGLYG--KERHN--PIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevKDRLNdyPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIaTHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLI 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
3.28e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 4 FEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGhdiaGIKRGHVPylrrdigm 83
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLRIGYLP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 ifQSHHLLMDRSVFDNvalplVIEGFT-LGEIRK------------------------------------RVAGALDMVG 126
Cdd:COG0488 68 --QEPPLDDDLTVLDT-----VLDGDAeLRALEAeleeleaklaepdedlerlaelqeefealggweaeaRAEEILSGLG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 127 LYGKERHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDpklsMDILRLFETF--NDAGTsVLIATHD 196
Cdd:COG0488 141 FPEEDLDRPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFlkNYPGT-VLVVSHD 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-216 |
3.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG----QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI-AGIKRGHVPY 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQshhlLMDRSVF-DNVALPLVIE----GFTLGEIRKRvagALDMVGLYGKERH----NPIMLSGGEQQRVG 147
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFeDTVEREIIFGpknfKMNLDEVKNY---AHRLLMDLGFSRDvmsqSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 148 IARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-202 |
5.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.01 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG----QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI-AGIKRGHVPY 76
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKER-HNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK13634 83 LRKKVGIVFQfPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIAR 202
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAAR 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-216 |
5.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrGHVPYLRRDIGMIFQS-HHLLMDRSV 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDI 176
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 177 LRLFETFNDA-GTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEAASSD-RILVMKAGEII 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-169 |
7.65e-24 |
|
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: 95.30 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG--GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLItviER---ASAGRVWINGHDIagiKRGHVPY 76
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDI---RDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGMIFQSHHLlMDRSVFDNVALPLviEGFTLGEIRK--RVAGALD-----------MVGLYGKerhnpiMLSGGEQ 143
Cdd:cd03249 75 LRSQIGLVSQEPVL-FDGTIAENIRYGK--PDATDEEVEEaaKKANIHDfimslpdgydtLVGERGS------QLSGGQK 145
|
170 180
....*....|....*....|....*.
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALD 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
9.12e-24 |
|
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: 94.74 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIY---AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpyL 77
Cdd:cd03266 1 MITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRV---AGALDMVGLYGKERHNpimLSGGEQQRVGIARAIVN 154
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLeelADRLGMEELLDRRVGG---FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-200 |
1.12e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.55 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRD 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDNVALPlVIEGFTLGEIRK--RVAGALDMV-----GLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLI 200
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI 542
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-202 |
1.20e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 94.65 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikrgHVPYLRR---DI 81
Cdd:TIGR04406 5 ENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIT-----HLPMHERarlGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPL-VIEGFTLGEIRKRVAGALDMVGLyGKERHNPIM-LSGGEQQRVGIARAIVNKPPLL 159
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQI-SHLRDNKAMsLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHD----LGLIAR 202
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNvretLDICDR 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
1.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.64 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT-VIERASAGRVWINghdIAGIKRGH--VPYL 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINgLLLPDDNPNSKIT---VDGITLTAktVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQS-HHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLiARMKYRTLTLKQGRMI 216
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIrKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLL 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-216 |
1.61e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRDIGMIFQSHHLLMD--R 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 95 SVFDNVALPLVIEGFTLGE-IRKRVAGALDMVGLygKERHN---PIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGL--LPEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 171 KLSMDILRL-FETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10261 497 SIRGQIINLlLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
2.26e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWI----NGHDIAGIKRGHVPY---------LRRDIG 82
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYskkiknfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQ--SHHLLMDRS----VFDNVALplvieGFTLGEIRKRVAGALDMVGL-YGKERHNPIMLSGGEQQRVGIARAIVNK 155
Cdd:PRK13631 120 MVFQfpEYQLFKDTIekdiMFGPVAL-----GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-216 |
3.39e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.80 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 5 EQVSKIYAGgQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGI---KRGhvpylRRDI 81
Cdd:PRK10895 7 KNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARA-----RRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLviegftlgEIRKrvagalDMVGLYGKERHNPIM---------------LSGGEQQRV 146
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVL--------QIRD------DLSAEQREDRANELMeefhiehlrdsmgqsLSGGERRRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 147 GIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-216 |
7.21e-23 |
|
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: 96.02 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYA----GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRV-------WINGHDIAGI 69
Cdd:TIGR03269 279 IIKVRNVSKRYIsvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 70 KRGHVpylRRDIGMIFQSHHLLMDRSVFDNVALPLVIE-GFTLGeiRKRVAGALDMVGLYGKERHN-----PIMLSGGEQ 143
Cdd:TIGR03269 359 GRGRA---KRYIGILHQEYDLYPHRTVLDNLTEAIGLElPDELA--RMKAVITLKMVGFDEEKAEEildkyPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLDP----KLSMDILRLFETFNDagtSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
9.87e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVpyLRRD 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPlvieGF--TLGEIRKRVAGALDMVG-LYGKERHNPIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG----GFfaERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
1.71e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK---------------------ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRV 59
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 60 WINGHdIAGIkrghvpyLrrDIGMIFQshhllMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPI-ML 138
Cdd:COG1134 84 EVNGR-VSAL-------L--ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPVkTY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 139 SGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
5.63e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInGHdiaGIKRGHVPylrrd 80
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE---TVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 igmifQSHHLL-MDRSVFDNVAlplviEGFTlGEIRKRVAGALDMVGLYGKERHNPI-MLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG0488 385 -----QHQEELdPDKTVLDELR-----DGAP-GGTEQEVRGYLGRFLFSGDDAFKPVgVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 159 LLADEPTGNLDPKlSMDILrlfetfNDA-----GTsVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG0488 454 LLLDEPTNHLDIE-TLEAL------EEAlddfpGT-VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-216 |
6.28e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.90 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIY---------------------AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVW 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 61 INGHDIAGIkrghvpylrrDIGMIFQshhllMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPI-MLS 139
Cdd:cd03220 81 VRGRVSSLL----------GLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPVkTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 140 GGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-222 |
1.02e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 20 DVSFHLQRGemafLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPyLRRDIGMIFQSHhllmDRSVF-- 97
Cdd:PRK13638 23 DFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA-LRQQVATVFQDP----EQQIFyt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 98 ---DNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKeRHNPIM-LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:PRK13638 94 didSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640581988 174 MDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGGEELG 222
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 |
2.08e-21 |
|
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: 91.79 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIE--RASAGRV-----------WINGHDIAG 68
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 69 ---------IKRGHVPY----------LRRDIGMIFQ-SHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLY 128
Cdd:TIGR03269 80 epcpvcggtLEPEEVDFwnlsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 129 GKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP---KLSMDILRlfETFNDAGTSVLIATHDLGLIARMKY 205
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPqtaKLVHNALE--EAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*....
gi 640581988 206 RTLTLKQGRMIggeELGTS 224
Cdd:TIGR03269 238 KAIWLENGEIK---EEGTP 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
2.38e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRG----HVPY 76
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelakRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRrdigmifQSHHLLMDRSVFDnvalpLVieGFtlG-----------EIRKRVAGALDMVGLYG-KERHnpI-MLSGGEQ 143
Cdd:COG4604 80 LR-------QENHINSRLTVRE-----LV--AF--GrfpyskgrltaEDREIIDEAIAYLDLEDlADRY--LdELSGGQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLDPKLS---MDILRlfETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSvqmMKLLR--RLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-217 |
2.42e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI----------AGIkrGHVPYLRRDIG 82
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairAGI--AYVPEDRKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 mifqshhLLMDRSVFDNVALPlVIEGFT------LGEIRKRVAGALDMVGLYGKERHNPIM-LSGGEQQRVGIARAIVNK 155
Cdd:COG1129 341 -------LVLDLSIRENITLA-SLDRLSrgglldRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-216 |
3.49e-21 |
|
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: 87.22 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT--VIERASAGRVWINGHDIagikrgHVPYLRR 79
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSHHLLMDRSVFDNVALPLVIEGftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 160 LADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL-GLIARMKYRTLTLKQGRMI 216
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-199 |
4.08e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikrgHVPYLRRDIGMIfqSHHLLM 92
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYL--GHRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DR--SVFDNVAlplviegF---TLGEIRKRVAGALDMVGLYGKErHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK13539 85 KPalTVAENLE-------FwaaFLGGEELDIAAALEAVGLAPLA-HLPFgYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 640581988 167 NLDPKLSMDILRLFETFNDAGTSVLIATH-DLGL 199
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAATHiPLGL 190
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-216 |
4.89e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 19 SDVSFHLQRGEMAFLTGHSGAGKS-TLLKLITVIE---RASAGRVWINGHDIAGIK-RGhvpylrRDIGMIFQShhllmD 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCAlRG------RKIATIMQN-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFD---NVALPLVIEGFTLGEIR--KRVAGALDMVGLYGKER---HNPIMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:PRK10418 89 RSAFNplhTMHTHARETCLALGKPAddATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640581988 166 GNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-202 |
5.77e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPylrRDIGMIFQSHHLLM 92
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVAL---PLVIEGFTLGEIRKR-VAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190
....*....|....*....|....*....|....
