|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
2.53e-140 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 391.72 E-value: 2.53e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:COG2884 1 MIRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQRGV 224
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-215 |
8.78e-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: 296.47 E-value: 8.78e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:TIGR02673 1 MIEFHNVSKAY-PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-216 |
3.04e-101 |
|
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: 292.39 E-value: 3.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQV 81
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
1.21e-89 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 263.44 E-value: 1.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKS--SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:COG1136 4 LLELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 R-QVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMrQRVVELSLGRLVRDEQ 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELAARA-DRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-216 |
7.14e-86 |
|
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: 253.57 E-value: 7.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSAR--PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLR 79
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 -QVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVdSMRQRVVELSLGRL 216
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
9.61e-84 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 252.31 E-value: 9.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
1.43e-78 |
|
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: 235.55 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSAR--PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
5.80e-74 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 224.97 E-value: 5.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQY--KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHVPKL 78
Cdd:COG1116 7 ALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV--------DGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHD 197
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
3.29e-71 |
|
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: 216.92 E-value: 3.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSK---FHVN-----KL 70
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlFALDedaraRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 71 RGRHVpklrqviGCVFQDFRLLQQKTVYDNVAFALEVIGKRtDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIA 150
Cdd:COG4181 88 RARHV-------GFVFQSFQLLPTLTALENVMLPLELAGRR-DARARAR-ALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDsmR-QRVVELSLGRLVRDEQ 221
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA--RcDRVLRLRAGRLVEDTA 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.43e-70 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 215.69 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:COG3638 2 MLELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVafaleVIGK--------------RTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQR 146
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNV-----LAGRlgrtstwrsllglfPPEDRERAL-EALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 147 VAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDhhiVDSMRQ---RVVELSLGRLVRD 219
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQ---VDLARRyadRIIGLRDGRVVFD 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-225 |
2.87e-70 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 218.13 E-value: 2.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:PRK11153 1 MIELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVrdEQRGVY 225
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV--EQGTVS 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
3.76e-69 |
|
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: 211.42 E-value: 3.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgRHVPKLRQV 81
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQD-----FRllqqKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:COG1122 77 VGLVFQNpddqlFA----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-212 |
1.71e-68 |
|
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: 209.64 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQY--KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHVPKLR 79
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV--------DGEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDhhiVD---SMRQRVVELS 212
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHD---IDeavFLADRVVVLS 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-217 |
2.00e-68 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 209.35 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:PRK10908 1 MIRFEHVSKAYLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-215 |
3.27e-67 |
|
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: 205.78 E-value: 3.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhVPKLRQVIG 83
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQDFRL-LQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
1.10e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 204.18 E-value: 1.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV----P 76
Cdd:COG3842 5 ALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL--------LDGRDVtglpP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQvIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:COG3842 75 EKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-219 |
1.10e-63 |
|
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: 198.18 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQV 81
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFA-------LEVIGKRTDAINRVVP-EVLETVGLSGKANRLPDELSGGEQQRVAIARAF 153
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGrlgrrstWRSLFGLFPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-197 |
4.17e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 196.37 E-value: 4.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNkLRGRHVPKLRQ 80
Cdd:COG1126 1 MIEIENLHKSFGD--LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRT--DAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSkaEAEERAM-ELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHE 195
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-219 |
7.11e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 195.67 E-value: 7.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklrGRHVPKLRQV 81
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-217 |
1.05e-62 |
|
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: 194.66 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQV 81
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-----GVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-217 |
2.07e-60 |
|
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: 189.37 E-value: 2.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQV 81
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKeLGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-217 |
7.50e-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: 7.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:COG1127 5 MIEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAeIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-197 |
1.30e-59 |
|
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: 186.58 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlRGRHVPKLRQV 81
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFAL-EVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
7.47e-59 |
|
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: 185.40 E-value: 7.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQV 81
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-197 |
1.46e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 188.36 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvPKLRQ 80
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP----PKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 vIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:COG3839 77 -IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15610239 161 LADEPTGNLDP----ETSRDIMDLLErinRTGTTVLMATHD 197
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRLHR---RLGTTTIYVTHD 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-217 |
2.92e-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: 192.04 E-value: 2.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSAR---PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPK 77
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQD-FR-LLQQKTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAF 153
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRAeRRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
4.74e-57 |
|
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: 180.78 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQY--KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:cd03257 1 LLEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQD--FRLLQQKTVYDNVAFALEVIGKRTD--AINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAF 153
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKkeARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-211 |
9.41e-57 |
|
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: 179.35 E-value: 9.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL-RQVI 82
Cdd:TIGR03608 1 LKNISKKFGD--KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDsMRQRVVEL 211
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-219 |
1.03e-56 |
|
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: 180.19 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:TIGR02315 1 MLEVENLSKVY-PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNV--------AFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
2.45e-55 |
|
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: 174.68 E-value: 2.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRhVPKLRQV 81
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALevigkrtdainrvvpevletvglsgkanrlpdelSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
3.28e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.12 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRHVPKLRQ 80
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF--------GKPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQ------DFRLlqqkTVYDNVAFAL----EVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIA 150
Cdd:COG1121 76 RIGYVPQraevdwDFPI----TVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
5.25e-54 |
|
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: 172.44 E-value: 5.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvPKLRQv 81
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP----PKDRD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQqRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
5.37e-54 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 173.36 E-value: 5.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgRHVPKLRQ 80
Cdd:PRK09493 1 MIEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK-VDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFA-LEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-197 |
6.85e-54 |
|
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: 173.77 E-value: 6.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFhvNKLRGRHVPKLRQV 81
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL--DTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:TIGR04520 79 VGMVFQnpDNQFVGA-TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHD 196
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-219 |
1.35e-52 |
|
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: 170.71 E-value: 1.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSS---ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQdF--RLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAFVN 155
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-222 |
2.38e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.51 E-value: 2.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVRVSKFHVNKLRGRhVP 76
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVD-VL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQD---FRllqqKTVYDNVAFALEVIG-KRTDAINRVVPEVLETVGLSGKANR--LPDELSGGEQQRVAIA 150
Cdd:cd03260 78 ELRRRVGMVFQKpnpFP----GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTgTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQR 222
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
3.40e-52 |
|
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: 168.83 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSAR--PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkL 78
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFR--LLQQKTVYDNVAFALEVIGKrtDAINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAFVN 155
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQRG 223
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVA 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-201 |
5.44e-51 |
|
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: 164.63 E-value: 5.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR--HVPKLRQV 81
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IgcvfQDFRLlqqkTVYDNVAFAL----EVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:cd03235 80 D----RDFPI----SVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIV 201
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLV 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
5.97e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.79 E-value: 5.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskFHVNKLRGRHVPKLRQV 81
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV---LNGRDLFTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 iGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:COG1118 78 -GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDhhIVDSMR--QRVVELSLGRLvrdEQRG 223
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHD--QEEALElaDRVVVMNQGRI---EQVG 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-197 |
7.03e-51 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 167.19 E-value: 7.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR-----VSKFHVNKLRgRHv 75
Cdd:COG1125 1 MIEFENVTKRYPDG-TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILidgedIRDLDPVELR-RR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 76 pklrqvIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGK--ANRLPDELSGGEQQRVAIARAF 153
Cdd:COG1125 78 ------IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:COG1125 152 AADPPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTHD 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-217 |
1.41e-50 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 164.78 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKLRQV 81
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGL--SGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDhhIVDSMR--QRVVELSLGRLV 217
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD--IDEAFRlaDRIAIMKNGEIV 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
5.12e-50 |
|
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: 162.89 E-value: 5.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDV-----RVSKFHVNKlrgrhvp 76
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDATDVPVQE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 klRQViGCVFQDFRLLQQKTVYDNVAFALEVIGKRT----DAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:cd03296 74 --RNV-GFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLvrdEQRG 223
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRI---EQVG 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
5.66e-50 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 160.64 E-value: 5.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgrHVPKLRQV 81
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVafalevigkrtdainrvvpevletvglsgkanrlpdELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
2.25e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVtkQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGR-----HVP 76
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY--------LDGKplsamPPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQDFRLLQQkTVYDNVAFALEVIGKRTDAINrvVPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAFVN 155
Cdd:COG4619 71 EWRRQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRER--ALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLL-ERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLrEYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
6.05e-49 |
|
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: 167.39 E-value: 6.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAeTPTSGDVRVS-KFHVNKLRGRHVPKLR 79
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRISGEvLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFRL-LQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:COG1123 83 RRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
1.24e-48 |
|
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: 169.24 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQV 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFALEVIgkrTDAinRVVpEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLGDPDA---TDE--EII-EAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMrQRVVELSLGRLVRD-------EQRG 223
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDgtheellARKG 701
|
..
gi 15610239 224 VY 225
Cdd:COG2274 702 LY 703
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
2.54e-48 |
|
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: 156.39 E-value: 2.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQV 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVafalevigkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERInRTGTTVLMATHDHHIVDSMRqRVVELSLGR 215
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDAD-RIIVLDDGR 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-216 |
3.76e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 158.06 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLR-QVIGCVFQDFRLLQQKTV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDI 177
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 178 MDLLERIN-RTGTTVLMATHDHHIVDSMrQRVVELSLGRL 216
Cdd:PRK11629 185 FQLLGELNrLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-217 |
8.34e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.48 E-value: 8.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNkLRGRHVPK---- 77
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQDFRLLQQKTVYDNVAFA-LEVIG-KRTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVN 155
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGlSKDQALARAE-KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-197 |
1.05e-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: 157.51 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRhvpKLRQ 80
Cdd:COG1120 1 MLEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR---ELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFA----LEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHD 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
1.08e-47 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 160.88 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQV 81
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 162 ADEPTGNLDPETsRDIMDL-LERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLvrdEQRG 223
Cdd:PRK09452 168 LDESLSALDYKL-RKQMQNeLKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI---EQDG 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-217 |
3.83e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.94 E-value: 3.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVN---KLRGRHVPKL 78
Cdd:COG4161 3 IQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFA-LEVIG-KRTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEApCKVLGlSKEQAREKAM-KLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-217 |
1.01e-46 |
|
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: 154.52 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL------RQVIGCVFQDFRL 91
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL--------FDGEDITGLppheiaRLGIGRTFQIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAFALEVIGKRTDAINRVVP----------EVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03219 87 FPELTVLENVMVAAQARTGSGLLLARARReereareraeELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-220 |
1.26e-46 |
|
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: 154.63 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvPKLRQ 80
Cdd:COG4555 1 MIEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP----REARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRDE 220
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-217 |
1.24e-45 |
|
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: 159.55 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQV 81
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLA------RPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 151 RAFV-NRPLVLLaDEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMrQRVVELSLGRLV 217
Cdd:COG4987 484 RALLrDAPILLL-DEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
2.01e-45 |
|
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: 148.18 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQVIGCVFQDFRLLQQKTVY 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS---LRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 99 DNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPD----ELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
4.04e-45 |
|
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: 149.96 E-value: 4.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgRHVPKLRQV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERInRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-223 |
5.50e-45 |
|
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: 153.27 E-value: 5.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGR---HVPKL 78
Cdd:TIGR03265 5 LSIDNIRKRF--GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG--------GRditRLPPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:TIGR03265 75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 159 VLLADEPTGNLDP---ETSRDIMDLLERinRTGTTVLMATHDHHIVDSMRQRVVELSLGRLvrdEQRG 223
Cdd:TIGR03265 155 LLLLDEPLSALDArvrEHLRTEIRQLQR--RLGVTTIMVTHDQEEALSMADRIVVMNHGVI---EQVG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
5.63e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 5.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRG-----RHV 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 76 PKLRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGK--RTDAINRVvPEVLETVGLSGKANRLPDELSGGEQQRVAIARAF 153
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGepKEEATARA-RELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-197 |
9.06e-45 |
|
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: 150.49 E-value: 9.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 12 KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLR-QVIGCVFQDFR 90
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 LLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180
....*....|....*....|....*...
gi 15610239 171 PETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:cd03294 193 PLIRREMQDELLRLQAElQKTIVFITHD 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-217 |
9.57e-45 |
|
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: 156.84 E-value: 9.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQV 81
Cdd:COG4988 337 IELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-------E----LSGGEQQRVAIA 150
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 151 RAFV-NRPLVLLaDEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMrQRVVELSLGRLV 217
Cdd:COG4988 486 RALLrDAPLLLL-DEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQA-DRILVLDDGRIV 550
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-197 |
1.83e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.36 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARpaldDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL-- 78
Cdd:COG3840 1 MLRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL--------WNGQDLTALpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 --RQViGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV-N 155
Cdd:COG3840 69 aeRPV-SMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 156 RPLVLLaDEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHD 197
Cdd:COG3840 148 RPILLL-DEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHD 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
4.72e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.47 E-value: 4.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQY--KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRHV--P 76
Cdd:COG4525 3 MLTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD--------GVPVtgP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQviGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:COG4525 75 GADR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHD 197
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
7.70e-44 |
|
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: 144.69 E-value: 7.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhVPKLRQVI 82
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQdfrllqqktvydnvafalevigkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-216 |
1.02e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.52 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVrvskfhvnkLRGRH-VPKLRQ 80
Cdd:PRK11247 13 LLLNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEviGK-RTDAInrvvpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGLK--GQwRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-217 |
2.01e-43 |
|
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: 145.94 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV----PKLRQvIGCVFQDFRLLQQ 94
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIL--------LNGKDItnlpPEKRD-ISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 KTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETS 174
Cdd:cd03299 86 MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 175 RDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03299 166 EKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
8.08e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 147.92 E-value: 8.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpklRQV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 iGCVFQDFRLLQQKTVYDNVAFALEVIGKR----TDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:PRK10851 77 -GFVFQHYALFRHMTVFDNIAFGLTVLPRRerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 158 LVLLADEPTGNLDP----ETSRDIMDLLERINRTGTTVlmaTHDHHIVDSMRQRVVELSLGRLvrdEQRG 223
Cdd:PRK10851 156 QILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFV---THDQEEAMEVADRVVVMSQGNI---EQAG 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-219 |
2.88e-41 |
|
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: 143.02 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 34 LIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTD 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 114 AINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETsRDIMDL-LERINRT-GTTV 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKL-RDQMQLeLKTIQEQlGITF 154
|
170 180
....*....|....*....|....*...
gi 15610239 192 LMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQI 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-218 |
6.72e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 143.44 E-value: 6.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 6 HVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQVIGCV 85
Cdd:PRK11607 24 NLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 86 FQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 166 TGNLDPETsRDIM-----DLLERInrtGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK11607 177 MGALDKKL-RDRMqlevvDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-217 |
6.82e-41 |
|
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: 141.73 E-value: 6.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRL---LLAAETPTSGDVRV--------SKFHV 67
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFdgedllklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 68 NKLRGRHvpklrqvIGCVFQD--------FrllqqkTVYDNVAFALEV--IGKRTDAINRVVpEVLETVGLSGKANRL-- 135
Cdd:COG0444 81 RKIRGRE-------IQMIFQDpmtslnpvM------TVGDQIAEPLRIhgGLSKAEARERAI-ELLERVGLPDPERRLdr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 136 -PDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSL 213
Cdd:COG0444 147 yPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYA 226
|
....
gi 15610239 214 GRLV 217
Cdd:COG0444 227 GRIV 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-197 |
1.07e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 137.18 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRhvpKLRQVI 82
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK---ELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GcvfqdfrllqqktvydnvafalevigkrtdainrVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:cd03214 76 A----------------------------------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHD 197
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHD 157
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-197 |
1.39e-40 |
|
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: 137.17 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgRHVPKLRQVIGCVFQDF-RLLQQKT 96
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-KGLLERRQRVGLVFQDPdDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRD 176
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|.