gi 640581988 169 DPKLSMDILRLFETFNDAGTSVLIATHDLGLIAR 202
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAAR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-216 |
1.72e-20 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.41 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLmDRSVFDNVAL--------PLVIEGFTLGEIRKRVAgalDMVGLYGKE-RHNPIMLSGGEQQRVGIARAI 152
Cdd:TIGR01193 551 NYLPQEPYIF-SGSILENLLLgakenvsqDEIWAACEIAEIKDDIE---NMPLGYQTElSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAgTSVLIAtHDLGlIARMKYRTLTLKQGRMI 216
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVA-HRLS-VAKQSDKIIVLDHGKII 687
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
2.01e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 85.99 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG--GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghvPYLRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQsHHLLMDRSVFDNVALPLviEGFTLGEIRK--RVAGALDMVGLYGKERHNPI-----MLSGGEQQRVGIARAI 152
Cdd:cd03248 89 KVSLVGQ-EPVLFARSLQDNIAYGL--QSCSFECVKEaaQKAHAHSFISELASGYDTEVgekgsQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAgTSVLIATHDLGLIARmKYRTLTLKQGRM 215
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-225 |
2.45e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.55 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIE----RASAGRVWINGHDIAGIK-RGHVPYLRRDIGMIFQS 87
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSpRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 HHLLMDRSvfDNVALPLV--IEGFTL-GEIRKRVA----GALDMVGLYGKERHNPIM------LSGGEQQRVGIARAIVN 154
Cdd:PRK15093 98 PQSCLDPS--ERVGRQLMqnIPGWTYkGRWWQRFGwrkrRAIELLHRVGIKDHKDAMrsfpyeLTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI---GGEELGTSP 225
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQTVetaPSKELVTTP 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
2.52e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRghvpYLRRDI 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-223 |
4.85e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 84.85 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTL-LKLITVIErASAGRVWINGHDIAGIKRgHvpYLRR 79
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIGL-H--DLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSHhLLMDRSVFDNV---------ALPLVIEGFTLGEIRKRVAGALDMVGLYGKErhNpimLSGGEQQRVGIAR 150
Cdd:cd03244 79 RISIIPQDP-VLFSGTIRSNLdpfgeysdeELWQALERVGLKEFVESLPGGLDTVVEEGGE--N---LSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 151 AIVNKPPLLLADEPTGNLDP---KLSMDILRlfETFndAGTSVLIATHDLGLIarMKY-RTLTLKQGRMIggeELGT 223
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPetdALIQKTIR--EAF--KDCTVLTIAHRLDTI--IDSdRILVLDKGRVV---EFDS 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-199 |
5.08e-20 |
|
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: 84.33 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYLRRDIGMIFQSHHLLM 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR----DEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVALPLVIegftLGEIRKRVAGALDMVGLYGKErHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK 171
Cdd:TIGR01189 87 ELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFE-DLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*....
gi 640581988 172 LSMDILRLFETFNDAGTSVLIATH-DLGL 199
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTHqDLGL 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-212 |
5.19e-20 |
|
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: 84.08 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYLRRDIGMIFQSHHLLM 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR----DSIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVALPLVIEGftlgeiRKRVAGALDMVGLYGKErHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK 171
Cdd:cd03231 87 TLSVLENLRFWHADHS------DEQVEEALARVGLNGFE-DRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 172 LSMDILRLFETFNDAGTSVLIATH-DLGlIARMKYRTLTLKQ 212
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHqDLG-LSEAGARELDLGF 200
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
1.15e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQ----KALSDVSFHLQRGEmaFLT--GHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghv 74
Cdd:COG1101 1 MLELKNLSKTFNPGTvnekRALDGLNLTIEEGD--FVTviGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 75 PYLR-RDIGMIFQ------SHHLlmdrSVFDNVALPL---VIEGFTLG-------EIRKRVAgALDMvGLygKER-HNPI 136
Cdd:COG1101 75 EYKRaKYIGRVFQdpmmgtAPSM----TIEENLALAYrrgKRRGLRRGltkkrreLFRELLA-TLGL-GL--ENRlDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 137 -MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDlgliarMKY------RTL 208
Cdd:COG1101 147 gLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN------MEQaldygnRLI 220
|
250
....*....|....*
gi 640581988 209 TLKQGRMI---GGEE 220
Cdd:COG1101 221 MMHEGRIIldvSGEE 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-197 |
1.31e-19 |
|
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: 83.75 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 23 FHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrghvpyLRRDIGMIFQSHHLLMDRSVfdNVAl 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK--------GWRHIGYVPQRHEFAWDFPI--SVA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 103 PLVIEGFT--LGEIRK-------RVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:TIGR03771 70 HTVMSGRTghIGWLRRpcvadfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180
....*....|....*....|....
gi 640581988 174 MDILRLFETFNDAGTSVLIATHDL 197
Cdd:TIGR03771 150 ELLTELFIELAGAGTAILMTTHDL 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-214 |
1.61e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.16 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKS-TLLKLITVIerASAGRV----WINGHDIAGIKRGHVPYLR-RDIGMIFQSH-- 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLPEKELNKLRaEQISMIFQDPmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 ------------------HLLMDRS--------VFDNVALPlviegftlgEIRKRVagaldmvGLYGKErhnpimLSGGE 142
Cdd:PRK09473 109 slnpymrvgeqlmevlmlHKGMSKAeafeesvrMLDAVKMP---------EARKRM-------KMYPHE------FSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 143 QQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-216 |
2.11e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 35 GHSGAGKSTLLKLITVIERASAGRVWINGH---DIAgiKRGHVPYLRRDIGMIFQSHHLLMDRSVFDNValplviegfTL 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAE--KGICLPPEKRRIGYVFQDARLFPHYKVRGNL---------RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 112 GEIRKRVAGALDMVGLYGKE----RHnPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD--------PKLSmdilRL 179
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEplldRY-PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPYLE----RL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 640581988 180 FETFNdagTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11144 175 AREIN---IPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-216 |
2.55e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEM-AFLtGHSGAGKSTLLKLITVIERASAGRVWINghdiagikrGHVPYLRR-----DIGMIF-QSH 88
Cdd:COG4586 36 EAVDDISFTIEPGEIvGFI-GPNGAGKSTTIKMLTGILVPTSGEVRVL---------GYVPFKRRkefarRIGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 HLLMDrsvfdnvaLPlVIEGFTL-GEI--------RKRVAGALDMVGLyGKERHNPI-MLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG4586 106 QLWWD--------LP-AIDSFRLlKAIyripdaeyKKRLDELVELLDL-GELLDTPVrQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-215 |
6.48e-19 |
|
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: 84.71 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRG----HVPY 76
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDREtfgkHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 LRRDIGmifqshhlLMDRSVFDNVALplVIEGFTLGEI--RKRVAGALDM-----------VGLYGkerhnpIMLSGGEQ 143
Cdd:TIGR01842 397 LPQDVE--------LFPGTVAENIAR--FGENADPEKIieAAKLAGVHELilrlpdgydtvIGPGG------ATLSGGQR 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 144 QRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYrTLTLKQGRM 215
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDK-ILVLQDGRI 531
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-182 |
7.04e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLklitvieRASAGrVWINGhdiagikRGHVpYLRRD 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL-------RAIAG-LWPYG-------SGRI-ARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIF--QSHHLLMDrSVFDNVALPLVIEGFTLGEIRKrvagALDMVGL------YGKERHNPIMLSGGEQQRVGIARAI 152
Cdd:COG4178 426 ARVLFlpQRPYLPLG-TLREALLYPATAEAFSDAELRE----ALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190
....*....|....*....|....*....|
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFET 182
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-216 |
1.35e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRDIGMIFQ--SHHLLMD 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH---FGDYSYRSQRIRMIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALPLVIE-GFTLGEIRKRVAGALDMVGLYGKE-RHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK 171
Cdd:PRK15112 104 QRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640581988 172 LSMDILRL-FETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK15112 184 MRSQLINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-216 |
1.59e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASaGRVWINGHDIAGIKrghVPYLRRDIGMIFQSHHLLMDRSVF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWS---AAELARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 98 DNVAL---PLVIEGFTLGEIRkRVAGALDMVGLYGKerhnPIM-LSGGEQQRVGIARAI------VNKPP-LLLADEPTG 166
Cdd:COG4138 88 QYLALhqpAGASSEAVEQLLA-QLAEALGLEDKLSR----PLTqLSGGEWQRVRLAAVLlqvwptINPEGqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 640581988 167 NLD--PKLSMDilRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:COG4138 163 SLDvaQQAALD--RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-229 |
2.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVI-ERAS----AGRVWINGHDIAGIKrgHVPYLRRDIGMIFQS 87
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIFNYR--DVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 HHLLmDRSVFDNVALPLVIEGFT-LGEIRKRVAGALDMVGLYG--KER--HNPIMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK14271 110 PNPF-PMSIMDNVLAGVRAHKLVpRKEFRGVAQARLTEVGLWDavKDRlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 163 EPTGNLDPKLSMDILRLFETFNDAGTsVLIATHDLGLIARMKYRTLTLKQGRMIG---GEELGTSPMSAK 229
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRLVEegpTEQLFSSPKHAE 257
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-216 |
2.57e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPylRRDIGMIFQSHHLLM 92
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNValpLVIE------GFTLG------------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK11300 94 EMTVIENL---LVAQhqqlktGLFSGllktpafrraesEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-223 |
3.56e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAG--GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrgHVpYLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD--HH-YLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSHhLLMDRSVFDNVALPLviEGFTLGEIRK--RVAGALDMVGLYGKERHNPI-----MLSGGEQQRVGIARAI 152
Cdd:TIGR00958 556 QVALVGQEP-VLFSGSVRENIAYGL--TDTPDEEIMAaaKAANAHDFIMEFPNGYDTEVgekgsQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMdilRLFETFNDAGTSVLIATHDLGLIARMKyRTLTLKQGRMiggEELGT 223
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVERAD-QILVLKKGSV---VEMGT 696
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-216 |
3.62e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAggqkALSDVSFHLQRGEMAFLTGHSGAGKS-TLLKLITVIERASA----GRVWINGHDIAGIKRGHVP- 75
Cdd:PRK10261 20 IAFMQEQQKIA----AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcDKMLLRRRSRQVIELSEQSa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 -YLRR----DIGMIFQSHHLLMDR--SVFDNVALPLVI-EGFTLGEIRKRVAGALDMVGLYGKE---RHNPIMLSGGEQQ 144
Cdd:PRK10261 96 aQMRHvrgaDMAMIFQEPMTSLNPvfTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 145 RVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
3.93e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGI--KRghvpyLR 78
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssRQ-----LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDNVAL---P-LVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVN 154
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 155 KPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-225 |
8.34e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.93 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHV------- 74
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLvayvpqs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 75 -------PYLRRDIGMIFQSHHLLMDRSvfdnvalplviegfTLGEIRKRVAGALDMVGLYgKERHNPI-MLSGGEQQRV 146
Cdd:PRK15056 87 eevdwsfPVLVEDVVMMGRYGHMGWLRR--------------AKKRDRQIVTAALARVDMV-EFRHRQIgELSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 147 GIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLtlkqgrMIGGEELGTSP 225
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV------MVKGTVLASGP 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-212 |
1.99e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 19 SDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgikRGHVPYLRRdigMIFQSHHLLMDR--SV 96
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR---RQRDEYHQD---LLYLGHQPGIKTelTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEirkRVAGALDMVGLYGKE----RHnpimLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKL 172
Cdd:PRK13538 92 LENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEdvpvRQ----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 173 SMDILRLFETFNDAGTSVLIATH-DLGLIArMKYRTLTLKQ 212
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTHqDLPVAS-DKVRKLRLGQ 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
2.74e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVwinghdiagikrGHVPYLRrd 80
Cdd:PRK09544 4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLlmdrsvfdNVALPLVIEGFTL---GEIRKRVAGALDMVGLyGKERHNPIM-LSGGEQQRVGIARAIVNKP 156
Cdd:PRK09544 69 IGYVPQKLYL--------DTTLPLTVNRFLRlrpGTKKEDILPALKRVQA-GHLIDAPMQkLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETF-NDAGTSVLIATHDLGLI 200
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHLV 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-222 |
3.49e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 19 SDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghvPYLRRDIGMIF-----QSHHLLMD 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNV-ALPLVIEGFTL--GEIRKRVAGALDMVGLYGKERHNPI-MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK15439 356 APLAWNVcALTHNRRGFWIkpARENAVLERYRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640581988 170 PKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGrMIGGEELG 222
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG-EISGALTG 487
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-200 |
4.30e-17 |
|
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: 74.79 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInghdIAGIKRGHVPylrrdi 81
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----GSTVKIGYFE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 gmifQshhllmdrsvfdnvalplviegftlgeirkrvagaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03221 70 ----Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 162 DEPTGNLDPKlSMDIL-RLFETFNDAgtsVLIATHDLGLI 200
Cdd:cd03221 95 DEPTNHLDLE-SIEALeEALKEYPGT---VILVSHDRYFL 130
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-216 |
4.51e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKS----TLLKLITVIERASAGRVWINGHDIAGIKRGHvpylRR-----DIGMIFQ 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE----RRnlvgaEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 87 SHHLLMDRSV---FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERH---NPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK11022 97 DPMTSLNPCYtvgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 161 ADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLlELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-195 |
9.66e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERAS---AGRVWINGHDIAGIK-RGHVPYLRRD---IG-------M 83
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEmRAISAYVQQDdlfIPtltvrehL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHhLLMDRSVfdnvalplviegfTLGEIRKRVAGALDMVGLyGKERHNPI-------MLSGGEQQRVGIARAIVNKP 156
Cdd:TIGR00955 121 MFQAH-LRMPRRV-------------TKKEKRERVDEVLQALGL-RKCANTRIgvpgrvkGLSGGERKRLAFASELLTDP 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-211 |
1.31e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 23 FHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKR-------GHVPYLRRDIGMIFQSHHLlmdrs 95
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfmaylGHLPGLKADLSTLENLHFL----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 96 vfdnvalplviEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMD 175
Cdd:PRK13543 107 -----------CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 640581988 176 ILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLK 211
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-215 |
1.42e-16 |
|
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: 78.52 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikRGHVPYLRRDIGMIFQSHHLLMD 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 174 MDILRLFETFNdAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:TIGR01257 1098 RSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-176 |
1.70e-16 |
|
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: 75.25 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKI--YAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI----------AGIkrGH 73
Cdd:TIGR03410 2 EVSNLnvYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppherarAGI--AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 VPYLRrdigMIFQS----HHLLMDRSVFDNVALPLVIEGFT----LGEIRKRVAGaldmvglygkerhnpiMLSGGEQQR 145
Cdd:TIGR03410 80 VPQGR----EIFPRltveENLLTGLAALPRRSRKIPDEIYElfpvLKEMLGRRGG----------------DLSGGQQQQ 139
|
170 180 190
....*....|....*....|....*....|.