gi 15610239 177 IMDLLERINRTGTTVLMATHD 197
Cdd:TIGR01166 166 MLAILRRLRAEGMTVVISTHD 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-197 |
4.03e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFhvnKLRGRHVPKLRQV 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQ--DFRLLQqKTVYDNVAFALEVIG-KRTDAINRVvPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK13635 83 VGMVFQnpDNQFVG-ATVQDDVAFGLENIGvPREEMVERV-DQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHD 197
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHD 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-197 |
5.72e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 140.24 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNK--LRGRHvpklrqv 81
Cdd:PRK11432 9 LKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQRD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 162 ADEPTGNLDPETSRD----IMDLLERINrtgTTVLMATHD 197
Cdd:PRK11432 160 FDEPLSNLDANLRRSmrekIRELQQQFN---ITSLYVTHD 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
5.84e-40 |
|
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: 137.86 E-value: 5.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKssARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKLR- 79
Cdd:COG0411 4 LLEVRGLTKRFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL--------FDGRDITGLPp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 -QV----IGCVFQDFRLLQQKTVYDNVAFALEVIGKRT---------------DAINRVVPEVLETVGLSGKANRLPDEL 139
Cdd:COG0411 74 hRIarlgIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 140 SGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.14e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 135.30 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpklRQ 80
Cdd:COG4133 2 MLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINrvVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV-NRPLV 159
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLsPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 160 LLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRqrvvELSLGR 215
Cdd:COG4133 154 LL-DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAAR----VLDLGD 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-214 |
1.40e-39 |
|
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: 136.06 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL---RQVigcVFQDFRLLQQK 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI--------LEGKQITEPgpdRMV---VFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEVIGK--RTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPET 173
Cdd:TIGR01184 70 TVRENIALAVDRVLPdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 174 SRDIMDLLERI-NRTGTTVLMATHDhhiVDS---MRQRVVELSLG 214
Cdd:TIGR01184 150 RGNLQEELMQIwEEHRVTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-197 |
1.93e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 136.37 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKLRQ 80
Cdd:PRK11248 1 MLQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT--------LDGKPVEGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK11248 71 ERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHD 197
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHD 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
2.58e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.94 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL 78
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 R-QVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:PRK10535 84 RrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVdSMRQRVVELSLGRLVRD 219
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRN 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
1.01e-38 |
|
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: 133.09 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVfLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklrGRHVPKLRQV 81
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVY---DNVAFALEVIGKRTDAInrvVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:cd03264 74 IGYLPQEFGVYPNFTVReflDYIAWLKGIPSKEVKAR---VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINrTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.05e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKLRQ 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE---NLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK13632 84 KIGIIFQnpDNQFIGA-TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRTGT-TVLMATHDhhivdsMRQ-----RVVELSLGRLVR 218
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHD------MDEailadKVIVFSEGKLIA 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-217 |
1.08e-38 |
|
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: 133.89 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvNKLRGRHVPKLRQV 81
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSmrQRVVELSLGRLV 217
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNA--DKIIVLKDGRIV 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
28-197 |
7.19e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 132.23 E-value: 7.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 28 KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVS----KFHVNKLRGRHVPKLRQV------IGCVFQDFRLLQQKTV 97
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeiRLKPDRDGELVPADRRQLqrirtrLGMVFQSFNLWSHMTV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YDNVAFA-LEVIGK-RTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSR 175
Cdd:COG4598 113 LENVIEApVHVLGRpKAEAIERAE-ALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVG 191
|
170 180
....*....|....*....|..
gi 15610239 176 DIMDLLERINRTGTTVLMATHD 197
Cdd:COG4598 192 EVLKVMRDLAEEGRTMLVVTHE 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
9.22e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 132.57 E-value: 9.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgRHVPKLRQ 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQ--DFRLLQQKTVYDnVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHD 202
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-217 |
9.24e-38 |
|
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: 133.28 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgRHVPKLRQVIGCVFQDFRLLQQKT 96
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRD 176
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15610239 177 IMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-219 |
9.99e-38 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 130.79 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKLRQV 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLqQKTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:cd03245 80 IGYVPQDVTLF-YGTLRDNITLG------APLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDsMRQRVVELSLGRLVRD 219
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGRIVAD 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
1.74e-37 |
|
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: 129.92 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNklrgrHVPKLRQVIGCVFQDFRLLQQKTVYDN 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-----AAPPADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 101 VAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDL 180
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 181 LERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:cd03298 171 VLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
1.81e-37 |
|
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: 130.97 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG-DVRVskFHvNKLRGRHVPKLR 79
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRL--FG-ERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDfrlLQQK-----TVYDNV---AFAleVIG---KRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVA 148
Cdd:COG1119 78 KRIGLVSPA---LQLRfprdeTVLDVVlsgFFD--SIGlyrEPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTG-TTVLMAThdHH---IVDSMrQRVVELSLGRLVRD 219
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVT--HHveeIPPGI-THVLLLKDGRVVAA 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-223 |
1.83e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 133.82 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSArPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvPKLRQ 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE----PADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 vIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK11650 78 -IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 161 LADEPTGNLDPETsRDIMDL----LERinRTGTTVLMATHDHhiVDSMR--QRVVELSLGRLvrdEQRG 223
Cdd:PRK11650 157 LFDEPLSNLDAKL-RVQMRLeiqrLHR--RLKTTSLYVTHDQ--VEAMTlaDRVVVMNGGVA---EQIG 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
2.39e-37 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 129.64 E-value: 2.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvpKLRQV 81
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-----EALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCvfqdfrLLQQKTVYDNVAF--ALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:cd03268 74 IGA------LIEAPGFYPNLTAreNLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-216 |
3.96e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 133.23 E-value: 3.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgrhVPKLRQV 81
Cdd:PRK11000 4 VTLRNVTKAYGDV--VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-----VPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 162 ADEPTGNLDP--------ETSRdimdLLERINRTGTTVlmaTHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK11000 157 LDEPLSNLDAalrvqmriEISR----LHKRLGRTMIYV---THDQVEAMTLADKIVVLDAGRV 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-196 |
4.92e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.06 E-value: 4.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrG---RHVPK- 77
Cdd:COG1132 340 IEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID--------GvdiRDLTLe 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 -LRQVIGCVFQDFRLLQqKTVYDNVAFALEvigKRTDAinRVVpEVLETVGLSGKANRLPD-----------ELSGGEQQ 145
Cdd:COG1132 411 sLRRQIGVVPQDTFLFS-GTIRENIRYGRP---DATDE--EVE-EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQ 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 146 RVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERInRTGTTVLMATH 196
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-197 |
5.19e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 129.51 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 26 IDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLR-QVIGCVFQDFRLLQQKTVYDNVAFA 104
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 105 LEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERI 184
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170
....*....|....
gi 15610239 185 NRT-GTTVLMATHD 197
Cdd:PRK10584 193 NREhGTTLILVTHD 206
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
18-219 |
7.88e-37 |
|
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: 129.34 E-value: 7.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVRVSKFHVNKlRGRHVPKLRQVIGCVFQDFRLL 92
Cdd:TIGR00972 16 ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIYD-KKIDVVELRRRVGMVFQKPNPF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QqKTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:TIGR00972 95 P-MSIYDNIAYGPRLHGIKDKKeLDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 168 NLDPETSRDIMDLLERInRTGTTVLMATHdhhivdSMRQ------RVVELSLGRLVRD 219
Cdd:TIGR00972 174 ALDPIATGKIEELIQEL-KKKYTIVIVTH------NMQQaarisdRTAFFYDGELVEY 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-217 |
9.06e-37 |
|
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: 128.26 E-value: 9.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlRGRHVpklRQV 81
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV---RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-217 |
1.41e-36 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 127.80 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKID---KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSK---FHVNKlrGRHVPKLRQVIGCVFQDFRLL 92
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRK--KINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQKTVYDNVAFALEVIGKRTDAINrvVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 173 TSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03297 166 LRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
12-218 |
1.43e-36 |
|
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: 131.51 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 12 KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKL-RQVIGCVFQDFR 90
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 LLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:TIGR01186 82 LFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 171 PETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:TIGR01186 162 PLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQ 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-218 |
2.68e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 129.09 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSS---ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHV-NKLRGRHVPK 77
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQdFRLLQ--QKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK13649 83 IRKKVGLVFQ-FPESQlfEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-198 |
3.71e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.44 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL---LAAETPTSGDVRvskfhvnkLRGR---H 74
Cdd:COG4136 1 MLSLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVL--------LNGRrltA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 75 VPKLRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:COG4136 71 LPAEQRRIGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVE-QALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDL-LERINRTGTTVLMATHDH 198
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDE 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.70e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 129.05 E-value: 4.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYK---SSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR----------------- 61
Cdd:PRK13651 3 IKVKNIVKIFNkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 62 -VSKFHVNKLRGRHVPK---LRQVIGCVFQ--DFRLLQQkTVYDNVAFALEVIG-KRTDAINRVVpEVLETVGLSGK-AN 133
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKKikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGvSKEEAKKRAA-KYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 134 RLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSL 213
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*.
gi 15610239 214 GRLVRD 219
Cdd:PRK13651 241 GKIIKD 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-217 |
5.16e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.24 E-value: 5.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlRGRHVPKLRQVIG 83
Cdd:PRK13637 8 LTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLS--GKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK13637 87 LVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-217 |
5.88e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 129.08 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQDFR--LLQQK 95
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPYasLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEV--IGKRTDAINRVVpEVLETVGLS-GKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:COG4608 113 TVGDIIAEPLRIhgLASKAERRERVA-ELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 173 TSRDIMDLLERI-NRTGTTVLMATHD----HHIVDsmrqRVVELSLGRLV 217
Cdd:COG4608 192 IQAQVLNLLEDLqDELGLTYLFISHDlsvvRHISD----RVAVMYLGKIV 237
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-219 |
1.22e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.73 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQY-------KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR 73
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 74 HVPKLRQVIGCVFQDF--RLLQQKTVYDNVAFALEVIGKRTDAINRV-VPEVLETVGLS-GKANRLPDELSGGEQQRVAI 149
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKAERLArASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
1.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHV--TKQYKSS-ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV-SKFHVNKLRGRHVPK 77
Cdd:PRK13634 3 ITFQKVehRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATH 196
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTH 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-218 |
1.36e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.12 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVsKFHVNKLRGRHVPKLRQVIGCVFQ--DFRLLQqK 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKKSLLEVRKTVGIVFQnpDDQLFA-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSR 175
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 176 DIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIK 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-217 |
1.53e-35 |
|
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: 125.24 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL--- 78
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR--------FDGRDITGLpph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 ---RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKrtDAINRVVPEVLETV-GLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:cd03224 71 eraRAGIGYVPEGRRIFPELTVEENLLLGAYARRR--AKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-216 |
1.73e-35 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 123.48 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQV 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLqQKTVYDNVafalevigkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMrQRVVELSLGRL 216
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-217 |
2.22e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVRvskfhvnkLRGR-------HVPKLRQVIG 83
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEIL--------LDGEdiydpdvDVVELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQdfrllqQ-----KTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAF 153
Cdd:COG1117 96 MVFQ------KpnpfpKSIYDNVAYGLRLHGIKSKSeLDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERInRTGTTVLMATHdhhivdSMRQ------RVVELSLGRLV 217
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTH------NMQQaarvsdYTAFFYLGELV 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
3.19e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.00 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgRHVPKLRQV 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQD-----FrllqQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:PRK13647 81 VGLVFQDpddqvF----SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
3.49e-35 |
|
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: 124.40 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgrHVPKL 78
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-196 |
3.90e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.00 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSS---ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKL-RGRHVP 76
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAF 153
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-196 |
5.61e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.59 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSS----ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrHVP 76
Cdd:PRK13633 4 MIKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE--NLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQ--DFRLLQqKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVA-TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATH 196
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-218 |
1.13e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.94 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRG-RHVPKLRQVIGCVFQdFRLLQ--QK 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQ-FPEAQlfEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETS 174
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 175 RDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
2.30e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.69 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKS-SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRL---LLAAEtptSGDVRVSKfhvNKLRGRHVP 76
Cdd:PRK13650 4 IIEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLidgLLEAE---SGQIIIDG---DLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQ--DFRLLQqKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK13650 78 DIRHKIGMVFQnpDNQFVG-ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVdSMRQRVVELSLGRL 216
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-197 |
3.58e-34 |
|
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: 121.21 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYKSSARpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklRGRHVPKLRQVI 82
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG------KPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQDF-RLLQQKTVYDNVAFALevigKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03226 74 GYVMQDVdYQLFTDSVREELLLGL----KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHD 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
4.18e-34 |
|
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: 121.95 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklRGRHVPKLRQV 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthdhHIVDSMRQ--RVVELSLGRLVRD-------EQ 221
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA----HRLSTIENadRIVVLEDGKIVERgtheellAQ 226
|
....*.
gi 15610239 222 RGVYGM 227
Cdd:cd03251 227 GGVYAK 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
9.34e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHV-PKLR 79
Cdd:COG4152 1 MLELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW--------DGEPLdPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:COG4152 71 RRIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-224 |
1.51e-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: 121.45 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSA-------RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR 73
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 74 HVPKLRQVIGCVFQDF--RLLQQKTVYDNVAFALEVIgKRTDAINRV--VPEVLETVGL-SGKANRLPDELSGGEQQRVA 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHL-TSLDESEQKarIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGRLVrdEQRGV 224
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV--EECDV 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-197 |
1.86e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.45 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQV 81
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQ--DFRLLQqKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK13640 86 VGIVFQnpDNQFVG-ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHD 197
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHD 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-209 |
2.12e-33 |
|
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: 125.48 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 15 ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvNKLRGRHVPKLRQVIGCVFQDFRLLQQ 94
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG---VPLADADADSWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 kTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:TIGR02857 411 -TIAENIRLA------RPDASDAEIREALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 164 EPTGNLDPETSRDIMDLLERInRTGTTVLMATHDHHIVDSMRQRVV 209
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIVV 528
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
7.59e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.45 E-value: 7.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTkqYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VigcvfqdfrlLQQKTvydNVAF---ALEVI-------GKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIA 150
Cdd:COG4559 79 V----------LPQHS---SLAFpftVEEVValgraphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 151 RAFV-------NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-215 |
1.50e-32 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 117.54 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV-SKFHVNKLRG---RHVPKLRQ-VIGCVFQDFRL 91
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLAQaspREILALRRrTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLsgkanrlPDEL--------SGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15610239 164 EPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-229 |
1.69e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.58 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKS-SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETptsGDvRVSKFHVNKL--------- 70
Cdd:PRK09984 1 MQTIIRVEKLAKTfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GD-KSAGSHIELLgrtvqregr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 71 RGRHVPKLRQVIGCVFQDFRLLQQKTVYDNV--------AFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGG 142
Cdd:PRK09984 77 LARDIRKSRANTGYIFQQFNLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 143 EQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQ 221
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....*...
gi 15610239 222 RGVYGMDR 229
Cdd:PRK09984 237 SQQFDNER 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-196 |
2.12e-32 |
|
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: 116.50 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 7 VTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL--LAAETPTSGDVRVSkfhvnklrGRHVPK--LRQVI 82
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLIN--------GRPLDKrsFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQDFRLLQQKTVYDNVAFALEvigkrtdainrvvpevletvgLSGkanrlpdeLSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAK---------------------LRG--------LSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190
....*....|....*....|....*....|....