gi 640581988 146 VGIARAIVNKPPLLLADEPTGNLDPKLSMDI 176
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDI 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-216 |
2.29e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRG----HVPYLRRDI----GMif 85
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarKVAYLPQQLpaaeGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 qshhllmdrSVFDNVALPLVIEGFTLG----EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK10575 101 ---------TVRELVAIGRYPWHGALGrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
2.83e-16 |
|
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: 73.34 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLklitvieRASAGrVWinghdiagikrghvPYLRRDI 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-------RALAG-LW--------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFdnvalplviegFTLGEIRKRVAGALDMVglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03223 59 GMPEGEDLLFLPQRPY-----------LPLGTLREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 640581988 162 DEPTGNLDPKLSMdilRLFETFNDAGTSVLIATH 195
Cdd:cd03223 116 DEATSALDEESED---RLYQLLKELGITVISVGH 146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
3.70e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgiKRGHVPYLRRD 80
Cdd:PRK09700 5 YISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFDNVALPLVIEGFTLG-------EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-197 |
6.35e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 12 AGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAG------IKRG--HVPYLRRDIGM 83
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsprerRRLGvaYIPEDRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IfqshhllMDRSVFDNVAL-----PLVIEGFTL--GEIRKRvagALDMVGLYG---KERHNPI-MLSGGEQQRVGIARAI 152
Cdd:COG3845 348 V-------PDMSVAENLILgryrrPPFSRGGFLdrKAIRAF---AEELIEEFDvrtPGPDTPArSLSGGNQQKVILAREL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL 462
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-216 |
6.75e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.25 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPylrRDI 81
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLLMDRSVFDNVA------LPLviegFTL--GEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIV 153
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVArgryphQPL----FTRwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFN-DAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-219 |
1.39e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA------GIKRGHVpYLRRDigmiFQSHHLL 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdGLANGIV-YISED----RKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNVALPlVIEGFT--LGEIRKR--VAGALDMVGLYG---KERHNPI-MLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:PRK10762 343 LGMSVKENMSLT-ALRYFSraGGSLKHAdeQQAVSDFIRLFNiktPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRmIGGE 219
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR-ISGE 476
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-216 |
1.44e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKIYAGgQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI------AGIKRGhvpy 76
Cdd:PRK11288 6 SFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttAALAAG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 77 lrrdIGMIFQSHHLLMDRSVFDNVALPLVIEGFTL---GEIRKRVAGALDMVGL----YGKERHnpimLSGGEQQRVGIA 149
Cdd:PRK11288 81 ----VAIIYQELHLVPEMTVAENLYLGQLPHKGGIvnrRLLNYEAREQLEHLGVdidpDTPLKY----LSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 150 RAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-195 |
1.55e-15 |
|
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: 72.69 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT-VIERASA--GRVWINGHDI-AGIKRGHVPYLRRDigMIFQShHLL 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGGTtsGQILFNGQPRkPDQFQKCVAYVRQD--DILLP-GLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNVALPLViEGFTLGEIRKRVAG------ALDMVGlygkerhNPIM--LSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:cd03234 98 VRETLTYTAILRLP-RKSSDAIRKKRVEDvllrdlALTRIG-------GNLVkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-200 |
1.57e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHL-QRGEMAfLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGhvpYLRRD 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVpSRGFVA-LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDrSVFDNVALplvieGFTLGEirKRVAGALDMV-----------GLY---GKERHNpimLSGGEQQRV 146
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTL-----GRDISE--EQVWQALETVqlaelarslpdGLYtplGEQGNN---LSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 147 GIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLI 200
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTI 538
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-214 |
2.58e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 15 QKALSDVSFHLQRGEMAFLTGHSGAGKS-TLLKLITVIERASA----GRVWINGHDIAGIKRGHVPYLRRD-IGMIFQS- 87
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTLRGVRGNkIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 -------HHLlmDRSVFDNVALPlviEGFTLGEIRKRVAGALDMVGL-YGKERHN--PIMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK15134 102 mvslnplHTL--EKQLYEVLSLH---RGMRREAARGEILNCLDRVGIrQAAKRLTdyPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 158 LLLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGR 214
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLrELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-201 |
5.89e-15 |
|
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: 70.90 E-value: 5.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRD 80
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMD--RSVFDnvalplVIEGFTLGEIRK--RVAGAldmvGLYgkerhnpimLSGGEQQRVGIARAIVNKP 156
Cdd:cd03369 84 LTIIPQDPTLFSGtiRSNLD------PFDEYSDEEIYGalRVSEG----GLN---------LSQGQRQLLCLARALLKRP 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLF-ETFNDAgtSVLIATHDLGLIA 201
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIrEEFTNS--TILTIAHRLRTII 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-194 |
1.02e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgiKRGHvpylRRDI 81
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARH----RRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 G-----MIfQ--SHHLLMDRSVFDNVA----LplviegFTLG--EIRKRVAGALDMVGLY-------GKerhnpimLSGG 141
Cdd:NF033858 75 CpriayMP-QglGKNLYPTLSVFENLDffgrL------FGQDaaERRRRIDELLRATGLApfadrpaGK-------LSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 142 EQQRVGIARAIVNKPPLLLADEPTGNLDPkLS-------MDILRLfetfNDAGTSVLIAT 194
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDP-LSrrqfwelIDRIRA----ERPGMSVLVAT 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-216 |
6.25e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDV------SFHLQRGEMAFLTGHSGAGKSTLLKLIT----------VIE-------------RASAGRVWing 63
Cdd:PRK11147 8 GAWLSFSDAplldnaELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriIYEqdlivarlqqdppRNVEGTVY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 64 hDI--AGIKrgHV-PYLRRdigmifqSHHLL-------MDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERH 133
Cdd:PRK11147 85 -DFvaEGIE--EQaEYLKR-------YHDIShlvetdpSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 134 NPimLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDpklsMDILRLFETF--NDAGTSVLIaTHDLGLIARMKYRTLTLK 211
Cdd:PRK11147 155 SS--LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFlkTFQGSIIFI-SHDRSFIRNMATRIVDLD 227
|
....*
gi 640581988 212 QGRMI 216
Cdd:PRK11147 228 RGKLV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-217 |
1.09e-13 |
|
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: 69.47 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLK-LITVIERASAGRVWINGHDIAgiKRGHVPYLRRDIGMIFQS---HHLL 91
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAGIAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNVALPlVIEGFTlGEIRKRVAGALDMVG-----LYGKERHN--PIM-LSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:TIGR02633 352 PILGVGKNITLS-VLKSFC-FKMRIDAAAELQIIGsaiqrLKVKTASPflPIGrLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 164 PTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-216 |
2.65e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASaGRVWINGHDIAG-------IKRGhvpYLRRDigmifQSHHL 90
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAwsaaelaRHRA---YLSQQ-----QTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 91 LMDrsVFDNVALPLViEGFTLGEIRKRVAGALDMVGLyGKERHNPI-MLSGGEQQRVGIARAIVNKPP-------LLLAD 162
Cdd:PRK03695 83 AMP--VFQYLTLHQP-DKTRTEAVASALNEVAEALGL-DDKLGRSVnQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 163 EPTGNLD--PKLSMDilRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK03695 159 EPMNSLDvaQQAALD--RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-199 |
6.96e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 15 QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDI-------------AGIKRGHVPYLRRDI 81
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqkqlcfVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHhllmdrSVFDNVALPLVIEGFTLGEIRKRVAGaldmvglygkerhnpiMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK13540 94 NCLYDIH------FSPGAVGITELCRLFSLEHLIDYPCG----------------LLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH-DLGL 199
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-221 |
2.35e-12 |
|
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: 63.31 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIE--RASAGRVWINGHDIAGIKrghvPYLR--RDIGMIFQSh 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP----PEERarLGIFLAFQY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 hllmdrsvfdnvalPLVIEGFTLGE-IRKRVAGaldmvglygkerhnpimLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:cd03217 86 --------------PPEIPGVKNADfLRYVNEG-----------------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 168 LDpklsMDILRL----FETFNDAGTSVLIATHDLGLIARMKY-RTLTLKQGRMI--GGEEL 221
Cdd:cd03217 135 LD----IDALRLvaevINKLREEGKSVLIITHYQRLLDYIKPdRVHVLYDGRIVksGDKEL 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-196 |
5.12e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInghdiaGIKRgHVPYlrrdigmiFQSHHLLM 92
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKL-EVAY--------FDQHRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 D--RSVFDNVAlplviEGftlgeiRKRVagaldMVGlyGKERH----------------NPI-MLSGGEQQRVGIARAIV 153
Cdd:PRK11147 395 DpeKTVMDNLA-----EG------KQEV-----MVN--GRPRHvlgylqdflfhpkramTPVkALSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 640581988 154 NKPPLLLADEPTGNLDpklsMDILRLFETFNDA--GTsVLIATHD 196
Cdd:PRK11147 457 KPSNLLILDEPTNDLD----VETLELLEELLDSyqGT-VLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-196 |
1.60e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.03 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 7 VSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINghdiAGIKRGHV---PYL------ 77
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVGYLpqePQLdptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGMIFQSHHLLMDR--SVFDNVALP------LVIEGFTLGEIrkrvagaLDMVGLYGKERHNPI------------- 136
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRfnEISAKYAEPdadfdkLAAEQAELQEI-------IDAADAWDLDSQLEIamdalrcppwdad 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 137 --MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKlSMDIL-RLFETFndAGTsVLIATHD 196
Cdd:TIGR03719 159 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVAWLeRHLQEY--PGT-VVAVTHD 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-170 |
2.92e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKIYAGgQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLrrDIGMIF 85
Cdd:PRK15439 16 SISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GIYLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 QSHHLLMDRSVFDNVALPLVIEGFTLgeirKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:PRK15439 93 QEPLLFPNLSVKENILFGLPKRQASM----QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
....*
gi 640581988 166 GNLDP 170
Cdd:PRK15439 169 ASLTP 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-216 |
3.05e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 10 IYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDIGMIFQSH 88
Cdd:PRK10789 322 TYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 HLLMDrSVFDNVAL--PlvieGFTLGEIRK--RVA-----------GALDMVGLYGkerhnpIMLSGGEQQRVGIARAIV 153
Cdd:PRK10789 399 FLFSD-TVANNIALgrP----DATQQEIEHvaRLAsvhddilrlpqGYDTEVGERG------VMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 154 NKPPLLLADEPTGNLDPKLSMDILRLFETFNDaGTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEAS-EILVMQHGHIA 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-228 |
3.80e-11 |
|
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: 62.15 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASA--GRVWINGHDIAGikRGHVPYLRRDIGMIFQSHHL 90
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKA--SNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 91 LMDRSVFDNVAL--PLVIEGFTL--GEIRKRVAGALDMVGLYGKERHNPIM-LSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:TIGR02633 90 VPELSVAENIFLgnEITLPGGRMayNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640581988 166 GNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggeelGTSPMSA 228
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV-----ATKDMST 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-216 |
4.64e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLK-LITVIERAS-AGRVWING-----HDI-----AGIKRGH-----VP 75
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKvLSGVYPHGSyEGEILFDGevcrfKDIrdseaLGIVIIHqelalIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLrrDIGM-IF----QSHHLLMDRSvfdnvalplviegftlgEIRKRVAGALDMVGLygkeRHNPIMLSG----GEQQRV 146
Cdd:NF040905 92 YL--SIAEnIFlgneRAKRGVIDWN-----------------ETNRRARELLAKVGL----DESPDTLVTdigvGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 147 GIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAG-TSVLIaTHDLGLIARMKYRTLTLKQGRMI 216
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIII-SHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-215 |
4.67e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 4 FEqVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA------GIKRG--HVP 75
Cdd:PRK09700 266 FE-VRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGmaYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 YLRRDIGmifqshhLLMDRSVFDNVALPLVIE----GFTLGEI-----RKRVAGALDMVGLYGKE-RHNPIMLSGGEQQR 145
Cdd:PRK09700 345 ESRRDNG-------FFPNFSIAQNMAISRSLKdggyKGAMGLFhevdeQRTAENQRELLALKCHSvNQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 146 VGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRM 215
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-196 |
4.69e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInGHDIagikrghvpylrrDI 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSH-HLLMDRSVFDNVAlplviEGFTLGEIRKRVAGALDMVGLY---GKERHNPI-MLSGGEQQRVGIARAIVNKP 156
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEIS-----GGLDIIKLGKREIPSRAYVGRFnfkGSDQQKKVgQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 157 PLLLADEPTGNLDpklsMDILRLFET--FNDAGTSVLIaTHD 196
Cdd:TIGR03719 463 NVLLLDEPTNDLD----VETLRALEEalLNFAGCAVVI-SHD 499
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-217 |
7.07e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA------GIKRGHV--PYLRRDIGmIF 85
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGIMlcPEDRKAEG-II 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 QSHhllmdrSVFDNVA-------LPLvieGFTLGEIRKRVAGALDMVGLYGK--ERHNPIM-LSGGEQQRVGIARAIVNK 155
Cdd:PRK11288 344 PVH------SVADNINisarrhhLRA---GCLINNRWEAENADRFIRSLNIKtpSREQLIMnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-196 |
8.00e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpyLRRDI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 82 GMIFQSHHLlmdrsvFDNVALPlviEGFTLGEirKRVAGALDMVGLYGKERHNP-----IMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK10522 400 SAVFTDFHL------FDQLLGP---EGKPANP--ALVEKWLERLKMAHKLELEDgrisnLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 157 PLLLADEPTGNLDPKLSMDILR-LFETFNDAGTSVLIATHD 196
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHD 509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-170 |
8.12e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEM-AFLtGHSGAGKSTLLKLITVIERASAGRVW-----INGHDIAgikrghvpyLRRDIGMIFQSHHL 90
Cdd:NF033858 281 AVDHVSFRIRRGEIfGFL-GSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIA---------TRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 91 LMDRSVFDNVAL--PLviegFTLG--EIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:NF033858 351 YGELTVRQNLELhaRL----FHLPaaEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
....
gi 640581988 167 NLDP 170
Cdd:NF033858 427 GVDP 430
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-195 |
1.02e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 8 SKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIeRASAGRVWINGHDIAGIKrghVPYLRRDIGMIFQS 87
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 --------------HHLLMDRSVF---DNVALPLVIEGFtlgeirkrvAGALDMVGLYGKerhnpIMLSGGEQQRVGIAR 150
Cdd:TIGR01271 1301 vfifsgtfrknldpYEQWSDEEIWkvaEEVGLKSVIEQF---------PDKLDFVLVDGG-----YVLSNGHKQLMCLAR 1366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 151 AIVNKPPLLLADEPTGNLDPkLSMDILR--LFETFNDAgtSVLIATH 195
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDP-VTLQIIRktLKQSFSNC--TVILSEH 1410
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-171 |
1.17e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 20 DVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINghDIAGIKRGHVPYLRRDIGMIFQSHhLLMDRSVFDN 99
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDP-LLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 100 VALPLVI-------------EGFTLGE-------IRKRVAGALDMVG--------LYGKERHNPI--------------- 136
Cdd:PTZ00265 480 IKYSLYSlkdlealsnyyneDGNDSQEnknkrnsCRAKCAGDLNDMSnttdsnelIEMRKNYQTIkdsevvdvskkvlih 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 137 -------------------MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPK 171
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-170 |
1.23e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLIT----------VI----ERASAGRVWinghDIagikrghvpylRRDIGM 83
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndLTlfgrRRGSGETIW----DI-----------KKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 84 IFQSHHllMDRSVFDNVaLPLVIEGF--TLG-------EIRKRVAGALDMVGLYGKERHNPIM-LSGGEQQRVGIARAIV 153
Cdd:PRK10938 341 VSSSLH--LDYRVSTSV-RNVILSGFfdSIGiyqavsdRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALV 417
|
170
....*....|....*..
gi 640581988 154 NKPPLLLADEPTGNLDP 170
Cdd:PRK10938 418 KHPTLLILDEPLQGLDP 434
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-217 |
1.39e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGEMAFLTGHSGAGKSTLLK-LITVIERASAGRVWINGHDIA------GIKRG--HVPYLRRDIGMIfq 86
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKirnpqqAIAQGiaMVPEDRKRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 87 shhLLMDrsVFDNVALPlVIEGFTLGEiRKRVAGALDMVGLYGKERH----NPIM----LSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13549 354 ---PVMG--VGKNITLA-ALDRFTGGS-RIDDAAELKTILESIQRLKvktaSPELaiarLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-195 |
1.56e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 15 QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIagikrghvpylrrdigmifqshHLLMDR 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN----------------------QFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 95 SVFDNVALplviegftLGEIrKRVAGALDMVGL-----YgkeRHNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:COG2401 101 SLIDAIGR--------KGDF-KDAVELLNAVGLsdavlW---LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*..
gi 640581988 170 PKLSMDILRLFETF-NDAGTSVLIATH 195
Cdd:COG2401 169 RQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-202 |
5.00e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 4 FEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA--GIKRghvpyLRRD 80
Cdd:PTZ00243 1311 FEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGayGLRE-----LRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQShHLLMDRSVFDNValplviEGFtLGEIRKRVAGALDMVGLYGK-----ERHNPIMLSGGEQQRVG------IA 149
Cdd:PTZ00243 1386 FSMIPQD-PVLFDGTVRQNV------DPF-LEASSAEVWAALELVGLRERvasesEGIDSRVLEGGSNYSVGqrqlmcMA 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 640581988 150 RAIVNK-PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIAtHDLGLIAR 202
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIA-HRLHTVAQ 1510
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-216 |
5.81e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIeRASAGRVWINGHDIAGIKRGHvpyLRRDIGMIFQSHHLLmD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPES---WRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFDNVALP----------LVIEGFTLGEIRKRVAGALD-MVGlygkerHNPIMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK11174 437 GTLRDNVLLGnpdasdeqlqQALENAWVSEFLPLLPQGLDtPIG------DQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 163 EPTGNLDPKLSMDILrlfETFNDA--GTSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PRK11174 511 EPTASLDAHSEQLVM---QALNAAsrRQTTLMVTHQLEDLAQWD-QIWVMQDGQIV 562
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-227 |
7.98e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASA--GRVWINGHDI--AGIKRGHvpylRRDIGMIFQSH 88
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqaSNIRDTE----RAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 89 HLLMDRSVFDNValplviegFTLGEIRKrvAGALDMVGLYGKER------------HNPIM-LSGGEQQRVGIARAIVNK 155
Cdd:PRK13549 92 ALVKELSVLENI--------FLGNEITP--GGIMDYDAMYLRAQkllaqlkldinpATPVGnLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIggeelGTSPMS 227
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI-----GTRPAA 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
1.10e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSkiYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVPYLRRD 80
Cdd:PRK13541 1 MLSLHQLQ--FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGmifqshhLLMDRSVFDNvaLPLVIEGFTLGEIrkrVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK13541 79 LG-------LKLEMTVFEN--LKFWSEIYNSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 640581988 161 ADEPTGNLDpKLSMDIL-RLFETFNDAGTSVLIATH 195
Cdd:PRK13541 147 LDEVETNLS-KENRDLLnNLIVMKANSGGIVLLSSH 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-197 |
1.15e-09 |
|
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: 56.79 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKlitvierASAGRVWINGH-DIAGIKRGHVPY--LRRDIGMIFQ--- 86
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS-------AFLRLLNTEGDiQIDGVSWNSVPLqkWRKAFGVIPQkvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 87 --SHHLLMDRS------------VFDNVALPLVIEGFtlgeirkrvAGALDMVGLYGKerhnpIMLSGGEQQRVGIARAI 152
Cdd:cd03289 88 ifSGTFRKNLDpygkwsdeeiwkVAEEVGLKSVIEQF---------PGQLDFVLVDGG-----CVLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 153 VNKPPLLLADEPTGNLDPkLSMDILR--LFETFndAGTSVLIATHDL 197
Cdd:cd03289 154 LSKAKILLLDEPSAHLDP-ITYQVIRktLKQAF--ADCTVILSEHRI 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-193 |
1.27e-09 |
|
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: 56.12 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVI--ERAS-AGRVWINGHDIAGIKRGHvpylRRDIGMIFQSHHllmdr 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYNGIPYKEFAEKY----PGEIIYVSEEDV----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 95 svfdNVALPLVIEgfTLgEIRKRVAGAlDMV-GlygkerhnpimLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLS 173
Cdd:cd03233 94 ----HFPTLTVRE--TL-DFALRCKGN-EFVrG-----------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180
....*....|....*....|.