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-217 |
2.53e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 118.96 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYkSSARP----ALDDINVKIDKGEFVFLIGPSGSGKSTFMRL---LLAAETPTS--GDVRVSkfhVNKLRG 72
Cdd:PRK13645 7 IILDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngLIISETGQTivGDYAIP---ANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 73 RHVPKLRQVIGCVFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAI 149
Cdd:PRK13645 83 KEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-217 |
1.18e-31 |
|
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: 120.94 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLLAAETPTSGDVRvskfhvnkLRGRHV-----PKLRQV----I 82
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSIL--------FDGQDLlglseRELRRIrgnrI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQD--------FRLLQQktvydnVAFALEVIGK--RTDAINRVVpEVLETVGLSGKANRL---PDELSGGEQQRVAI 149
Cdd:COG4172 95 AMIFQEpmtslnplHTIGKQ------IAEVLRLHRGlsGAAARARAL-ELLERVGIPDPERRLdayPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-201 |
1.27e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.25 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 15 ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklRGRHVPKLRQvIGCVFQDFRLlqq 94
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-------GGARVAYVPQ-RSEVPDSLPL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 kTVYDNVA---FALEVIGKRTDAINR-VVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:NF040873 73 -TVRDLVAmgrWARRGLWRRLTRDDRaAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 15610239 171 PETSRDIMDLLERINRTGTTVLMATHDHHIV 201
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
1.39e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.44 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgRHVPKLRQ 80
Cdd:PRK13652 3 LIETRDLCYSYSGS-KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQ--DFRLLQqKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK13652 79 FVGLVFQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-216 |
3.19e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRG----------RHVPKLRQVIGCVFQD 88
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 FRLLQQKTVYDNVAFA-LEVIG-KRTDAINRVVpEVLETVGLSGKAN-RLPDELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:PRK10619 101 FNLWSHMTVLENVMEApIQVLGlSKQEARERAV-KYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 166 TGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-217 |
5.16e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 119.14 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAET--PTSGDV--RVSK------FHVNKLR 71
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVALcekcgyVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 72 GRHVPK----------------------LRQVIGCVFQ-DFRLLQQKTVYDNVAFALEVIG-KRTDAINRVVpEVLETVG 127
Cdd:TIGR03269 79 GEPCPVcggtlepeevdfwnlsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGyEGKEAVGRAV-DLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 128 LSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMD-LLERINRTGTTVLMATHDHHIVDSMRQ 206
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|.
gi 15610239 207 RVVELSLGRLV 217
Cdd:TIGR03269 238 KAIWLENGEIK 248
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-218 |
6.90e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.35 E-value: 6.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 34 LIGPSGSGKSTFMRLLLAAETPTSGDVRV-------SKfhvnklRGRHVPKLRQVIGCVFQDFRLLQQKTVYDNVAFALe 106
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdSA------RGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLYGR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 107 vigKRTDAINRVVP--EVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERI 184
Cdd:COG4148 103 ---KRAPRAERRISfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 15610239 185 NR-TGTTVLMATHDhhiVDSMRQ---RVVELSLGRLVR 218
Cdd:COG4148 180 RDeLDIPILYVSHS---LDEVARladHVVLLEQGRVVA 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-217 |
1.01e-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: 113.09 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgRHVpkLRQVIGCVFQDFRLLQqK 95
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKS--LRSMIGVVLQDTFLFS-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIARAFVNRPLVLLADE 164
Cdd:cd03254 92 TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 165 PTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSmrQRVVELSLGRLV 217
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA--DKILVLDDGKII 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-221 |
1.08e-30 |
|
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: 118.25 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAEtPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQD-F-----RL 91
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFgslspRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 lqqkTVYDNVAFALEV--IGKRTDAINRVVPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGN 168
Cdd:COG4172 380 ----TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 169 LDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLVrdEQ 221
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV--EQ 507
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-219 |
2.69e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.98 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARpaldDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvNKLRGRHVPKLRQ 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM----RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL-----NGQDHTTTPPSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK10771 72 PVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRT-GTTVLMAThdHHIVDSMR--QRVVELSLGRLVRD 219
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVS--HSLEDAARiaPRSLVVADGRIAWD 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
2.77e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 4 LDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrgrhvpKLRqvIG 83
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLR--IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRV--------------------------------VPEVLETVGLSGK 131
Cdd:COG0488 65 YLPQEPPLDDDLTVLDTVLDGDAELRALEAELEELeaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 132 -ANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETsrdiMDLLER--INRTGtTVLMATHDHHIVDSMRQRV 208
Cdd:COG0488 145 dLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEflKNYPG-TVLVVSHDRYFLDRVATRI 219
|
250
....*....|
gi 15610239 209 VELSLGRLVR 218
Cdd:COG0488 220 LELDRGKLTL 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
3.37e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.49 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKS---SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKL----RGR 73
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeykRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 74 HvpklrqvIGCVFQD------FRLlqqkTVYDNVAFALE----------VIGKRTDAINrvvpEVLETVGLsGKANRLPD 137
Cdd:COG1101 81 Y-------IGRVFQDpmmgtaPSM----TIEENLALAYRrgkrrglrrgLTKKRRELFR----ELLATLGL-GLENRLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 138 E---LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMATHdhhivdSMRQ------R 207
Cdd:COG1101 145 KvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTH------NMEQaldygnR 218
|
250
....*....|..
gi 15610239 208 VVELSLGRLVRD 219
Cdd:COG1101 219 LIMMHEGRIILD 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-217 |
3.37e-30 |
|
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: 111.22 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRHV-PKLRQ 80
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--------GKPLdIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIG-KRTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:cd03269 71 RIGYLPEERGLYPKMKVIDQLVYLAQLKGlKKEEARRRID-EWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-197 |
1.24e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTkqYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQ 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VigcvfqdfrlLQQKTvydNVAFAL---EVI-------GKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIA 150
Cdd:PRK13548 80 V----------LPQHS---SLSFPFtveEVVamgraphGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 151 RAFV------NRPLVLLADEPTGNLDPETSRDIMDLL-ERINRTGTTVLMATHD 197
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHD 200
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
1.96e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.92 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPK---- 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL--------LNGQPIADysea 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 -LRQVIGCVFQDFRLLQQkTVYDNVAFALEvigkrtDAINRVVPEVLETVGLS-------------GKANRlpdELSGGE 143
Cdd:PRK11160 411 aLRQAISVVSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEklleddkglnawlGEGGR---QLSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 144 QQRVAIARAFV-NRPLVLLaDEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMrQRVVELSLGRLV 217
Cdd:PRK11160 481 QRRLGIARALLhDAPLLLL-DEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.06e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.09 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgRHVPKLRQ 80
Cdd:PRK13636 5 ILKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-KGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQD-FRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK13636 83 SVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLL-ERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-219 |
3.54e-29 |
|
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: 108.78 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 24 VKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRHVPKLRQVIGCVFQ------DFRLLQQKTV 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVA--------GASPGKGWRHIGYVPQrhefawDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDI 177
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610239 178 MDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSlGRLVRD 219
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIAD 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-196 |
3.59e-29 |
|
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: 109.17 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRP---ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKL 78
Cdd:cd03249 1 IEFKNVSFRYPS--RPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVFQDFRLLQqKTVYDNVAFALEvigkrtdaiNRVVPEVLETvglSGKAN------RLPD-----------ELSG 141
Cdd:cd03249 76 RSQIGLVSQEPVLFD-GTIAENIRYGKP---------DATDEEVEEA---AKKANihdfimSLPDgydtlvgergsQLSG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 142 GEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERInRTGTTVLMATH 196
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-217 |
4.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 109.69 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSArPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrHVPKLRQ 80
Cdd:PRK13644 1 MIRLENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRL-LQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK13644 78 LVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH---DHHIVDsmrqRVVELSLGRLV 217
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHnleELHDAD----RIIVMDRGKIV 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-219 |
5.49e-29 |
|
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: 108.57 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSAR-------------------PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV 62
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 63 SKFHVNKLRGRHVPKlrqvIGCVF-QDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSG 141
Cdd:cd03267 81 AGLVPWKRRKKFLRR----IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 142 GEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-216 |
5.93e-29 |
|
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: 114.34 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlrgrHVPKLRQV 81
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERInRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
7.32e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnklRGRHVpklrq 80
Cdd:COG0488 315 VLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---------LGETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQ-QKTVYDNVAFALEViGKRTDAINrvvpeVLETVGLSG-KANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:COG0488 379 KIGYFDQHQEELDpDKTVLDELRDGAPG-GTEQEVRG-----YLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLEriNRTGtTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALD--DFPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-219 |
1.23e-28 |
|
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: 107.96 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvNKLRGRHVPKLRQV 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfRLLQQKTVYDNVAFA--------LEVIGKRTDAIN--RVVPEVLET-VGLSGKAnrlpdeLSGGEQQRVAIA 150
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALAdpgmsmerVIEAAKLAGAHDfiSELPEGYDTiVGEQGAG------LSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthdHHIVDSMR-QRVVELSLGRLVRD 219
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIA---HRLSTVKNaDRIIVMEKGRIVEQ 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-197 |
2.93e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFM----RLLlaaeTPTSGDVRVSKFHVNKLRG---- 72
Cdd:COG4604 1 MIEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLL----PPDSGEVLVDGLDVATTPSrela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 73 RHVPKLRQVIGCVfqdFRLlqqkTVYDNVAFaleviG-------KRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQ 145
Cdd:COG4604 75 KRLAILRQENHIN---SRL----TVRELVAF-----GrfpyskgRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 146 RVAIARAFV-NRPLVLLaDEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:COG4604 143 RAFIAMVLAqDTDYVLL-DEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHD 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-227 |
3.79e-28 |
|
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: 111.35 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRhvpKLRQV 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA---SLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFaleviGKRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthdhHIVDSMRQ--RVVELSLGRLVRD-------EQ 221
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA----HRLSTIEKadRIVVMDDGRIVERgthnellAR 557
|
....*.
gi 15610239 222 RGVYGM 227
Cdd:TIGR02203 558 NGLYAQ 563
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
6.68e-28 |
|
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: 110.53 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSArPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVpklRQV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:TIGR02868 411 VSVCAQDAHLFDT-TVRENLRLA------RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLeRINRTGTTVLMATHD 197
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHH 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-215 |
1.27e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHVPK---- 77
Cdd:PRK13536 42 IDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--------LGVPVPArarl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-210 |
2.13e-27 |
|
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: 109.14 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklrgRHVPK--LR 79
Cdd:COG5265 358 VRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-----RDVTQasLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDfRLLQQKTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVA 148
Cdd:COG5265 432 AAIGIVPQD-TVLFNDTIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthdhH----IVDS-----MRQ-RVVE 210
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA----HrlstIVDAdeilvLEAgRIVE 572
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-216 |
2.20e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.79 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVkiDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrhvPKLRQV 81
Cdd:TIGR01277 1 LALDKVRYEYEH--LPMEFDLNV--ADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:TIGR01277 72 VSMLFQENNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERI-NRTGTTVLMAThdHHIVDSMR--QRVVELSLGRL 216
Cdd:TIGR01277 152 LDEPFSALDPLLREEMLALVKQLcSERQRTLLMVT--HHLSDARAiaSQIAVVSQGKI 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-193 |
2.73e-27 |
|
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: 104.29 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR-----VSKFHVNKLRGR-- 73
Cdd:COG0410 3 MLEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgedITGLPPHRIARLgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 74 -HVPKLRQVigcvfqdFRLLqqkTVYDNvafaLEV---IGKRTDAINRVVPEVLET--VgLSGKANRLPDELSGGEQQRV 147
Cdd:COG0410 81 gYVPEGRRI-------FPSL---TVEEN----LLLgayARRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQML 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 148 AIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLM 193
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-218 |
4.72e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.70 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVN------KLRGRHVPK-------LRQVIGC 84
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhELITNPYSKkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 85 VFQ--DFRLLQQkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGL-SGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-216 |
5.07e-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: 105.96 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLR-GRHVPKLRQVIGCVFQDFRLLQQKTVYD 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 NVAFALevigKRTDAINRVVP--EVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDI 177
Cdd:TIGR02142 95 NLRYGM----KRARPSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 178 MDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:TIGR02142 171 LPYLERLHAeFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-197 |
5.93e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.08 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQDFRLLQQK 95
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEVIGKRTDAINR-VVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETS 174
Cdd:PRK11831 100 NVFDNVAYPLREHTQLPAPLLHsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180
....*....|....*....|....
gi 15610239 175 RDIMDLLERINRT-GTTVLMATHD 197
Cdd:PRK11831 180 GVLVKLISELNSAlGVTCVVVSHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-218 |
7.29e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 107.58 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSAR---PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGD--VRVSKFHVN------K 69
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmtkpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 70 LRGRhvpkLRQVIGCVFQDFRLLQQKTVYDNVafalevigkrTDAINRVVPE---------VLETVGLSGKA-----NRL 135
Cdd:TIGR03269 359 GRGR----AKRYIGILHQEYDLYPHRTVLDNL----------TEAIGLELPDelarmkaviTLKMVGFDEEKaeeilDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 136 PDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMD-LLERINRTGTTVLMATHDHHIVDSMRQRVVELSLG 214
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....
gi 15610239 215 RLVR 218
Cdd:TIGR03269 505 KIVK 508
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-196 |
8.99e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.24 E-value: 8.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGrhvpKLRQV 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNvafalevIGKRtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFV-NRPLVL 160
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNN-------LGRR---------------------------FSGGERQRLALARILLqDAPIVL 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 161 LaDEPTGNLDPETSRDIMDLLERINRtGTTVLMATH 196
Cdd:cd03247 122 L-DEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-196 |
1.65e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYkssarP---ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHV-- 75
Cdd:COG3845 5 ALELRGITKRF-----GgvvANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI--------DGKPVri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 76 --PK--LRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGK---RTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVA 148
Cdd:COG3845 72 rsPRdaIALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGgrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-218 |
2.70e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 12 KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLR-QVIGCVFQDFR 90
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 LLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 171 PETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK10070 197 PLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-200 |
3.87e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 101.08 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDV-----RVSKFHVNKlrgrhvp 76
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqDITKLPMHK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNR 156
Cdd:cd03218 72 RARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 157 PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthDHHI 200
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLIT--DHNV 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-196 |
5.73e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKlRGRHVpklRQV 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHA---RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-196 |
6.76e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 6.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV----P 76
Cdd:COG1129 4 LLEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL--------LDGEPVrfrsP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 K--LRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGK---RTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIAR 151
Cdd:COG1129 74 RdaQAAGIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 152 AFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-206 |
7.11e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVRVSKFHVNKLRGRHVpKLRQVIGCVFQD---F 89
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTV-DLRKEIGMVFQQpnpF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 90 RLlqqkTVYDNVAFALEVIGKRTDAinrVVPEVLETvGLSGKA------NRLPDE---LSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK14239 99 PM----SIYENVVYGLRLKGIKDKQ---VLDEAVEK-SLKGASiwdevkDRLHDSalgLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERInRTGTTVLMATHdhhivdSMRQ 206
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTR------SMQQ 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-217 |
1.04e-25 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.49 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrGRHvpKLRQV 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLH--DLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfRLLQQKTVYDNvafaLEVIGKRTDA-INrvvpEVLETVGLSGKANRLPDEL-----------SGGEQQRVAI 149
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSN----LDPFGEYSDEeLW----QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLeRINRTGTTVLMATHD-HHIVDSmrQRVVELSLGRLV 217
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTI-REAFKDCTVLTIAHRlDTIIDS--DRILVLDKGRVV 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-196 |
1.07e-25 |
|
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: 99.78 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 6 HVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVrvskfhvnKLRGRHVPK--LRQvIG 83
Cdd:TIGR03740 5 NLSKRFGK--QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI--------IFDGHPWTRkdLHK-IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINrvvpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190
....*....|....*....|....*....|...
gi 15610239 164 EPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-204 |
1.26e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.06 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR---VSKFHVNK-LRGRHvpk 77
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgADLSQWDReELGRH--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 lrqvIGCVFQDFRLLQqKTVYDNVA-F----ALEVI--GKRTDA---INRVvPEVLET-VGLSGKAnrlpdeLSGGEQQR 146
Cdd:COG4618 408 ----IGYLPQDVELFD-GTIAENIArFgdadPEKVVaaAKLAGVhemILRL-PDGYDTrIGEGGAR------LSGGQRQR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 147 VAIARAFVNRP-LVLLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSM 204
Cdd:COG4618 476 IGLARALYGDPrLVVL-DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV 533
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
1.55e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.50 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklRGRHV----PK 77
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------DGKEVsfasPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 --LRQVIGCVFQdfrllqqktvydnvafalevigkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFVN 155
Cdd:cd03216 71 daRRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-217 |
1.78e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFM----RLLLAAETPTSGDVRVSKFHVNKLRGRHVpKLRQVIGCVFQDFRLLQQ 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSKIKVDGKVLYFGKDIFQIDAI-KLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 KTVYDNVAFALEVIG-KRTDAINRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNL 169
Cdd:PRK14246 105 LSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15610239 170 DPETSRDIMDLLERINRTgTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.14e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.93 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP-------------------ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR 61
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 62 VSKFHVNKLRGRHvpkLRQvIGCVF------------QD-FRLLqqKTVY--DNVAFAlevigKRTDainrvvpEVLETV 126
Cdd:COG4586 81 VLGYVPFKRRKEF---ARR-IGVVFgqrsqlwwdlpaIDsFRLL--KAIYriPDAEYK-----KRLD-------ELVELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 127 GLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMR 205
Cdd:COG4586 143 DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALC 222
|
250
....*....|....
gi 15610239 206 QRVVELSLGRLVRD 219
Cdd:COG4586 223 DRVIVIDHGRIIYD 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-201 |
2.92e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGdvRVSKFHVNKLRGR-HVPKLRQVIGCVFQDFRLL 92
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEG--RVEFFNQNIYERRvNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQkTVYDNVAFALEVIGKRTDA-INRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:PRK14258 101 PM-SVYDNVAYGVKIVGWRPKLeIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|....*
gi 15610239 168 NLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIV 201
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQV 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-217 |
3.41e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklRGRHVPKLRQV 81
Cdd:PRK13657 335 VEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfRLLQQKTVYDNV------------------AFALEVIGKRTDAINRVVPEvletvglsgKANRLpdelSGGE 143
Cdd:PRK13657 411 IAVVFQD-AGLFNRSIEDNIrvgrpdatdeemraaaerAQAHDFIERKPDGYDTVVGE---------RGRQL----SGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 144 QQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthdhHIVDSMRQ--RVVELSLGRLV 217
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA----HRLSTVRNadRILVFDNGRVV 548
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-196 |
3.98e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.83 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVRVSKFHVNKLrgrHVPKLRQVIGCVFQDFRLLQ 93
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKM---DVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 94 QKTVYDNVAFALEV--IGKRTDAINRVVPEVLETVGLSGKA-NRL---PDELSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:PRK14247 96 NLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVkDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180
....*....|....*....|....*....
gi 15610239 168 NLDPETSRDIMDLLERINRTgTTVLMATH 196
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-219 |
7.15e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLrqvIGCVFQDFRLLQQKT 96
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR---VASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFA----LEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:PRK09536 94 VRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15610239 173 TSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRlVRD 219
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGR-VRA 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-217 |
1.66e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.22 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKST----FMRLL-LAAETPTSGDVRVskFHVNKLRGRHVP-KLRQVIGCVFQDFRLL 92
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTllrtFNRLLeLNEEARVEGEVRL--FGRNIYSPDVDPiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQKTVYDNVAFALEVIG--KRTDAINRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 167 GNLDPETSRDIMDLLERInRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-196 |
1.85e-24 |
|
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: 100.89 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLR----GRHvpk 77
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfGKH--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 lrqvIGCVFQDFRLLQqKTVYDNVAfaleVIGKRTDAinrvvPEVLETVGLSGKAN---RLPD-----------ELSGGE 143
Cdd:TIGR01842 394 ----IGYLPQDVELFP-GTVAENIA----RFGENADP-----EKIIEAAKLAGVHElilRLPDgydtvigpggaTLSGGQ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 144 QQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
4.25e-24 |
|
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: 93.28 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrgrhvpklRQV 81
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQdfrllqqktvydnvafalevigkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIARAFVNRPLVLL 161
Cdd:cd03221 65 IGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 162 ADEPTGNLDPETsrdIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELS 212
Cdd:cd03221 94 LDEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELE 141
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-215 |
5.21e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLrqviGCV--FQDFRLLQQK 95
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM----GVVrtFQHVRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFA-------------LEVIGKR---TDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK11300 96 TVIENLLVAqhqqlktglfsglLKTPAFRraeSEALDRAA-TWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-196 |
6.08e-24 |
|
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: 94.35 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 15 ARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR---------HVPKLRQVIgcv 85
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphenilylgHLPGLKPEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 86 fqdfrllqqkTVYDNVAFALEVIGkrtdAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:TIGR01189 89 ----------SALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 15610239 166 TGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-196 |
6.11e-24 |
|
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: 95.42 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 5 DHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVnklrgRHVP---KLRQV 81
Cdd:TIGR04406 5 ENLIKSYKK--RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDI-----THLPmheRARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVIGKRT-DAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKDLDrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-220 |
6.14e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 94.91 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARP--------------------ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR 61
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 62 VskfhvnklRGRHVPKLRqvIGCVFQDfrllqQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLsGKANRLP-DELS 140
Cdd:cd03220 81 V--------RGRVSSLLG--LGGGFNP-----ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 141 GGEQQRV--AIARAFvnRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:cd03220 145 SGMKARLafAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
..
gi 15610239 219 DE 220
Cdd:cd03220 223 DG 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-202 |
8.66e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.10 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL-- 78
Cdd:COG1137 3 TLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF--------LDGEDITHLpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 ----RQVIGCVFQD---FRLLqqkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIAR 151
Cdd:COG1137 73 hkraRLGIGYLPQEasiFRKL---TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 152 AFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMAthDHH------IVD 202
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLIT--DHNvretlgICD 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-219 |
1.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.54 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 7 VTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvNKLRGRHVPKLRQVIGCVF 86
Cdd:PRK13642 11 VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 87 QD-FRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:PRK13642 88 QNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 166 TGNLDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSmRQRVVELSLGRLVRD 219
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-217 |
1.78e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLlaaETP----TSGDVRvskFHVNKLRGRHVPKLRQV----IG 83
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL---PSPpvvyPSGDIR---FHGESLLHASEQTLRGVrgnkIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 CVFQD----FRLLQ--QKTVYdnvafalEVI----GKRTDAINRVVPEVLETVGLSGKANRL---PDELSGGEQQRVAIA 150
Cdd:PRK15134 96 MIFQEpmvsLNPLHtlEKQLY-------EVLslhrGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-197 |
4.56e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVtkQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKL-- 78
Cdd:PRK10247 7 LLQLQNV--GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL--------FEGEDISTLkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 ---RQVIGCVFQDFRLLQQkTVYDNVAFALEVIGKRTDAiNRVVPEvLETVGLSGKA-NRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK10247 77 eiyRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDP-AIFLDD-LERFALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHD 197
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHD 197
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-212 |
5.00e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQyKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaAETPTSGDVRVskfhvnklrgrHVPKLRQ 80
Cdd:COG4178 362 ALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI--AGLWPYGSGRI-----------ARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIgcvfqdfrLLQQK------TVYDNVAFALEViGKRTDAinrVVPEVLETVGLSGKANRLPDE------LSGGEQQRVA 148
Cdd:COG4178 428 VL--------FLPQRpylplgTLREALLYPATA-EAFSDA---ELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERiNRTGTTVLMATH-----DHHivdsmrQRVVELS 212
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHrstlaAFH------DRVLELT 557
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-196 |
7.08e-23 |
|
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: 92.33 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTF----MRLLLAAETpTSGDVRVSkfhvNKLRGRHvpKLRQVIGCVFQDFRLLQQ 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLldaiSGRVEGGGT-TSGQILFN----GQPRKPD--QFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 KTVYDNVAFALEVIGKR--TDAINRVVPEV--LETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:cd03234 96 LTVRETLTYTAILRLPRksSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*.
gi 15610239 171 PETSRDIMDLLERINRTGTTVLMATH 196
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-217 |
1.39e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.07 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 13 SSARPALDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLLAAETPTSGDVRVS--KFHVNKLRGRHVPKLRQVIGCVF 86
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDgkPVAPCALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 87 QDFRllqqkTVYDNVAFALEVIGKRTDaiNRVVPEVLETVGLSGKANRL---PDELSGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:PRK10418 93 NPLH-----TMHTHARETCLALGKPAD--DATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 164 EPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-215 |
2.11e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKS-TFMRL--LLAAETPTSGDVRVSKFHVNKLRGRHVPKLR-QVIGCVFQD----- 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELNKLRaEQISMIFQDpmtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 ---FR--------LLQQKTVYDNVAFALEVigKRTDAINrvVPEVLETVGLsgkanrLPDELSGGEQQRVAIARAFVNRP 157
Cdd:PRK09473 111 npyMRvgeqlmevLMLHKGMSKAEAFEESV--RMLDAVK--MPEARKRMKM------YPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGR 215
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-217 |
2.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSA---RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHV-NKLRGRHVPK 77
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQdFRLLQ--QKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRL-PDELSGGEQQRVAIARAFV 154
Cdd:PRK13646 83 VRKRIGMVFQ-FPESQlfEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-217 |
3.30e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQD--FRLLQQK 95
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEvIGKRTDAINRV--VPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:PRK11308 110 KVGQILEEPLL-INTSLSAAERRekALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 173 TSRDI----MDLLERInrtGTTVLMATHD----HHIVDSmrqrVVELSLGRLV 217
Cdd:PRK11308 189 VQAQVlnlmMDLQQEL---GLSYVFISHDlsvvEHIADE----VMVMYLGRCV 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-210 |
3.60e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.40 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPK---- 77
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR--------LDGRPLSSlshs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 -LRQVIGCVFQDFRLLQQkTVYDNVAFALEVIGKRtdainrvVPEVLETVGLSGKANRLPD-----------ELSGGEQQ 145
Cdd:PRK10790 412 vLRQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQ-------VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 146 RVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDS------MRQRVVE 210
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEAdtilvlHRGQAVE 554
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-217 |
7.80e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQD--FRLLQQK 95
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEVIG-KRTDAINRVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPET 173
Cdd:PRK10261 419 TVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 174 SRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-197 |
7.99e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL-----LAAETPTSGDVrvsKFHVNKLRGRHVP--KLRQVIGCVFQD-- 88
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKV---TFHGKNLYAPDVDpvEVRRRIGMVFQKpn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 -FrllqQKTVYDNVAFALEVIGKRTDaINRVVPEVLETVGL----SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:PRK14243 102 pF----PKSIYDNIAYGARINGYKGD-MDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|....
gi 15610239 164 EPTGNLDPETSRDIMDLLERINRTGTTVLMaTHD 197
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIV-THN 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-222 |
1.82e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAE--TPTSGDVRVSKFHVNklrgrhvpklrqvigcvfqdfrllQ 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG------------------------R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 94 QKTVYDNVAfalevigkRTDAINRVVpEVLETVGLSGKAN--RLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:COG2401 99 EASLIDAIG--------RKGDFKDAV-ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15610239 172 ETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMR-QRVVELSLGRLVRDEQR 222
Cdd:COG2401 170 QTAKRVARNLQKLARrAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEKRR 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-219 |
2.60e-21 |
|
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: 91.72 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYkSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrGRHVpkLRQV 81
Cdd:TIGR01193 474 IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHT--LRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfRLLQQKTVYDNVafaleVIGKRTDAINRVVPEVLETVGLSGKANRLP-----------DELSGGEQQRVAIA 150
Cdd:TIGR01193 550 INYLPQE-PYIFSGSILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLerINRTGTTVLMATHDHHIVdSMRQRVVELSLGRLVRD 219
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQ 689
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-197 |
2.86e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV-----SKFHVNKLrGRHV 75
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLgdkpiSMLSSRQL-ARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 76 PKLRQVigcvfqdfrLLQQK--TVYDNVAFA----LEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAI 149
Cdd:PRK11231 79 ALLPQH---------HLTPEgiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 150 ARAFV-NRPLVLLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:PRK11231 150 AMVLAqDTPVVLL-DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-221 |
3.16e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKST----FMRLLlaaetPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQD--FRL 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAFALEVIGKRTDAINRV--VPEVLETVGLSGKA-NRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGN 168
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLSAAQREqqVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15610239 169 LDPETSRDIMDLLERI-NRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVrdEQ 221
Cdd:PRK15134 456 LDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV--EQ 507
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-196 |
6.18e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhVPKLRQV 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQkTVYDNVAFALEVIGKR------------TDAINRvVPEVLETV-GLSGKAnrlpdeLSGGEQQRVA 148
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQYSReqieeaarmayaMDFINK-MDNGLDTViGENGVL------LSGGQRQRIA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERI--NRtgtTVLMATH 196
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAH 537
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-225 |
6.35e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKS-SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQ 80
Cdd:TIGR00958 479 IEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDfRLLQQKTVYDNVAFAL------------------EVIGKRTDAINRVVPEvletvglsgKANrlpdELSGG 142
Cdd:TIGR00958 556 QVALVGQE-PVLFSGSVRENIAYGLtdtpdeeimaaakaanahDFIMEFPNGYDTEVGE---------KGS----QLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 143 EQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRtgtTVLMATHD-------HHIVDSMRQRVVELSLGR 215
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASR---TVLLIAHRlstveraDQILVLKKGSVVEMGTHK 698
|
250
....*....|
gi 15610239 216 LVRDEQrGVY 225
Cdd:TIGR00958 699 QLMEDQ-GCY 707
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-217 |
8.25e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.61 E-value: 8.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 12 KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQD--F 89
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 90 RLLQQKTVYDNVAFALEVIGKR--TDAINRVVPEVLETVGL-SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTYHPKlsRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15610239 167 GNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-216 |
1.10e-20 |
|
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: 85.56 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 14 SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR--------HVPKLRQVIGcv 85
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdairagiaYVPEDRKREG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 86 fqdfrLLQQKTVYDNVAfalevigkrtdainrvvpevletvglsgkanrLPDELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:cd03215 89 -----LVLDLSVAENIA--------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 166 TGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
1.26e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARP--------------------ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDV 60
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 61 RVskfhvnklRGRHVPKLRqvIGCVFQ-DFrllqqkTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLsGKANRLP-DE 138
Cdd:COG1134 84 EV--------NGRVSALLE--LGAGFHpEL------TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAEL-GDFIDQPvKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 139 LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
..