gi 640581988 174 MDILRLFETFNDA-GTSVLIA 193
Cdd:cd03233 155 LEILKCIRTMADVlKTTTFVS 175
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-193 |
1.44e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITV----IERASAGRVWINGHDIAGIK---RG----------HVPYLRRD 80
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKkhyRGdvvynaetdvHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIF-------QSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGAlDMV-GlygkerhnpimLSGGEQQRVGIARAI 152
Cdd:TIGR00956 157 ETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGN-DFVrG-----------VSGGERKRVSIAEAS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILR-LFETFNDAGTSVLIA 193
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRaLKTSANILDTTPLVA 266
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-90 |
1.90e-09 |
|
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: 57.12 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK----ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHvpYl 77
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA--Y- 404
|
90
....*....|...
gi 640581988 78 RRDIGMIFQSHHL 90
Cdd:COG4615 405 RQLFSAVFSDFHL 417
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-197 |
2.00e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQK-ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGikrgHVPYLRR 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSH---HLLMDRsvfDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKP 156
Cdd:TIGR01257 2013 NMGYCPQFDaidDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 640581988 157 PLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-196 |
3.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRfeqVSKIYAGGQKALSDVSfhlqrgeMAFLTGH-------SGAGKSTLLKLITVIERASAGRVWINghdiAGIKRGH 73
Cdd:PRK11819 9 MNR---VSKVVPPKKQILKDIS-------LSFFPGAkigvlglNGAGKSTLLRIMAGVDKEFEGEARPA----PGIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 VPylrrdigmifQSHHLLMDRSVFDNValplvIEGftLGEIRKRVA-----------------------GAL----DMVG 126
Cdd:PRK11819 75 LP----------QEPQLDPEKTVRENV-----EEG--VAEVKAALDrfneiyaayaepdadfdalaaeqGELqeiiDAAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 127 LYGKERHNPI-M--------------LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKlSMDILRLF-ETFndAGTsV 190
Cdd:PRK11819 138 AWDLDSQLEIaMdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVAWLEQFlHDY--PGT-V 213
|
....*.
gi 640581988 191 LIATHD 196
Cdd:PRK11819 214 VAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-213 |
4.34e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKrghVPYLRRDIGMIFQ-----SHHLLM 92
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQdpvlfSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 93 DRSVFDNVALPLVIEGFTLGEIRKRVAG---ALDMVGLYGKERhnpimLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWWALELAHLKTFVSAlpdKLDHECAEGGEN-----LSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 640581988 170 PKLSMDILRLFET-FNDAgtSVLIATHDLGLIarMKY-RTLTLKQG 213
Cdd:TIGR00957 1454 LETDNLIQSTIRTqFEDC--TVLTIAHRLNTI--MDYtRVIVLDKG 1495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-216 |
6.84e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLI------TVIERASA--GRVWINGHDIAGIKrghVPYLRRDIGMIFQSHH 89
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgGGAPRGARvtGDVTLNGEPLAAID---APRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 90 LLMDRSVFDNVALPLVIEGFTLGEIRKRVAG----ALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVN---------KP 156
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640581988 157 PLLLADEPTGNLDpkLSMDiLRLFETFNDAG----TSVLIATHDLGLIARMKYRTLTLKQGRMI 216
Cdd:PRK13547 174 RYLLLDEPTAALD--LAHQ-HRLLDTVRRLArdwnLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-177 |
7.53e-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: 55.30 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVwinghdiagikrghvpylrRDIGMIFQSHHL--LMDRS 95
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------------KHSGRISFSPQTswIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 96 VFDNvalplVIEGFTLGEIRKR-VAGALDM---VGLYGKERHNPIM-----LSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:TIGR01271 503 IKDN-----IIFGLSYDEYRYTsVIKACQLeedIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|.
gi 640581988 167 NLDPKLSMDIL 177
Cdd:TIGR01271 578 HLDVVTEKEIF 588
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-216 |
7.83e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgiKRGhVPYLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFG-LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DIGMIFQSHHLLMDRSVF--------DNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERhnpimLSGGEQQRVGIARA 151
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFnidpfsehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN-----FSVGQRQLLSLARA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 152 IVNKPPLLLADEPTGNLDPKLSMDILR-LFETFNDAgtSVLIATHDLGLIARMKyRTLTLKQGRMI 216
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRtIREEFKSC--TMLVIAHRLNTIIDCD-KILVLSSGQVL 1448
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-202 |
9.34e-09 |
|
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: 53.63 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQ----KALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHdIAgikrgHVPyl 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA-----YVS-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 rrdigmifQSHhLLMDRSVFDNV--ALPL-------VIEGFTLGE-IRKRVAGALDMVGLYGkerhnpIMLSGGEQQRVG 147
Cdd:cd03250 73 --------QEP-WIQNGTIRENIlfGKPFdeeryekVIKACALEPdLEILPDGDLTEIGEKG------INLSGGQKQRIS 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 148 IARAIVNKPPLLLADEPTGNLDPKLSMDILR--LFETFNDAGTsVLIATHDLGLIAR 202
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT-RILVTHQLQLLPH 193
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-214 |
1.34e-08 |
|
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: 54.37 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINghdiagiKRGHV------ 74
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-------AKGKLfyvpqr 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 75 PY-----LRRDIgmIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRvAGALDMVGLYGKErhnpimLSGGEQQRVGIA 149
Cdd:TIGR00954 524 PYmtlgtLRDQI--IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDV------LSGGEKQRIAMA 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 150 RAIVNKPPLLLADEPTGNLDPKLSMdilRLFETFNDAGTSVLIATHDLGLIarmKYRTLTLKQGR 214
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSHRKSLW---KYHEYLLYMDG 653
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-197 |
1.57e-08 |
|
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: 53.10 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 11 YAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRV-WINGHDIAGIKRGHVPYLRRDIGMIFQSHH 89
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 90 LLmDRSVFDNVAL---------PLVIEGFTLG-EIRKRVAGALDMVGLYGkerhnpIMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03290 90 LL-NATVEENITFgspfnkqryKAVTDACSLQpDIDLLPFGDQTEIGERG------INLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 640581988 160 LADEPTGNLDPKLSMDILR--LFETFNDAGTSVLIATHDL 197
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-226 |
1.74e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 7 VSKIYAGgQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAGIKRGHVpyLRRDIGMIFQ 86
Cdd:PRK10982 4 ISKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 87 SHHLLMDRSVFDNVAL---PLviEGFTL--GEIRKRVAGALDMVGLYGKERHNPIMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgryPT--KGMFVdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 162 DEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIGGEELGTSPM 226
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTM 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-201 |
3.71e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGH-DIAGIKRGHVPylrr 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVD---- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 diGMIFQSHHLLMDRSVFdnvalPLVIEgftlgeirKRVAGALDMVGLYGKERHNPI-MLSGGEQQRVGIARAIVNKPPL 158
Cdd:PLN03073 584 --GLDLSSNPLLYMMRCF-----PGVPE--------QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640581988 159 LLADEPTGNLDPKLSMDILRLFETFNDAgtsVLIATHDLGLIA 201
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDEHLIS 688
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-221 |
3.87e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 52.38 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 13 GGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIE--RASAGRVWINGHDIAGI------KRGhvpylrrdIGMI 84
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELspderaRAG--------IFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 85 FQS---------HHLLmdRSVFDNVALPLViegfTLGEIRKRVAGALDMVGLygkerhNPIML--------SGGEQQRVG 147
Cdd:COG0396 83 FQYpveipgvsvSNFL--RTALNARRGEEL----SAREFLKLLKEKMKELGL------DEDFLdryvnegfSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 148 IARAIVNKPPLLLADEPTGNLDpklsMDILRL----FETFNDAGTSVLIATHDLGLIarmKY----RTLTLKQGRMI--G 217
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD----IDALRIvaegVNKLRSPDRGILIITHYQRIL---DYikpdFVHVLVDGRIVksG 223
|
....