gi 15610239 219 DE 220
Cdd:COG1134 227 DG 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-217 |
1.54e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTfmrLL--LAAETPTSGDVRvskfhvnkLRGRhvpKLRQVIGCVFQDFR--LLQQ 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLarMAGLLPGQGEIL--------LNGR---PLSDWSAAELARHRayLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 KT------VYDNVAFALEVIGkRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAF------VN-RPLVLL 161
Cdd:COG4138 78 QSppfampVFQYLALHQPAGA-SSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 162 ADEPTGNLD--PETSRDimDLLERINRTGTTVLMATHD--HhivdSMRQ--RVVELSLGRLV 217
Cdd:COG4138 157 LDEPMNSLDvaQQAALD--RLLRELCQQGITVVMSSHDlnH----TLRHadRVWLLKQGKLV 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-217 |
3.20e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKssARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG-------DVRVSKFHVNKLRGrh 74
Cdd:PRK10895 4 LTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISLLPLHARARRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 75 vpklrqvIGCVFQDFRLLQQKTVYDNVAFALEV-----IGKRTDAINrvvpEVLETVGLSGKANRLPDELSGGEQQRVAI 149
Cdd:PRK10895 80 -------IGYLPQEASIFRRLSVYDNLMAVLQIrddlsAEQREDRAN----ELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-196 |
4.68e-20 |
|
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: 84.44 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 9 KQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRhvpklrqvIGCVFQd 88
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------GS--------IAYVSQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 FRLLQQKTVYDNVAFALEVIGKRTDainrvvpEVLETVGLSGKANRLPD-------E----LSGGEQQRVAIARAFVNRP 157
Cdd:cd03250 74 EPWIQNGTIRENILFGKPFDEERYE-------KVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15610239 158 LVLLADEPTGNLDPETSRDIMD-LLERINRTGTTVLMATH 196
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTH 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-196 |
5.33e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklRGRHVPKLRQVIGCV-FQDF--RLL 92
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVAEACHYLgHRNAmkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 qqkTVYDNVAFALEVIGKRtdaiNRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV-NRPLVLLaDEPTGNLDP 171
Cdd:PRK13539 89 ---TVAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRPIWIL-DEPTAALDA 160
|
170 180
....*....|....*....|....*
gi 15610239 172 ETSRDIMDLLERINRTGTTVLMATH 196
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-217 |
5.89e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.50 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAeTPTSGDVRVSKFHVN-----KLRGRhvpKLRQVIG----CVFQD 88
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADRFRWNgidllKLSPR---ERRKIIGreiaMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 FR--LLQQKTVYDNVAFAL---EVIGK---RTDAINRVVPEVLETVGL-SGKA--NRLPDELSGGEQQRVAIARAFVNRP 157
Cdd:COG4170 98 PSscLDPSAKIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-229 |
6.17e-20 |
|
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: 84.50 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYKSSarPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKL----RGRH---- 74
Cdd:TIGR03410 2 EVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLppheRARAgiay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 75 VPKLRQVigcvfqdFRLLqqkTVYDNVAFALEVIGKRTDAINRVVPE---VLETVglsgkANRLPDELSGGEQQRVAIAR 151
Cdd:TIGR03410 80 VPQGREI-------FPRL---TVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-----LGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 152 AFVNRPLVLLADEPTGNLDPETSRDIMDLLERIN-RTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQRGvyGMDR 229
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGD--ELDE 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-196 |
7.89e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 87.76 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvNKLRGRHVPKLRQ 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA----GKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
1.33e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfHVNKLRGRHVPK--- 77
Cdd:PRK09544 4 LVSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----RNGKLRIGYVPQkly 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQDFRLLQQKTVYDNVAFALEvigkrtdainRVvpevletvglsgKANRLPD----ELSGGEQQRVAIARAF 153
Cdd:PRK09544 78 LDTTLPLTVNRFLRLRPGTKKEDILPALK----------RV------------QAGHLIDapmqKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIV 201
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLV 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-217 |
1.44e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 11 YKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgRHVPKLRQVIGCVFQDfr 90
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 lLQQKTVY----DNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:PRK13638 86 -PEQQIFYtdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 167 GNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-210 |
2.50e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.73 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITL---DHVTKQYKSSARP-------ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskFHVNKL 70
Cdd:COG4167 1 MSALlevRNLSKTFKYRTGLfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEIL---INGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 71 RGRHVPKLRQVIGCVFQDF------RL---------LQQKTVYDNVAfalevigkRTDAINrvvpEVLETVGLSGK-ANR 134
Cdd:COG4167 78 EYGDYKYRCKHIRMIFQDPntslnpRLnigqileepLRLNTDLTAEE--------REERIF----ATLRLVGLLPEhANF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 135 LPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDL-LERINRTGTTVLMATHD----HHIVDS---MRQ 206
Cdd:COG4167 146 YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLmLELQEKLGISYIYVSQHlgivKHISDKvlvMHQ 225
|
....*
gi 15610239 207 -RVVE 210
Cdd:COG4167 226 gEVVE 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-197 |
2.82e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 20 DDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLrqvIGCVFQDFRLLQQKTVYD 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR---IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 NVA---FALEVIGKR-----TDAINRVvpevLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:PRK10253 101 LVArgrYPHQPLFTRwrkedEEAVTKA----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*..
gi 15610239 172 ETSRDIMDLLERINRT-GTTVLMATHD 197
Cdd:PRK10253 177 SHQIDLLELLSELNREkGYTLAAVLHD 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-216 |
6.98e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.64 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQVIGCVFQDFRLLQQktv 97
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKLFSAVFTDFHLFDQ--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 ydnvafaleVIGKR-TDAINRVVPEVLETVGLSGKA----NRLPD-ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:PRK10522 412 ---------LLGPEgKPANPALVEKWLERLKMAHKLeledGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 172 ETSRDI-MDLLERINRTGTTVLMATHDHHIVDsMRQRVVELSLGRL 216
Cdd:PRK10522 483 HFRREFyQVLLPLLQEMGKTIFAISHDDHYFI-HADRLLEMRNGQL 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-225 |
7.32e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAeTPTSGDVRVSKFHVNKLrgrHVPKLRQVIGCVFQDFRLLQQkT 96
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:PRK11174 439 LRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 166 TGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMRQRVVeLSLGRLVrdeQRGVY 225
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQWDQIWV-MQDGQIV---QQGDY 567
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-216 |
9.76e-19 |
|
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: 81.36 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 7 VTKQYKS-SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHvpkLRQVIGCV 85
Cdd:cd03248 17 VTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY---LHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 86 FQDfRLLQQKTVYDNVAFALevigkrTDAINRVVPEVLETVGLSGKANRLPDE-----------LSGGEQQRVAIARAFV 154
Cdd:cd03248 94 GQE-PVLFARSLQDNIAYGL------QSCSFECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTgTTVLMATHDHHIVDSMRQRVVeLSLGRL 216
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILV-LDGGRI 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-217 |
1.38e-18 |
|
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: 83.83 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYKSSaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrgrhvPKLRqvI 82
Cdd:TIGR03719 6 TMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------------PGIK--V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRV--------------------VPEVLETVGL---------SGKAN 133
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEIsakyaepdadfdklaaeqaeLQEIIDAADAwdldsqleiAMDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 134 RLPD------ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETsrdiMDLLER--INRTGtTVLMATHDHHIVDSMR 205
Cdd:TIGR03719 151 RCPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERhlQEYPG-TVVAVTHDRYFLDNVA 225
|
250
....*....|..
gi 15610239 206 QRVVELSLGRLV 217
Cdd:TIGR03719 226 GWILELDRGRGI 237
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-212 |
1.47e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 80.66 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 11 YKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHV-NKLRGRHVPKLRQVIGcvfqdf 89
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGHLPG------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 90 rLLQQKTVYDNVAFALEVIGKRTdaiNRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNL 169
Cdd:PRK13543 93 -LKADLSTLENLHFLCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15610239 170 DPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELS 212
Cdd:PRK13543 169 DLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-202 |
1.56e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV-SKFHVnklrgrhvpklrqvigCVFQDFR--LLQQK 95
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEV----------------AYFDQHRaeLDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAfalevIGKRTDAIN---RVVPEVLETVGLSGKANRLP-DELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:PRK11147 399 TVMDNLA-----EGKQEVMVNgrpRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
170 180 190
....*....|....*....|....*....|...
gi 15610239 172 ETsrdiMDLLERI--NRTGtTVLMATHDHHIVD 202
Cdd:PRK11147 474 ET----LELLEELldSYQG-TVLLVSHDRQFVD 501
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-217 |
2.02e-18 |
|
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: 81.03 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR--------VSKFHVNKLRG 72
Cdd:TIGR02323 3 LLQVSGLSKSYGG--GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsgaeLELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 73 RHVpkLRQVIGCVFQDFR--LLQQKTVYDNVAFALEVIGKR-TDAINRVVPEVLETVGLS-GKANRLPDELSGGEQQRVA 148
Cdd:TIGR02323 81 RRL--MRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
4.47e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 26 IDKGEFVFLIGPSGSGKSTfmrLL--LAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVigcvfqdfrLLQQktvyDNVAF 103
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKST---LLarMAGLLPGSGSIQFAGQPLEAWSAAELARHRAY---------LSQQ----QTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 104 ALEVI---------GKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAF--VNRPL-----VLLADEPTG 167
Cdd:PRK03695 83 AMPVFqyltlhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWPDInpagqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 168 NLDPeTSRDIMD-LLERINRTGTTVLMATHD-HHivdSMRQ--RVVELSLGRLV----RDE 220
Cdd:PRK03695 163 SLDV-AQQAALDrLLSELCQQGIAVVMSSHDlNH---TLRHadRVWLLKQGKLLasgrRDE 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-196 |
5.41e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLL---LAAETPTSGDVRVSKFHVNKlrgrhvPKLRQVIGCVFQDFRLLQQK 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDA------KEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 TVYDNVAFALEV-IGKRTDAINRV--VPEVLETVGLSGKANRL---PDE---LSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:TIGR00955 115 TVREHLMFQAHLrMPRRVTKKEKRerVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 15610239 167 GNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-217 |
6.19e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.92 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaaetptSGDVRVSKFHVNKLRGRHVPKLRqvigcvfQDFRLLQQKT 96
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIIYEQDLIVARLQ-------QDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIG---KRTDAINRVVP-------------------------------EVLETVGLSgkANRLPDELSGG 142
Cdd:PRK11147 83 VYDFVAEGIEEQAeylKRYHDISHLVEtdpseknlnelaklqeqldhhnlwqlenrinEVLAQLGLD--PDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 143 EQQRVAIARAFVNRPLVLLADEPTGNLDPETsrdiMDLLERINRT--GTTVLMaTHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTfqGSIIFI-SHDRSFIRNMATRIVDLDRGKLV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-217 |
7.79e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVpkLRQ 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQQKTVYDNVA----FA-LEVIGKRTDAINRVVPEVLETvglsgKANRlPDELSGGEQQRVAIARAFVN 155
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAmggfFAeRDQFQERIKWVYELFPRLHER-----RIQR-AGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 156 RPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-225 |
1.35e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.81 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 5 DHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR--------VSKFHVNKLRGRHVp 76
Cdd:PRK11701 10 RGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlRDLYALSEAERRRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 kLRQVIGCVFQDFR--LLQQKTVYDNVAFALEVIGKRT-DAINRVVPEVLETVGLSgkANR---LPDELSGGEQQRVAIA 150
Cdd:PRK11701 87 -LRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHD--------HHIVdSMRQ-RVVELSLGRLVRDE 220
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDlavarllaHRLL-VMKQgRVVESGLTDQVLDD 242
|
....*
gi 15610239 221 QRGVY 225
Cdd:PRK11701 243 PQHPY 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-217 |
2.01e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLlaaETPtsGDVRVSKFHVNklrGRHVPKL-----RQVIGC---- 84
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI---DYP--GRVMAEKLEFN---GQDLQRIsekerRNLVGAevam 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 85 VFQD--FRLLQQKTVYDNVAFALEVI--GKRTDAINRVVpEVLETVGLSGKANRL---PDELSGGEQQRVAIARAFVNRP 157
Cdd:PRK11022 94 IFQDpmTSLNPCYTVGFQIMEAIKVHqgGNKKTRRQRAI-DLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLL-ERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLlELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-196 |
2.09e-17 |
|
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: 77.15 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR---------HVPKLRQVIgcvf 86
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiargllylgHAPGIKTTL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 87 qdfrllqqkTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:cd03231 89 ---------SVLENLRFW------HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 15610239 167 GNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-217 |
2.84e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTkqYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHV----NKLRGRHVPKL 78
Cdd:PRK10575 13 ALRNVS--FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 79 RQVIGCVfqdfrllQQKTVYDNVAFALE----VIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK10575 91 PQQLPAA-------EGMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-212 |
5.77e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 75.27 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQyKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaaetptSGDVRVSKFHVNKLRGRH---VPK- 77
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWGSGRIGMPEGEDllfLPQr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 -------LRQVIgcvfqdfrllqqktVYdnvafalevigkrtdainrvvpevletvglsgkanrlP--DELSGGEQQRVA 148
Cdd:cd03223 73 pylplgtLREQL--------------IY-------------------------------------PwdDVLSGGEQQRLA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 149 IARAFVNRPLVLLADEPTGNLDPETSRDIMDLLeriNRTGTTVLMATHdHHIVDSMRQRVVELS 212
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-222 |
1.36e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.92 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARP---ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRHVPK- 77
Cdd:COG4615 328 LELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD--------GQPVTAd 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 ----LRQVIGCVFQDFRLLQqktvydnvafalEVIGKRTDAINRVVPEVLETVGLSGK----ANRLPD-ELSGGEQQRVA 148
Cdd:COG4615 400 nreaYRQLFSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHKvsveDGRFSTtDLSQGQRKRLA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 149 IARAFV-NRPLVLLaDEPTGNLDPETsRDI--MDLLERINRTGTTVLMATHDH---HIVDsmrqRVVELSLGRLVRDEQR 222
Cdd:COG4615 468 LLVALLeDRPILVF-DEWAADQDPEF-RRVfyTELLPELKARGKTVIAISHDDryfDLAD----RVLKMDYGKLVELTGP 541
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-218 |
1.78e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 14 SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfHVNKLRGRHVPK-LRQVIGCVFQDfR-- 90
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL---DGKPVRIRSPRDaIRAGIAYVPED-Rkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 --LLQQKTVYDNVAFA-LEVIGK----RTDAINRVVPEVLETVGLsgkanRLPD------ELSGGEQQRVAIARAFVNRP 157
Cdd:COG1129 339 egLVLDLSIRENITLAsLDRLSRggllDRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610239 158 LVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-197 |
2.01e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklrGRHVpklrqV 81
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETV-----K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQdFR--LLQQKTVYDNVAFALEVI--GKRTdaINrvvpevleTVGLSGKAN-------RLPDELSGGEQQRVAIA 150
Cdd:TIGR03719 387 LAYVDQ-SRdaLDPNKTVWEEISGGLDIIklGKRE--IP--------SRAYVGRFNfkgsdqqKKVGQLSGGERNRVHLA 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLEriNRTGTTVLMaTHD 197
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALL--NFAGCAVVI-SHD 499
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-196 |
3.02e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 36 GPSGSGKSTFMRLLLAAETPTSGDVRVSKfHV--NKLRGRHVPKLRQVIGCVFQDFRLLQQKTVYDNVAFAleVIGKRTD 113
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG--MAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 114 AINRVVpevlETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVL 192
Cdd:PRK11144 108 QFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPIL 183
|
....
gi 15610239 193 MATH 196
Cdd:PRK11144 184 YVSH 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-214 |
3.35e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPKLRQVIgcvFQDF------ 89
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRRQRDEY---HQDLlylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 90 ----RLLqqkTVYDNVAFALEVIGKRTDAinrVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV-NRPLVLLaDE 164
Cdd:PRK13538 83 pgikTEL---TALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLtRAPLWIL-DE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 165 PTGNLDPETSRDIMDLLERINRTGTTVLMAThdHHIVDSMRQRVVELSLG 214
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTT--HQDLPVASDKVRKLRLG 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-217 |
6.53e-16 |
|
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: 73.22 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGdvrvsKFHVNKLRGRHVP--KLR 79
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-----KIEIDGIDISTIPleDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFRLLqQKTVYDNvafaLEVIGKRTDAinrvvpEVLETVGLSGKANrlpdELSGGEQQRVAIARAFVNRPLV 159
Cdd:cd03369 82 SSLTIIPQDPTLF-SGTIRSN----LDPFDEYSDE------EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLeRINRTGTTVLMATHD-HHIVDSmrQRVVELSLGRLV 217
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTI-REEFTNSTILTIAHRlRTIIDY--DKILVMDAGEVK 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-196 |
7.31e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRq 80
Cdd:PRK09700 5 YISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 vIGCVFQDFRLLQQKTVYDNVaFALEVIGKRTDAINRV--------VPEVLETVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:PRK09700 82 -IGIIYQELSVIDELTVLENL-YIGRHLTKKVCGVNIIdwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-197 |
3.12e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNK-LRGR---HVPK 77
Cdd:PRK15056 7 IVVNDVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNlvaYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIgcvfQDFRLLQQKTV----YDNVAFAlevigKRTDAINR-VVPEVLETVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:PRK15056 86 SEEVD----WSFPVLVEDVVmmgrYGHMGWL-----RRAKKRDRqIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHD 197
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-196 |
3.53e-15 |
|
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: 73.71 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSArpALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkFHVNKLRGRHVPKL-R 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIY-WSGSPLKASNIRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFRLLQQKTVYDNVAFALEVI--GKRT--DAINRVVPEVLETVGLSGKANRLP-DELSGGEQQRVAIARAFV 154
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEITlpGGRMayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-217 |
4.81e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLD--HVTKQYKSSARP--ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAetpTSGDVRVSkfhVNKLRgrhvp 76
Cdd:PRK15093 1 MPLLDirNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVT---ADRMR----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 klrqvigcvFQDFRLLQ------QKTVYDNVAFAL----------EVIGKR-TDAI----------------NRVVPEVL 123
Cdd:PRK15093 70 ---------FDDIDLLRlsprerRKLVGHNVSMIFqepqscldpsERVGRQlMQNIpgwtykgrwwqrfgwrKRRAIELL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 124 ETVGLSGKANRL---PDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHH 199
Cdd:PRK15093 141 HRVGIKDHKDAMrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQ 220
|
250
....*....|....*...