gi 640581988 218 GEEL 221
Cdd:COG0396 224 GKEL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-168 |
5.06e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA--GIKRGHvpylRRDIGMIFQSHHLL 91
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQ----EAGIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNValplviegFTLGEIRKRVaGALDMVGLYGKE---------RHNPIMLSG----GEQQRVGIARAIVNKPPL 158
Cdd:PRK10762 92 PQLTIAENI--------FLGREFVNRF-GRIDWKKMYAEAdkllarlnlRFSSDKLVGelsiGEQQMVEIAKVLSFESKV 162
|
170
....*....|
gi 640581988 159 LLADEPTGNL 168
Cdd:PRK10762 163 IIMDEPTDAL 172
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-169 |
6.45e-08 |
|
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: 51.78 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 14 GQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVwinghdiagikrghvpylrRDIGMIFQSHHL--L 91
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------------KHSGRISFSSQFswI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDRSVFDNvalplVIEGFTLGEIR-KRVAGALDMVGLYGK--ERHNPIM------LSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:cd03291 110 MPGTIKEN-----IIFGVSYDEYRyKSVVKACQLEEDITKfpEKDNTVLgeggitLSGGQRARISLARAVYKDADLYLLD 184
|
....*..
gi 640581988 163 EPTGNLD 169
Cdd:cd03291 185 SPFGYLD 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
7.62e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInghdiaG--IKRGHVpylrr 79
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GetVKLAYV----- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 80 DigmifQSH-HLLMDRSVFDNvalplviegftlgeirkrVAGALDMVGLYGKE--------RHN--------PI-MLSGG 141
Cdd:PRK11819 393 D-----QSRdALDPNKTVWEE------------------ISGGLDIIKVGNREipsrayvgRFNfkggdqqkKVgVLSGG 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 142 EQQRVGIARAIVNKPPLLLADEPTGNLDpklsMDILRLFET--FNDAGTSVLIaTHD 196
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEalLEFPGCAVVI-SHD 501
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-200 |
1.36e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVSKIYaGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLItvierasAGRVWINGHDIA---GIKRGHvpyl 77
Cdd:PRK10636 312 LLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVSGEIGlakGIKLGY---- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 rrdigmiFQSHHLLM---DRSVFDNVA--LPLVIEgftlGEIRKRVAGaldmVGLYGKERHNPI-MLSGGEQQRVGIARA 151
Cdd:PRK10636 380 -------FAQHQLEFlraDESPLQHLArlAPQELE----QKLRDYLGG----FGFQGDKVTEETrRFSGGEKARLVLALI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 640581988 152 IVNKPPLLLADEPTGNLDpkLSMDiLRLFETFNDAGTSVLIATHDLGLI 200
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLD--LDMR-QALTEALIDFEGALVVVSHDRHLL 490
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-197 |
1.89e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGGQK-------------------ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVwin 62
Cdd:PRK13545 5 VKFEHVTKKYKMYNKpfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 63 ghDIAGikrghvpylrrDIGMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPI-MLSGG 141
Cdd:PRK13545 82 --DIKG-----------SAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADI-GKFIYQPVkTYSSG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 142 EQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-202 |
2.24e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 79 RDIGMIFQSHHLLMDRSVFDNVALPLviEGFTLGEIrKRVA--GALDM------------VGLYGKErhnpimLSGGEQQ 144
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGK--EDATREDV-KRACkfAAIDEfieslpnkydtnVGPYGKS------LSGGQKQ 1365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 145 RVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFND-AGTSVLIATHDLGLIAR 202
Cdd:PTZ00265 1366 RIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKR 1424
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-214 |
3.65e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLKlitvierASAGRvwINGHDIAGI-----KRGHVPYLRRdIGMIFQSHHL-- 90
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLN-------ALAGR--IQGNNFTGTilannRKPTKQILKR-TGFVTQDDILyp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 91 -LMDRSVFDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKErhNPIM-------LSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PLN03211 154 hLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCE--NTIIgnsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640581988 163 EPTGNLDPKLSMDILRLFETFNDAGTSVLIATHD-LGLIARMKYRTLTLKQGR 214
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
138-197 |
3.85e-07 |
|
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: 49.29 E-value: 3.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-195 |
7.55e-07 |
|
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: 48.01 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLL------KLITVIErasaGRVWINGhdiagikRGHVPYLRRDIGMIFQshhll 91
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLdvlagrKTAGVIT----GEILING-------RPLDKNFQRSTGYVEQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 92 MDrsvfdnVALPL--VIEGFTLGeirkrvagALdmvgLYGkerhnpimLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03232 87 QD------VHSPNltVREALRFS--------AL----LRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 640581988 170 PKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-215 |
2.81e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 3 RFEQVSKiyaggqKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWInghdiagikrghvpylRRDIG 82
Cdd:PTZ00243 667 FFELEPK------VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA----------------ERSIA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 83 MIFQsHHLLMDRSVFDNVA---------LPLVIEGFTLGEIRKRVAGALDM-VGLYGkerhnpIMLSGGEQQRVGIARAI 152
Cdd:PTZ00243 725 YVPQ-QAWIMNATVRGNILffdeedaarLADAVRVSQLEADLAQLGGGLETeIGEKG------VNLSGGQKARVSLARAV 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640581988 153 VNKPPLLLADEPTGNLDPKLSMDILRlfETFND--AGTSVLIATHDLGLIARMKYrTLTLKQGRM 215
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHVGERVVE--ECFLGalAGKTRVLATHQVHVVPRADY-VVALGDGRV 859
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
139-230 |
3.34e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 139 SGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMI-- 216
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIad 225
|
90 100
....*....|....*....|....
gi 640581988 217 ----------GGEELGTSPMSAKE 230
Cdd:NF000106 226 gkvdelktkvGGRTLQIRPAHAAE 249
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-201 |
4.47e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 4.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 138 LSGGEQQRVGIARAIVNKPP---LLLADEPTGNLDPKlsmDILRLFETFN---DAGTSVLIATHDLGLIA 201
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFH---DVKKLLEVLQrlvDKGNTVVVIEHNLDVIK 236
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
138-201 |
5.51e-06 |
|
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: 46.23 E-value: 5.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 138 LSGGEQQ---RVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIA 201
Cdd:pfam13304 237 LSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-196 |
6.62e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 1 MIRFEQVsKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRV---------WINgHDIAGIKR 71
Cdd:PRK10636 1 MIVFSSL-QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVN-QETPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 72 GHVPYL---RRDIGMIFQSHHLLMDRSvfDNVALPLV------IEGFTlgeIRKRVAGALDMVGLYGKERHNPIM-LSGG 141
Cdd:PRK10636 79 PALEYVidgDREYRQLEAQLHDANERN--DGHAIATIhgkldaIDAWT---IRSRAASLLHGLGFSNEQLERPVSdFSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 142 EQQRVGIARAIVNKPPLLLADEPTGNLDpklsMDILRLFETF--NDAGTSVLIaTHD 196
Cdd:PRK10636 154 WRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWlkSYQGTLILI-SHD 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-195 |
6.90e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 9 KIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKliTVIERASAGRV-----WINGHDI-AGIKRG---------H 73
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN--VLAERVTTGVItggdrLVNGRPLdSSFQRSigyvqqqdlH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 74 VPYLRRDIGMIFqSHHLLMDRSVFDNVALPLVIEGFTLGEIRKrVAGALdmVGLYGkerhnpIMLSGGEQQRVGIARAIV 153
Cdd:TIGR00956 848 LPTSTVRESLRF-SAYLRQPKSVSKSEKMEYVEEVIKLLEMES-YADAV--VGVPG------EGLNVEQRKRLTIGVELV 917
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 640581988 154 NKPPLLL-ADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
138-197 |
1.10e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDL 197
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-169 |
1.44e-05 |
|
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: 44.71 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 22 SFHLQ-------RGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA----GIK---RGHVPYLRRDIGMIFQS 87
Cdd:cd03237 12 EFTLEveggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKadyEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 88 HhllmdrSVFDN-VALPLVIEGftlgeirkrvagaldmvgLYGKERHNpimLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:cd03237 92 H------PYFKTeIAKPLQIEQ------------------ILDREVPE---LSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
...