gi 15610239 200 IVDSMRQRVVELSLGRLV 217
Cdd:PRK15093 221 MLSQWADKINVLYCGQTV 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-219 |
8.09e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 8.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 14 SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG-----DVRVSKFHVnkLRGRHVPKLRQVIGCVFQD 88
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 FRLLQQkTVYDNV---AFALEVIGKRTdaINRVVPEVLETVGL-SGKANRLPD---ELSGGEQQRVAIARAFVNRPLVLL 161
Cdd:PRK14271 110 PNPFPM-SIMDNVlagVRAHKLVPRKE--FRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 162 ADEPTGNLDPETSRDIMDLLERINRTgTTVLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-226 |
1.19e-14 |
|
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: 70.51 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 26 IDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVrvskfhvnklrgrhvPKLRQVIGCVFQDFRLLQQKTVYDnvaFAL 105
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---------------EIELDTVSYKPQYIKADYEGTVRD---LLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 106 EVI-GKRTDAINRVvpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE----TSRDIMDL 180
Cdd:cd03237 84 SITkDFYTHPYFKT--EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15610239 181 LERINRtgtTVLMATHDHHIVDSMRQRVvelslgrLVRDEQRGVYG 226
Cdd:cd03237 162 AENNEK---TAFVVEHDIIMIDYLADRL-------IVFEGEPSVNG 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-217 |
1.31e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 3 TLDHVTKQYkSSARPALDDIN------VKIdkGefvfLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrgrhvP 76
Cdd:PRK11819 8 TMNRVSKVV-PPKKQILKDISlsffpgAKI--G----VLGLNGAGKSTLLRIMAGVDKEFEGEARPA------------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 KLRqvIGCVFQDFRLLQQKTVYDNVAfalEVIGKRTDAINR-----------------------VVPEVLETVGL----- 128
Cdd:PRK11819 69 GIK--VGYLPQEPQLDPEKTVRENVE---EGVAEVKAALDRfneiyaayaepdadfdalaaeqgELQEIIDAADAwdlds 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 129 ----SGKANRLPD------ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETsrdiMDLLER--INRTGtTVLMATH 196
Cdd:PRK11819 144 qleiAMDALRCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQflHDYPG-TVVAVTH 218
|
250 260
....*....|....*....|.
gi 15610239 197 DHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11819 219 DRYFLDNVAGWILELDRGRGI 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-196 |
1.81e-14 |
|
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: 69.19 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 12 KSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETP--TSGDVRVSkfhvnklrGRHVPK-LRQVIGCVFQD 88
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILIN--------GRPLDKnFQRSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 89 FRLLQQKTVYDNVAFAlevigkrtdAINRvvpevletvglsgkanrlpdELSGGEQQRVAIARAFVNRPLVLLADEPTGN 168
Cdd:cd03232 88 DVHSPNLTVREALRFS---------ALLR--------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180
....*....|....*....|....*...
gi 15610239 169 LDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-196 |
3.36e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 6 HVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRlLLAAETPT---SGDVRvskFHVNKLRGRHVPKLRQV- 81
Cdd:PRK13549 10 NITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEII---FEGEELQASNIRDTERAg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQQKTVYDNVAFALEVI-GKRTD--AINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPL 158
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITpGGIMDydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-196 |
6.18e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGE-FVFLiGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV-PK---LRQVIGCVFQDFRLL 92
Cdd:NF033858 281 AVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAW--------LFGQPVdAGdiaTRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQKTVYDNVA-----FALEvigkrTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:NF033858 352 GELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|...
gi 15610239 168 NLDPeTSRD----IMDLLERinRTGTTVLMATH 196
Cdd:NF033858 427 GVDP-VARDmfwrLLIELSR--EDGVTIFISTH 456
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-194 |
7.76e-14 |
|
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: 67.67 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 6 HVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLL---LAAETPTSGDVRVSKFHVNKLRGRHVpklRQVI 82
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYP---GEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GCVFQD--FRLLqqkTVYDNVAFALEVIGkrtDAINRVVpevletvglsgkanrlpdelSGGEQQRVAIARAFVNRPLVL 160
Cdd:cd03233 87 YVSEEDvhFPTL---TVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVL 140
|
170 180 190
....*....|....*....|....*....|....*
gi 15610239 161 LADEPTGNLDPETSRDIMDLLERINR-TGTTVLMA 194
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADvLKTTTFVS 175
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-196 |
1.15e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 11 YKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhVPKLRQVIGCVFQDfR 90
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQT-P 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 LLQQKTVYDNVAFAlevigkRTDAINRVVPEVLETVGLSGKANRLPD-----------ELSGGEQQRVAIARAFVNRPLV 159
Cdd:PRK10789 399 FLFSDTVANNIALG------RPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEI 472
|
170 180 190
....*....|....*....|....*....|....*..
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERInRTGTTVLMATH 196
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-217 |
1.47e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLLAAetptSGDVRVSKFHVNKlRGRHVPKLRQVIGCVFQDFR-- 90
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQA----GGLVQCDKMLLRR-RSRQVIELSEQSAAQMRHVRga 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 ----LLQQKTVYDNVAFAL-EVIGK---------RTDAInRVVPEVLETVGLSGKA---NRLPDELSGGEQQRVAIARAF 153
Cdd:PRK10261 105 dmamIFQEPMTSLNPVFTVgEQIAEsirlhqgasREEAM-VEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLERINR-TGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-203 |
3.91e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrGRHVPKLRQ 80
Cdd:PRK15064 1 MLSTANITMQF--GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP-------NERLGKLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 vIGCVFQDFRLLQqkTVYDNVAFALEVIGKRtDAInRVVPEV----------LETV-----GLSGKA------------- 132
Cdd:PRK15064 72 -DQFAFEEFTVLD--TVIMGHTELWEVKQER-DRI-YALPEMseedgmkvadLEVKfaemdGYTAEAragelllgvgipe 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 133 ---NRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLeriNRTGTTVLMATHDHHIVDS 203
Cdd:PRK15064 147 eqhYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL---NERNSTMIIISHDRHFLNS 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-219 |
5.63e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 111 RTDAINRVvPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTT 190
Cdd:NF000106 118 RKDARARA-DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100
....*....|....*....|....*....
gi 15610239 191 VLMATHDHHIVDSMRQRVVELSLGRLVRD 219
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-182 |
6.79e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVskfhvnklrGRHVpklrqV 81
Cdd:PRK11819 325 IEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GETV-----K 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQdFR--LLQQKTVYDNVAFALEVI--GKRTdainrvVPE--VLETVGLSGkanrlPD------ELSGGEQQRVAI 149
Cdd:PRK11819 389 LAYVDQ-SRdaLDPNKTVWEEISGGLDIIkvGNRE------IPSraYVGRFNFKG-----GDqqkkvgVLSGGERNRLHL 456
|
170 180 190
....*....|....*....|....*....|...
gi 15610239 150 ARAFVNRPLVLLADEPTGNLDPETSRDIMDLLE 182
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-195 |
2.05e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKssARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV------SKFHVNKLRGR-- 73
Cdd:NF033858 2 ARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPRia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 74 HVPklrQVIGcvfqdfR-LLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:NF033858 80 YMP---QGLG------KnLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERI--NRTGTTVLMAT 195
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLVAT 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-216 |
2.27e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGR--------HVPKLRQVIGcVFQDFRLL 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLPEDRQSSG-LYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQKT--VYDNVAFALevigkRTDAINRVVPEVLETVGLS-GKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNL 169
Cdd:PRK15439 360 WNVCalTHNRRGFWI-----KPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15610239 170 DPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-175 |
3.73e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRq 80
Cdd:PRK15439 11 LLCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 vIGCVFQDFRLLQQKTVYDNVAFALEvigKRTDAINRvVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVL 160
Cdd:PRK15439 88 -IYLVPQEPLLFPNLSVKENILFGLP---KRQASMQK-MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170
....*....|....*.
gi 15610239 161 LADEPTGNLDP-ETSR 175
Cdd:PRK15439 163 ILDEPTASLTPaETER 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-226 |
6.12e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 26 IDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG----DVRVS-KfhvnklrgrhvPklrqvigcvfQDFRLLQQKTVYDN 100
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpELKISyK-----------P----------QYIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 101 vafaLEVIGKRTDAiNRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE----TSRD 176
Cdd:PRK13409 421 ----LRSITDDLGS-SYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKA 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 177 IMDLLErinRTGTTVLMATHDHHIVDSMRQRVvelslgrLVRDEQRGVYG 226
Cdd:PRK13409 496 IRRIAE---EREATALVVDHDIYMIDYISDRL-------MVFEGEPGKHG 535
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-215 |
6.41e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaaetptSGDVRVSKFHVNKL-RGRHVPK-LRQVIGCVFQDFRLLQ 93
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILaNNRKPTKqILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 94 QKTVYDNVAFALEVIGKRT---DAINRVVPEVLETVGLSGKANRLPDE-----LSGGEQQRVAIARAFVNRPLVLLADEP 165
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSltkQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 166 TGNLDPETSRDIMDLLERINRTGTTVLMATHD-HHIVDSMRQRVVELSLGR 215
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-196 |
7.14e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETpTSGDVRVSKFHVNKLRgrhVPKLRQV 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT---LQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQ---QKTVYDNVAFALEVIGKrtdainrvvpeVLETVGLSGKANRLPDE-----------LSGGEQQRV 147
Cdd:TIGR01271 1294 FGVIPQKVFIFSgtfRKNLDPYEQWSDEEIWK-----------VAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLM 1362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 148 AIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERiNRTGTTVLMATH 196
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH 1410
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-170 |
1.53e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHvnKLRGRHVPKLRQVIGCVFQDfRLLQQKTVYDN 100
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRSKIGVVSQD-PLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 101 VAFAL--------------------------------EVIGKRTDAINRVVPEVL-------------ETVGLSGK---- 131
Cdd:PTZ00265 480 IKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDMSNTTDSNELiemrknyqtikdsEVVDVSKKvlih 559
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15610239 132 --ANRLPD-----------ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:PTZ00265 560 dfVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-202 |
2.90e-11 |
|
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: 62.49 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 25 KIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG----DVRVS-KfhvnklrgrhvPklrQVIGcvfQDFrllqQKTVYD 99
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdeDLKISyK-----------P---QYIS---PDY----DGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 NVAfalEVIGKRTDAiNRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMD 179
Cdd:COG1245 421 FLR---SANTDDFGS-SYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 496
|
170 180
....*....|....*....|....
gi 15610239 180 LLERINR-TGTTVLMATHDHHIVD 202
Cdd:COG1245 497 AIRRFAEnRGKTAMVVDHDIYLID 520
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
4.79e-11 |
|
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: 61.02 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKST----FMRLLlaaetPTSGDVRVSKFHVNKLRgrhVPK 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLL-----NTEGDIQIDGVSWNSVP---LQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 78 LRQVIGCVFQDFRLLQqKTVYDNvafaLEVIGKRTDainRVVPEVLETVGLSGKANRLPDEL-----------SGGEQQR 146
Cdd:cd03289 75 WRKAFGVIPQKVFIFS-GTFRKN----LDPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 147 VAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERiNRTGTTVLMATH 196
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-216 |
5.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvNKLRGRHVPK--LRQVIGCVFQDFR---L 91
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD----GHEVVTRSPQdgLANGIVYISEDRKrdgL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAF-ALEVIGKRTDAINRV----------------VPEVLETVGLsgkanrlpdeLSGGEQQRVAIARAFV 154
Cdd:PRK10762 342 VLGMSVKENMSLtALRYFSRAGGSLKHAdeqqavsdfirlfnikTPSMEQAIGL----------LSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-217 |
7.40e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYksSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrgrhvpklRQV 81
Cdd:PRK15064 320 LEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE--------------NAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfrllqqkTVYDnvaFA-----LEVIGK-RTDAIN-RVVPEVLETVGLSGK-ANRLPDELSGGEQQRVAIARAF 153
Cdd:PRK15064 384 IGYYAQD-------HAYD---FEndltlFDWMSQwRQEGDDeQAVRGTLGRLLFSQDdIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMDLLEriNRTGtTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALE--KYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
16-198 |
8.14e-11 |
|
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: 58.53 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETptsgdvrvskFHVNKLRGRHVPKLRQVIGCVfqdfrllqqk 95
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALG----------GAQSATRRRSGVKAGCIVAAV---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 96 tvydNVAFALEVIGkrtdainrvvpevletvglsgkanrlpdeLSGGEQQRVAIA-----RAFVNRPLVLLaDEPTGNLD 170
Cdd:cd03227 68 ----SAELIFTRLQ-----------------------------LSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLD 113
|
170 180
....*....|....*....|....*...
gi 15610239 171 PETSRDIMDLLERINRTGTTVLMATHDH 198
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-179 |
9.12e-11 |
|
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: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRhvpklrqvIGCVFQdFRLLQQKT 96
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS--------GR--------ISFSPQ-TSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIGKR-TDAIN--------RVVPEVLETVGLSGKANrlpdeLSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:TIGR01271 503 IKDNIIFGLSYDEYRyTSVIKacqleediALFPEKDKTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|..
gi 15610239 168 NLDPETSRDIMD 179
Cdd:TIGR01271 578 HLDVVTEKEIFE 589
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-229 |
1.01e-10 |
|
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: 61.11 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 9 KQYKSSARPALD----DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrGRHvpKLRQVIGC 84
Cdd:TIGR00957 1288 RNYCLRYREDLDlvlrHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLH--DLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 85 VFQDFRLLQqktvyDNVAFALEVIGKRTDainRVVPEVLETVGLSGKANRLPDEL-----------SGGEQQRVAIARAF 153
Cdd:TIGR00957 1365 IPQDPVLFS-----GSLRMNLDPFSQYSD---EEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 154 VNRPLVLLADEPTGNLDPETSrdimDLLERINRT---GTTVLMATHD-HHIVDSMrqRVVELSLGRlVRD--------EQ 221
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETD----NLIQSTIRTqfeDCTVLTIAHRlNTIMDYT--RVIVLDKGE-VAEfgapsnllQQ 1509
|
....*....
gi 15610239 222 RGV-YGMDR 229
Cdd:TIGR00957 1510 RGIfYSMAK 1518
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-196 |
1.01e-10 |
|
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: 59.27 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 13 SSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVS-KFHVNKLRGRHVPKLRQVIGCVFQDFRL 91
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQqKTVYDNVAFALEVIGKRTDAinrvvpeVLETVGLSGKANRLP--DE---------LSGGEQQRVAIARAFVNRPLVL 160
Cdd:cd03290 91 LN-ATVEENITFGSPFNKQRYKA-------VTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNIV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 15610239 161 LADEPTGNLDPETSRDIMD--LLERINRTGTTVLMATH 196
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-179 |
1.32e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 59.87 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSkfhvnklrGRhvpklrqvIGCVFQdFRLLQQKT 96
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--------GR--------ISFSSQ-FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDE----LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:cd03291 114 IKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*..
gi 15610239 173 TSRDIMD 179
Cdd:cd03291 194 TEKEIFE 200
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-220 |
1.65e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 14 SARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAaETPTSGDVRVSkfhvnkLRGR--HVPKLRQVIGCVFQDFRL 91
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVV------IRGSvaYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAFALEVIGKRTDaINRVVPEVLETVGLSGKanrlpdELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:PLN03232 701 FGSDFESERYWRAIDVTALQHD-LDLLPGRDLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15610239 172 ETSRDIMDLLERINRTGTTVLMATHDHHIVDSMrQRVVELSLGrLVRDE 220
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEG-MIKEE 820
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-204 |
2.00e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 28 KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVrvskfhvnklrgrhvpklrqvigcvfqdfrllqqktvydnVAFALEV 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------IYIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 108 IGKRTDAINRVVPEvletvglsgkaNRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLE----- 182
Cdd:smart00382 41 ILEEVLDQLLLIIV-----------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|...
gi 15610239 183 -RINRTGTTVLMATHDHHIVDSM 204
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-191 |
2.52e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 17 PALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLL-----------AAETPTSGDV-----------------RVSKFHVN 68
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhiVFKNEHTNDMtneqdyqgdeeqnvgmkNVNEFSLT 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 69 KLRGR-----------------------HVPKLRQVIGCVFQDfRLLQQKTVYDNVAFALEViGKRTDaINRV-----VP 120
Cdd:PTZ00265 1262 KEGGSgedstvfknsgkilldgvdicdyNLKDLRNLFSIVSQE-PMLFNMSIYENIKFGKED-ATRED-VKRAckfaaID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 121 EVLET--------VGLSGKAnrlpdeLSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPET----SRDIMDLLERINRTG 188
Cdd:PTZ00265 1339 EFIESlpnkydtnVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliEKTIVDIKDKADKTI 1412
|
...
gi 15610239 189 TTV 191
Cdd:PTZ00265 1413 ITI 1415
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-217 |
3.54e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrgrhvpklrqVIGCVFQDFRLLQqKTVY 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER----------------SIAYVPQQAWIMN-ATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 99 DNVAFALEVIGKR-TDAInRV---------VPEVLET-VGLSGKanrlpdELSGGEQQRVAIARA-FVNRPLVLLaDEPT 166
Cdd:PTZ00243 739 GNILFFDEEDAARlADAV-RVsqleadlaqLGGGLETeIGEKGV------NLSGGQKARVSLARAvYANRDVYLL-DDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 167 GNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVdSMRQRVVELSLGRLV 217
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVE 860
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-217 |
4.66e-10 |
|
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: 58.00 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhVPKLRQV 81
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQD---------FRLLQQKTVYDNVAF-ALEVigKRTDAINRVVPEVLETVGLSGKANrlpdeLSGGEQQRVAIAR 151
Cdd:cd03288 97 LSIILQDpilfsgsirFNLDPECKCTDDRLWeALEI--AQLKNMVKSLPGGLDAVVTEGGEN-----FSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 152 AFVNRPLVLLADEPTGNLDPETSrdimDLLERINRTG----TTVLMATHDHHIVDSmrQRVVELSLGRLV 217
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATE----NILQKVVMTAfadrTVVTIAHRVSTILDA--DLVLVLSRGILV 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-202 |
6.43e-10 |
|
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: 57.38 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 29 GEFVFLIGPSGSGKSTFMRLLLAAETPTSGdvrvsKFHVNklrgrhvPKLRQVI----GCVFQDF--RLLQ------QKT 96
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG-----KFDDP-------PDWDEILdefrGSELQNYftKLLEgdvkviVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VY-DNVAFAleVIGKRTDAINRV-----VPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:cd03236 94 QYvDLIPKA--VKGKVGELLKKKdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|..
gi 15610239 171 PETSRDIMDLLERINRTGTTVLMATHDHHIVD 202
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-173 |
1.00e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV----PKLRQV--IGCVFQDFRL 91
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL--------YLGKEVtfngPKSSQEagIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAFALEVIGK--RTD--AINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTG 167
Cdd:PRK10762 91 IPQLTIAENIFLGREFVNRfgRIDwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
....*..
gi 15610239 168 NL-DPET 173
Cdd:PRK10762 171 ALtDTET 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-179 |
1.17e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.03 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAaetptsgdvrvskfHVNKLRGrHVpKLRQV 81
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEG-HV-HMKGS 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDfRLLQQKTVYDNVAFALEVIGKRTDAinrvvpeVLETVGLSGKANRLPD-----------ELSGGEQQRVAIA 150
Cdd:TIGR00957 701 VAYVPQQ-AWIQNDSLRENILFGKALNEKYYQQ-------VLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLA 772
|
170 180
....*....|....*....|....*....
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMD 179
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-218 |
1.42e-09 |
|
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: 55.61 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAE--TPTSGDVRvskfhvnkLRGRHVPKL------RQVIGCVFQDfr 90
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIL--------FKGEDITDLppeeraRLGIFLAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 91 llqqktvydnvafALEVIGKRTDAINRVVPEvletvglsgkanrlpdELSGGEQQRVAIARAFVNRP-LVLLaDEPTGNL 169
Cdd:cd03217 86 -------------PPEIPGVKNADFLRYVNE----------------GFSGGEKKRNEILQLLLLEPdLAIL-DEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 170 DPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMR-QRVVELSLGRLVR 218
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIKpDRVHVLYDGRIVK 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-181 |
1.43e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 34 LIGPSGSGKSTFMRLLLAAETPTSGDVRVS--KFHVNKLRGRhvpklRQVIGCVFQD--------FRLLQQKTVYDNVAF 103
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDdhPLHFGDYSYR-----SQRIRMIFQDpstslnprQRISQILDFPLRLNT 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 104 ALEVIgKRTDAINrvvpEVLETVGL-SGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLL 181
Cdd:PRK15112 119 DLEPE-QREKQII----ETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-218 |
2.05e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHV------PKLRQVIGCVFQDFRL 91
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL--------IDGQEMrfasttAALAAGVAIIYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVAF-----ALEVIGKRTdaINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPT 166
Cdd:PRK11288 91 VPEMTVAENLYLgqlphKGGIVNRRL--LNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15610239 167 GNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-224 |
2.07e-09 |
|
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: 56.55 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGeFVFLIGPSGSGKSTFMRLL-LAAETPTSGDVRVSKFHvnklRGRHVPKLRQVIGCVFQD-----FRLL 92
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALrLLLGPSSSRKFDEEDFY----LGDDPDLPEIEIELTFGSllsrlLRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 QQKTVYDNVAFALEVIGKR--------TDAINRVVPEVLE--------------------TVGLSGKANRLPDELSGGEQ 144
Cdd:COG3593 89 LKEEDKEELEEALEELNEElkealkalNELLSEYLKELLDgldlelelsldeledllkslSLRIEDGKELPLDRLGSGFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 145 QRV------AIARAFVNRPLVLLA-DEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRvvelSLGRLV 217
Cdd:COG3593 169 RLIllallsALAELKRAPANPILLiEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPLE----NIRRLR 244
|
....*..
gi 15610239 218 RDEQRGV 224
Cdd:COG3593 245 RDSGGTT 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-199 |
2.31e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAaETPTSGDVRVSkfhvnkLRGR--HVPKlrqvIGCVFQdfrllq 93
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRSDASVV------IRGTvaYVPQ----VSWIFN------ 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 94 qKTVYDNVAFALEVIGKRtdaINRVVpevlETVGLSGKANRLPD-----------ELSGGEQQRVAIARAFVNRPLVLLA 162
Cdd:PLN03130 693 -ATVRDNILFGSPFDPER---YERAI----DVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190
....*....|....*....|....*....|....*..
gi 15610239 163 DEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHH 199
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLH 801
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-194 |
2.48e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlAAETPTSGDVRVSKFHVNKLRGRH-VPKLR-QVIGCVFQDFRLlQQKT 96
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTI-ASNTDGFHIGVEGVITYDGITPEEiKKHYRgDVVYNAETDVHF-PHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFA--LEVIGKRTDAINR------VVPEVLETVGLSGKAN-RLPDEL----SGGEQQRVAIARAFVNRPLVLLAD 163
Cdd:TIGR00956 155 VGETLDFAarCKTPQNRPDGVSReeyakhIADVYMATYGLSHTRNtKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190
....*....|....*....|....*....|..
gi 15610239 164 EPTGNLDPETSRDIMDLLERI-NRTGTTVLMA 194
Cdd:TIGR00956 235 NATRGLDSATALEFIRALKTSaNILDTTPLVA 266
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-201 |
3.27e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDV-RVSKFHVNKLRGRHVPKLRqvigcvfqdfrLLQQKTVYd 99
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAVFSQHHVDGLD-----------LSSNPLLY- 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 nvafalevigkrtdaINRVVPEVLE--------TVGLSGKANRLPD-ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:PLN03073 595 ---------------MMRCFPGVPEqklrahlgSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190
....*....|....*....|....*....|.
gi 15610239 171 PETsrdIMDLLERINRTGTTVLMATHDHHIV 201
Cdd:PLN03073 660 LDA---VEALIQGLVLFQGGVLMVSHDEHLI 687
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-197 |
3.84e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR-----VSKFHVNKLRGR---HVPKLRQVIGCVfQ 87
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgedITGLSPRERRRLgvaYIPEDRLGRGLV-P 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 88 DFrllqqkTVYDNvaFALEVIGK---------RTDAINRVVPEVLE-----TVGLSGKAnrlpDELSGGEQQRVAIARAF 153
Cdd:COG3845 350 DM------SVAEN--LILGRYRRppfsrggflDRKAIRAFAEELIEefdvrTPGPDTPA----RSLSGGNQQKVILAREL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 154 VNRPLVLLADEPTGNLDPETSRDIMD-LLERINRtGTTVLMATHD 197
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDA-GAAVLLISED 461
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-196 |
6.22e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 8 TKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaAETPTSGDVRVSKFHVNklrGRHVPK-LRQVIGCVF 86
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVITGGDRLVN---GRPLDSsFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 87 QDFRLLQQKTVYDNVAFA--LEVIGKRTDA-INRVVPEVLETVGLSGKANRL---PDE-LSGGEQQRVAIARAFVNRP-L 158
Cdd:TIGR00956 843 QQDLHLPTSTVRESLRFSayLRQPKSVSKSeKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPkL 922
|
170 180 190
....*....|....*....|....*....|....*...
gi 15610239 159 VLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:TIGR00956 923 LLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-171 |
6.65e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlAAETPTSGDVRVSKFHVNKLRGRHVPKLRQV 81
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHPQGYSNDLTLFGRRRGSGETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCV----FQDFRLlqqKTVYDNVAFA--LEVIG---KRTDAINRVVPEVLETVGLSGKANRLP-DELSGGEQQRVAIAR 151
Cdd:PRK10938 338 IGYVssslHLDYRV---STSVRNVILSgfFDSIGiyqAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVR 414
|
170 180
....*....|....*....|
gi 15610239 152 AFVNRPLVLLADEPTGNLDP 171
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDP 434
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-219 |
8.16e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKssARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlAAETPTS---------GDVRVSKFHVNKLR 71
Cdd:PRK13547 1 MLTADHLHVARR--HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL-AGDLTGGgaprgarvtGDVTLNGEPLAAID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 72 GRHVPKLRQVIGcvfQDFRLLQQKTVYDNVAFALEVIGKRTDAINR----VVPEVLETVGLSGKANRLPDELSGGEQQRV 147
Cdd:PRK13547 78 APRLARLRAVLP---QAAQPAFAFSAREIVLLGRYPHARRAGALTHrdgeIAWQALALAGATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 148 AIARAFVN---------RPLVLLADEPTGNLDPETSRDIMDLLERINRT-GTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK13547 155 QFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
..
gi 15610239 218 RD 219
Cdd:PRK13547 235 AH 236
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-201 |
1.11e-08 |
|
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: 53.77 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFM----------RLLLAAETPTSGDVRVSKFHVNKLR-------GRhVP----- 76
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIEGLEHIDKVIvidqspiGR-TPrsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 77 -------KLRQVIGCVFQDFRLLQQ--------KTVYD----NVAFALEVIgKRTDAINRVVpEVLETVGLSG-KANRLP 136
Cdd:cd03271 90 tytgvfdEIRELFCEVCKGKRYNREtlevrykgKSIADvldmTVEEALEFF-ENIPKIARKL-QTLCDVGLGYiKLGQPA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 137 DELSGGEQQRVAIARAFVNRP----LVLLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIV 201
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRStgktLYIL-DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-204 |
1.58e-08 |
|
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: 52.99 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 23 NVKIDKGEFVFLI-GPSGSGKSTfmrLLLAAETPTSGDVRVskfhvNKLRGRHVPKL---RQVIGCVFQDFRLLQQK--T 96
Cdd:cd03240 15 RSEIEFFSPLTLIvGQNGAGKTT---IIEALKYALTGELPP-----NSKGGAHDPKLireGEVRAQVKLAFENANGKkyT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 97 VYDNVAFALEVIGKRTDAINRVVPEVLETvglsgkanrlpdeLSGGEQQ------RVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:cd03240 87 ITRSLAILENVIFCHQGESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 15610239 171 PETSRD-IMDLLERINRTGT-TVLMATHDHHIVDSM 204
Cdd:cd03240 154 EENIEEsLAEIIEERKSQKNfQLIVITHDEELVDAA 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-203 |
3.68e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrhvpklrqvigcVFQDfrllQQKTV 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL--------------IFID----QLQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YDnvafalevigkrtdainrvvpevletVGLSG-KANRLPDELSGGEQQRVAIAR-AFVN-RPLVLLADEPTGNLDPETS 174
Cdd:cd03238 72 ID--------------------------VGLGYlTLGQKLSTLSGGELQRVKLASeLFSEpPGTLFILDEPSTGLHQQDI 125
|
170 180
....*....|....*....|....*....
gi 15610239 175 RDIMDLLERINRTGTTVLMATHDHHIVDS 203
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-202 |
4.67e-08 |
|
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: 51.87 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAEtptsGDVR----VSKFHVNKLRGRHVPKLRQVIGcvfqdfrL--- 91
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAE----GQRRyvesLSAYARQFLGQMDKPDVDSIEG-------Lspa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 --LQQKT--------------VYD--NVAFALEVIGKRTDAINRVVpevLETVGLSGKANrlpdELSGGEQQRVAIAR-- 151
Cdd:cd03270 80 iaIDQKTtsrnprstvgtvteIYDylRLLFARVGIRERLGFLVDVG---LGYLTLSRSAP----TLSGGEAQRIRLATqi 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 152 --AFVNRPLVLlaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDH-------HIVD 202
Cdd:cd03270 153 gsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEdtiraadHVID 210
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
23-229 |
6.85e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 51.89 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 23 NVK-IDKGEFVF-----LIGPSGSGKSTFMRLLLA----------AE--TPTSGDVRVSKFHVN-KLRGRHVPKLRQVIG 83
Cdd:COG4938 8 NFGpFKEAELELkpltlLIGPNGSGKSTLIQALLLllqsnfiylpAErsGPARLYPSLVRELSDlGSRGEYTADFLAELE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 84 cvFQDFRLLQQKTVYDNVAFALEVI--GKRTDAINRVVPEVLETVGLSGKANRLPDELSGgeQQR-----VAIARAFVNR 156
Cdd:COG4938 88 --NLEILDDKSKELLEQVEEWLEKIfpGKVEVDASSDLVRLVFRPSGNGKRIPLSNVGSG--VSEllpilLALLSAAKPG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 157 PLVLLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVElslGRLVRDEQRGVYGMDR 229
Cdd:COG4938 164 SLLII-EEPEAHLHPKAQSALAELLAELANSGVQVIIETHSDYILNGLRNLIKE---GKLLDPDDVAVYFFER 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-200 |
6.94e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 34 LIGPSGSGKSTFMRLLLAAETP--TSGDVRVSKFHVN-----KLRGR------HVPKLRQVIGCVFQDF-RLLQQKTVYD 99
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKqetfaRISGYceqndiHSPQVTVRESLIYSAFlRLPKEVSKEE 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 NVAFALEV-----IGKRTDAInrvvpevletVGLSGKANrlpdeLSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETS 174
Cdd:PLN03140 991 KMMFVDEVmelveLDNLKDAI----------VGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180
....*....|....*....|....*.
gi 15610239 175 RDIMDLLERINRTGTTVLMATHDHHI 200
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-196 |
7.36e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLA--AETPTSGDVRVSKFHVNKLRgrhvPKLRQVIGC--VFQ---- 87
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE----PEERAHLGIflAFQypie 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 88 -------DF--------RLLQQKTVYDNVAFaLEVIGKRTDAINrvvpevLETVGLSGKANrlpDELSGGEQQRVAIARA 152
Cdd:CHL00131 96 ipgvsnaDFlrlaynskRKFQGLPELDPLEF-LEIINEKLKLVG------MDPSFLSRNVN---EGFSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH 196
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-196 |
8.37e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVpkLRQVIGCVFQDFRLLQQKTV 97
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YDNV---AFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETS 174
Cdd:PRK10982 91 MDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEV 170
|
170 180
....*....|....*....|..