gi 640581988 167 NLD 169
Cdd:cd03237 145 YLD 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-217 |
1.45e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIA------GIKRGH--VPYL 77
Cdd:PRK10982 252 EVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneAINHGFalVTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 78 RRDIGmIFQSHHLLMDrSVFDNVALPLVIEGF-TLGEIRKRVAGALDMVGLYGKERHNPI-MLSGGEQQRVGIARAIVNK 155
Cdd:PRK10982 332 RRSTG-IYAYLDIGFN-SLISNIRNYKNKVGLlDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640581988 156 PPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIARMKYRTLTLKQGRMIG 217
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-200 |
1.49e-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: 43.85 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 6 QVSKIYaggQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKliTVIERASAGRVwinghdIAGIKRghvpYLRRDIGMIF 85
Cdd:cd03238 2 TVSGAN---VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL------ISFLPK----FSRNKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 86 QshhllmdrsvfdnvaLPLVIEgftlgeirkrvagaldmVGLyGKERHNPIM--LSGGEQQRVGIARAIVNKPP--LLLA 161
Cdd:cd03238 67 Q---------------LQFLID-----------------VGL-GYLTLGQKLstLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 640581988 162 DEPTGNLDPKlsmDILRLFETFN---DAGTSVLIATHDLGLI 200
Cdd:cd03238 114 DEPSTGLHQQ---DINQLLEVIKgliDLGNTVILIEHNLDVL 152
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-169 |
5.50e-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: 42.97 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTL----LKLITVIErasaGRVWINGHDIAGIKrghVPYLRRDIGMIFQSHHLLMD 93
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---LHTLRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 94 RSVFD--------NVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERhnpimLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:cd03288 110 SIRFNldpeckctDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
....
gi 640581988 166 GNLD 169
Cdd:cd03288 185 ASID 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-169 |
6.47e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSKIYAGG-QKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGHDIAgiKRGhVPYLRRD 80
Cdd:PLN03130 1238 IKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFG-LMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 81 IGMIFQSHHLLMDRSVFD--------NVALPLVIEGFTLGEIRKRVAGALDMVGLYGKERhnpimLSGGEQQRVGIARAI 152
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNldpfnehnDADLWESLERAHLKDVIRRNSLGLDAEVSEAGEN-----FSVGQRQLLSLARAL 1389
|
170
....*....|....*..
gi 640581988 153 VNKPPLLLADEPTGNLD 169
Cdd:PLN03130 1390 LRRSKILVLDEATAAVD 1406
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-200 |
6.74e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 6.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 136 IMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGT-SVLIATHDLGLI 200
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL 135
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-198 |
7.94e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 17 ALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVIERASAGRVWINGhdiagikrghvpylrrDIGMIFQSHHLLMDRSV 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLyGKERHNPIM-LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMD 175
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180
....*....|....*....|...
gi 640581988 176 ILRLFETFNDAGTSVLIATHDLG 198
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLG 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
101-197 |
2.70e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 101 ALPLVIEGfTLGEIRKRV--AGALDMVglygKERHN--PIM------LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK13409 171 LIPKVFKG-KVRELLKKVdeRGKLDEV----VERLGleNILdrdiseLSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
90 100
....*....|....*....|....*..
gi 640581988 171 KLSMDILRLFETFNDaGTSVLIATHDL 197
Cdd:PRK13409 246 RQRLNVARLIRELAE-GKYVLVVEHDL 271
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-200 |
3.01e-04 |
|
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: 40.70 E-value: 3.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 138 LSGGEQQRVGIARAIVNKPP--LLLADEPTGNLDPKlsmDILRLFETFN---DAGTSVLIATHDLGLI 200
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPR---DNDRLIETLKrlrDLGNTVLVVEHDEDTI 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-169 |
4.04e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 2 IRFEQVSkIYAGGQKALSDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVierasagrvwingHDIAGIKRG----HVP-- 75
Cdd:PLN03073 178 IHMENFS-ISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAM-------------HAIDGIPKNcqilHVEqe 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 76 -----------YLRRDI---GMIFQSHHLLMDRSVFDNVALPLVIEGFTLGEIRKRVAGA--------LDMVGLYGKE-R 132
Cdd:PLN03073 244 vvgddttalqcVLNTDIertQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQrleeiykrLELIDAYTAEaR 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 640581988 133 HNPIM----------------LSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PLN03073 324 AASILaglsftpemqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-205 |
4.10e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 33 LTGHSGAGKSTLLKLITVIerasagrvwINGHDIAGIKRG-HVPYLRR------DIGMIFQS-----HHLLMDRSVFDNV 100
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYA---------LTGELPPNSKGGaHDPKLIRegevraQVKLAFENangkkYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 101 AlplviegFT-LGEIRKRVagaLDMVGLygkerhnpimLSGGEQQ------RVGIARAIVNKPPLLLADEPTGNLDP-KL 172
Cdd:cd03240 98 I-------FChQGESNWPL---LDMRGR----------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNI 157
|
170 180 190
....*....|....*....|....*....|....
gi 640581988 173 SMDILRLFETFN-DAGTSVLIATHDLGLIARMKY 205
Cdd:cd03240 158 EESLAEIIEERKsQKNFQLIVITHDEELVDAADH 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-200 |
4.25e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 125 VGL-YGKERHNPIMLSGGEQQRVGIARAIVNK---PPLLLADEPTGNL---DPKLSMDIL-RLFetfnDAGTSVLIATHD 196
Cdd:TIGR00630 816 VGLgYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLqRLV----DKGNTVVVIEHN 891
|
....
gi 640581988 197 LGLI 200
Cdd:TIGR00630 892 LDVI 895
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-202 |
7.41e-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: 7.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 138 LSGGEQQRVGIARAI----VNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATHDLGLIAR 202
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAEL 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-219 |
7.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 18 LSDVSFHLQRGEMAFLTGHSGAGKSTLLK-LITVIERASAGRVWInghdiagikRGHVPYLRRdIGMIFQShhllmdrSV 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI---------RGSVAYVPQ-VSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 97 FDNVALPLVIEGFTLGEIRKRVAGALDMVGLYGKER----HNPIMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKL 172
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 640581988 173 SMDILRLFETFNDAGTSVLIATHDLGLIARMKyRTLTLKQGrMIGGE 219
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMD-RIILVSEG-MIKEE 820
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
138-200 |
1.14e-03 |
|
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: 39.38 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----KLSMDILRLFETFndaGTSVLIATHDLGLI 200
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAENR---GKTAMVVDHDIYLI 519
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-200 |
1.75e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640581988 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----KLSMDILRLFETfNDAgtSVLIATHDLGLI 200
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRIAEE-REA--TALVVDHDIYMI 517
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
131-196 |
1.76e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640581988 131 ERHNPIM--LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDpklsMDILR-LFETFNDAGTSVLIATHD 196
Cdd:PRK15064 147 EQHYGLMseVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----INTIRwLEDVLNERNSTMIIISHD 211
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-195 |
1.78e-03 |
|
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: 38.83 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 16 KALSDVSFHLQRGeMAFLTGHSGAGKSTLLKLITVIERASAGRVwINGHDIAGIKRGHVPYLRrdIGMIFQSH-HLLMDR 94
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRK-FDEEDFYLGDDPDLPEIE--IELTFGSLlSRLLRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 95 SVFDNVALPLVIEGFTL-GEIRKRVAGALDMVGLYGKERHNP--------------------IMLSGGEQQRV-----GI 148
Cdd:COG3593 88 LLKEEDKEELEEALEELnEELKEALKALNELLSEYLKELLDGldlelelsldeledllkslsLRIEDGKELPLdrlgsGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 149 ARAIV-------------NKPPLLLADEPTGNLDPKLSMDILRLFETFNDAGTSVLIATH 195
Cdd:COG3593 168 QRLILlallsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
137-200 |
2.14e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 2.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640581988 137 MLSGGEQQRVGIARAIVN---KPPLLLADEPTGNLDPKLSMDILRLF-ETFNDAGTSVLIATHDLGLI 200
Cdd:COG1106 202 EESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFlDLANKNNAQLIFTTHSTELL 269
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-200 |
4.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 4.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640581988 138 LSGGEQQRVGIARAIV---NKPPLLLADEPT-GnldpkLSM-DILRLFETFN---DAGTSVLIATHDLGLI 200
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTtG-----LHFhDIRKLLEVLHrlvDKGNTVVVIEHNLDVI 892
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-51 |
6.16e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 6.16e-03
10 20 30
....*....|....*....|....*....|...
gi 640581988 19 SDVSFHLQRGEMAFLTGHSGAGKSTLLKLITVI 51
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-192 |
7.62e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 36.92 E-value: 7.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 640581988 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPKLSMDILRLFETFNDAG-TSVLI 192
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGiTLVLV 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
111-196 |
9.54e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 36.91 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640581988 111 LGEIRKRVAGALDmVGL-YGKERHNPIMLSGGEQQRVGIARAI------VnkppLLLADEPTGNLDPKlsmDILRLFET- 182
Cdd:TIGR00630 462 LKEIRERLGFLID-VGLdYLSLSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQR---DNRRLINTl 533
|
90
....*....|....*.
gi 640581988 183 --FNDAGTSVLIATHD 196
Cdd:TIGR00630 534 krLRDLGNTLIVVEHD 549
|
|
| |