gi 15610239 175 RDIMDLLERINRTGTTVLMATH 196
Cdd:PRK10982 171 NHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-196 |
1.19e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRgrhvpklRQVIGCVFQDFRLLQQKTVY 98
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 99 DNVAFALEVIGKRTdainrVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIM 178
Cdd:PRK13541 89 ENLKFWSEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*...
gi 15610239 179 DLLERINRTGTTVLMATH 196
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSH 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-191 |
1.28e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 21 DINVKIDKGEFVFLIGPSGSGKSTFMRLLlAAETPTSGDVRvSKFHVNKLRgrHVPK--------LR-QVIgcvFQDFRL 91
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRL-TKPAKGKLF--YVPQrpymtlgtLRdQII---YPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 -LQQKTVYDNVAFALEVIGKRTDAINRvvpevleTVGLSGKANRLpDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:TIGR00954 543 dMKRRGLSDKDLEQILDNVQLTHILER-------EGGWSAVQDWM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|.
gi 15610239 171 PETSRDIMDLLERINRTGTTV 191
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSV 635
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-227 |
1.32e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 28 KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnklrgrHVPKLRQVI----GCVFQD-FRLLQQKTV----- 97
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------------EEPSWDEVLkrfrGTELQDyFKKLANGEIkvahk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 --YdnVAFALEVI-GKRTDAINRV-----VPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNL 169
Cdd:COG1245 166 pqY--VDLIPKVFkGTVRELLEKVdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15610239 170 DP----ETSRDIMDLLErinrTGTTVLMATHDHHIVDSMRQrVVELSLGrlvrdeQRGVYGM 227
Cdd:COG1245 244 DIyqrlNVARLIRELAE----EGKYVLVVEHDLAILDYLAD-YVHILYG------EPGVYGV 294
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-219 |
1.63e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLlaaetptSG-------------DVRVSKFHvnklrgrhvpKLRQ---- 80
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGvyphgsyegeilfDGEVCRFK----------DIRDseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 --VIgcVFQDFRLLQQKTVYDNVAFALEvIGKRT----DAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFV 154
Cdd:NF040905 79 giVI--IHQELALIPYLSIAENIFLGNE-RAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATH----------------DHHIVDSMRQRVVELSLGRLVR 218
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHklneirrvadsitvlrDGRTIETLDCRADEVTEDRIIR 235
|
.
gi 15610239 219 D 219
Cdd:NF040905 236 G 236
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
95-202 |
2.73e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.08 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 95 KTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQ---RVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:pfam13304 193 KLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHP 272
|
90 100 110
....*....|....*....|....*....|.
gi 15610239 172 ETSRDIMDLLERINRTGTTVLMATHDHHIVD 202
Cdd:pfam13304 273 KLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-216 |
3.51e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARP------------------ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSG--DVR 61
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGtvDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 62 VSKFHVNKLRGrhvpklrqvigcvfqdfrLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSG 141
Cdd:PRK13545 85 GSAALIAISSG------------------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 142 GEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK13545 147 GMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-202 |
4.53e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 28 KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR--VSKFHVnklrgrhvpkLRQVIGCVFQD-FRLLQQKTV------- 97
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeePSWDEV----------LKRFRGTELQNyFKKLYNGEIkvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 98 YdnVAFALEVI-GKRTDAINRV-----VPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDP 171
Cdd:PRK13409 168 Y--VDLIPKVFkGKVRELLKKVdergkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|....*
gi 15610239 172 ----ETSRDIMDLLErinrtGTTVLMATHDHHIVD 202
Cdd:PRK13409 246 rqrlNVARLIRELAE-----GKYVLVVEHDLAVLD 275
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-214 |
6.60e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 133 NRLPDELSGGEQQRVAIARAFVNR--PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVdSMRQRVVE 210
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIID 549
|
....
gi 15610239 211 LSLG 214
Cdd:PRK00635 550 IGPG 553
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-203 |
7.26e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSsaRPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKfhvnklrgrhvpklrq 80
Cdd:PRK10636 312 LLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK---------------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 viGCVFQDFRLLQqktvydnvafaLEVIgkRTDA-----INRVVPEVLET--------VGLSG-KANRLPDELSGGEQQR 146
Cdd:PRK10636 374 --GIKLGYFAQHQ-----------LEFL--RADEsplqhLARLAPQELEQklrdylggFGFQGdKVTEETRRFSGGEKAR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 147 VAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLerINRTGTTVLMaTHDHHIVDS 203
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVV-SHDRHLLRS 492
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-206 |
9.38e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 23 NVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDvRVSKF-HVNKLRgrhVPKLRQVIGCVFQDFR--LLQQKTvYD 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFsHITRLS---FEQLQKLVSDEWQRNNtdMLSPGE-DD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 100 NVAFALEVIGKRTDAINRVVpEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMD 179
Cdd:PRK10938 98 TGRTTAEIIQDEVKDPARCE-QLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180
....*....|....*....|....*...
gi 15610239 180 LLERINRTGTT-VLMATHDHHIVDSMRQ 206
Cdd:PRK10938 177 LLASLHQSGITlVLVLNRFDEIPDFVQF 204
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-212 |
1.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 136 PDELSGG--EQ----QRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRtGTTVLMATHDHHIVDSMRQ--- 206
Cdd:COG4717 556 VEELSRGtrEQlylaLRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAK-GRQVIYFTCHEELVELFQEega 634
|
....*.
gi 15610239 207 RVVELS 212
Cdd:COG4717 635 HVIELE 640
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-211 |
1.54e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 10 QYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRV----SKFHVNK-LRGRHVPKLRQVIGC 84
Cdd:PRK10636 8 QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwQLAWVNQeTPALPQPALEYVIDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 85 VfQDFRLLQQKTVYDNV---AFALEVIGKRTDAIN-----RVVPEVLETVGLSGKANRLP-DELSGGEQQRVAIARAFVN 155
Cdd:PRK10636 88 D-REYRQLEAQLHDANErndGHAIATIHGKLDAIDawtirSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 156 RPLVLLADEPTGNLDpetsRDIMDLLERI--NRTGTTVLMaTHDHHIVDSMRQRVVEL 211
Cdd:PRK10636 167 RSDLLLLDEPTNHLD----LDAVIWLEKWlkSYQGTLILI-SHDRDFLDPIVDKIIHI 219
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-226 |
1.70e-06 |
|
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: 46.80 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 26 IDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDvrvskfhvnklrgrhvpklrqvigcvfqdfrllqqktvydnvafal 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN---------------------------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 106 evigkrtDAINRVVPEVletvglsgKANRLpdELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE----TSRDIMDLL 181
Cdd:cd03222 56 -------DEWDGITPVY--------KPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLS 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15610239 182 ERINRtgtTVLMATHDHHIVDSMRQRVVelslgrlVRDEQRGVYG 226
Cdd:cd03222 119 EEGKK---TALVVEHDLAVLDYLSDRIH-------VFEGEPGVYG 153
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-217 |
1.80e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 1 MITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKLRQ 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 81 VIGCVFQDFRLLQqktvyDNVAFALEVIGKRTD-----AINRV-VPEVLE--TVGLSGKANRLPDELSGGEQQRVAIARA 152
Cdd:PLN03232 1311 VLSIIPQSPVLFS-----GTVRFNIDPFSEHNDadlweALERAhIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 153 FVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSmrQRVVELSLGRLV 217
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC--DKILVLSSGQVL 1448
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
16-184 |
2.78e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 16 RPALDDINVKIDKGefVFLI-GPSGSGKSTF---MRLLLAAETPTSGDVRVSKFHVNKLRGR------HVPKLRQVI--- 82
Cdd:COG0419 11 RSYRDTETIDFDDG--LNLIvGPNGAGKSTIleaIRYALYGKARSRSKLRSDLINVGSEEASvelefeHGGKRYRIErrq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 83 GcVFQDFRLLQQKTVYDNVA--FALEVIGKRTDAINRVVPEVLETVGLSGKANRL-------------PDELSGGEQQRV 147
Cdd:COG0419 89 G-EFAEFLEAKPSERKEALKrlLGLEIYEELKERLKELEEALESALEELAELQKLkqeilaqlsgldpIETLSGGERLRL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 15610239 148 AIARAfvnrpLVLLADepTGNLDPETSRDIMDLLERI 184
Cdd:COG0419 168 ALADL-----LSLILD--FGSLDEERLERLLDALEEL 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-217 |
2.92e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 2 ITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLrgrHVPKLRQV 81
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 82 IGCVFQDFRLLQqktvyDNVAFALEVIGKRTDAinrVVPEVLE-----------TVGLSGKANRLPDELSGGEQQRVAIA 150
Cdd:PLN03130 1315 LGIIPQAPVLFS-----GTVRFNLDPFNEHNDA---DLWESLErahlkdvirrnSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610239 151 RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSmrQRVVELSLGRLV 217
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC--DRILVLDAGRVV 1451
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
138-216 |
3.59e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 3.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 138 ELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-177 |
6.04e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKS----TFMRLLlaaETpTSGDVRVSkfhvnklrGRHVP-----KLRQVIGCVFQDf 89
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKStlllTFMRMV---EV-CGGEIRVN--------GREIGayglrELRRQFSMIPQD- 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 90 RLLQQKTVYDNV-AF----------ALEVIGKRtdaiNRVVPEV--LETVGLSGKANrlpdeLSGGEQQRVAIARAFVNR 156
Cdd:PTZ00243 1393 PVLFDGTVRQNVdPFleassaevwaALELVGLR----ERVASESegIDSRVLEGGSN-----YSVGQRQLMCMARALLKK 1463
|
170 180
....*....|....*....|..
gi 15610239 157 -PLVLLADEPTGNLDPETSRDI 177
Cdd:PTZ00243 1464 gSGFILMDEATANIDPALDRQI 1485
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-197 |
7.64e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 18 ALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVR----VSKFHVNK-LRGrhvpklrqvigcvfqdfrll 92
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngeVSVIAISAgLSG-------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 qQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPE 172
Cdd:PRK13546 99 -QLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*
gi 15610239 173 TSRDIMDLLERINRTGTTVLMATHD 197
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
139-219 |
1.28e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.59 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 139 LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVR 218
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
.
gi 15610239 219 D 219
Cdd:TIGR02633 484 D 484
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
32-209 |
3.40e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.41 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 32 VFLI-GPSGSGKSTF---MRLLLAAETPTSGDVRVSKFHVNK-----------LRGRHVPKLRQVIGCVFQDFR---LLQ 93
Cdd:cd03279 30 LFLIcGPTGAGKSTIldaITYALYGKTPRYGRQENLRSVFAPgedtaevsftfQLGGKKYRVERSRGLDYDQFTrivLLP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 94 QktvydnvafalevigkrtdainrvvpevletvglsGKANRL----PDELSGGEQQRVAIARAFVNRPLV---------- 159
Cdd:cd03279 110 Q-----------------------------------GEFDRFlarpVSTLSGGETFLASLSLALALSEVLqnrggarlea 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15610239 160 LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVV 209
Cdd:cd03279 155 LFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLE 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-217 |
6.27e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 22 INVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvnkLRGRHVPkLRQVIGCVFQDFRL---------- 91
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY--------LDGKPID-IRSPRDAIRAGIMLcpedrkaegi 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 92 LQQKTVYDNVA--------FALEVIGKRTDA------INRvvpevletvgLSGK---ANRLPDELSGGEQQRVAIARAFV 154
Cdd:PRK11288 343 IPVHSVADNINisarrhhlRAGCLINNRWEAenadrfIRS----------LNIKtpsREQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 155 NRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLV 217
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
139-216 |
8.09e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 8.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 139 LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRL 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-201 |
8.58e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.08 E-value: 8.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 139 LSGGEQQRVAIARAFVNR---PLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIV 201
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
139-213 |
1.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 139 LSGGEqqRVAIARAFV---------NRPLVLLaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMrQRVV 209
Cdd:PRK03918 789 LSGGE--RIALGLAFRlalslylagNIPLLIL-DEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAA-DYVI 864
|
....
gi 15610239 210 ELSL 213
Cdd:PRK03918 865 RVSL 868
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
99-170 |
1.90e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 99 DNVAFALEVIGKRTDAINRVVPEVLETVGLSGKA------NRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLD 170
Cdd:PLN03073 299 DAVSQRLEEIYKRLELIDAYTAEARAASILAGLSftpemqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
139-208 |
3.90e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 3.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15610239 139 LSGGEQQRVAIARAFVNRPLV--------LLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHdhhiVDSMRQRV 208
Cdd:PRK10246 950 LSGGESFLVSLALALALSDLVshktridsLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISH----VEAMKERI 1023
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-211 |
7.99e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 7.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610239 139 LSGGEQQRVAIAR---AFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVdSMRQRVVEL 211
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLEL 884
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
139-193 |
1.07e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15610239 139 LSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLM 193
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-211 |
1.25e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 19 LDDINVKIDKGE-FVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIgCVFQDFRLL----- 92
Cdd:COG3950 14 FEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLI-LYYGTSRLLldgpl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 93 -----------QQKTVYDN---------------VAFALEVIGKRTD-----------AINRVVPEVlETVGLSGKANRL 135
Cdd:COG3950 93 kklerlkeeyfSRLDGYDSlldedsnlreflewlREYLEDLENKLSDeldekleavreALNKLLPDF-KDIRIDRDPGRL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 136 -----------PDELSGGEQQRVAIA--------------RAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINrTGTT 190
Cdd:COG3950 172 vildkngeelpLNQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIF-PNIQ 250
|
250 260
....*....|....*....|.
gi 15610239 191 VLMATHDHHIVDSMRQRVVEL 211
Cdd:COG3950 251 FIVTTHSPLILSSLEDEEVIV 271
|
|
| COG3378 |
COG3378 |
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons]; |
31-75 |
1.48e-03 |
|
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];
Pssm-ID: 442605 [Multi-domain] Cd Length: 403 Bit Score: 39.15 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 31 FVFLIGPSGSGKSTFMRLLLA------AETPTSGDVRVSKFHVNKLRGRHV 75
Cdd:COG3378 145 FFFLYGPGGNGKSTFLNLLTAllgkdnASSASLETLTENRFDLARLKGKRL 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
80-202 |
1.49e-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: 39.23 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 80 QVIGCVFQDFrllQQKTVYDNVAF--ALEVIGKRTDAINRVVPEVLE------TVGLSG-KANRLPDELSGGEQQRVAIA 150
Cdd:TIGR00630 424 TVGGKSIADV---SELSIREAHEFfnQLTLTPEEKKIAEEVLKEIRErlgfliDVGLDYlSLSRAAGTLSGGEAQRIRLA 500
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610239 151 R----AFVNRPLVLlaDEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDH-------HIVD 202
Cdd:TIGR00630 501 TqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEdtiraadYVID 561
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-57 |
1.91e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15610239 20 DDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTS 57
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
32-82 |
3.37e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 36.52 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15610239 32 VFLIGPSGSGKSTFMRLLLAAEtptsGDVRVSKfhvNKLRGRHVPKLRQVI 82
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEEL----GAVRLSS---DDERKRLFGEGRPSI 45
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-74 |
4.63e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 4.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15610239 28 KGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRvskfhvNKL-RGRH 74
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS------EKLgRGRH 125
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
138-183 |
7.87e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.52 E-value: 7.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610239 138 ELSGGEQQR---VAIARAFV--------NRP---LVLLaDEPTGNLDPETSRDIMDLLER 183
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegRPPaprLVFL-DEAFAKLDEENIRTALELLRA 90
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
137-196 |
8.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 8.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15610239 137 DELSGGEQQ------RVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGT---TVLMATH 196
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipQVIMISH 868
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-44 |
9.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 9.11e-03
10 20
....*....|....*....|....*.
gi 15610239 19 LDDINVKIDKGEFVFLIGPSGSGKST 44
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
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