|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
2.93e-136 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 380.94 E-value: 2.93e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPqYRHLELNQGFLSEVEDYGR 224
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMP-KRVLELEDGRLVRDEARGV 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
3.58e-121 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 343.01 E-value: 3.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPqYRHLELNQGFL 216
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRS-YRMLTLSDGHL 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
1.04e-109 |
|
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: 313.80 E-value: 1.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPqYRHLELNQG 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVA-HRVIILDDG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-216 |
3.07e-93 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 271.97 E-value: 3.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRpQYRHLELNQGFL 216
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTT-RHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-196 |
2.31e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 252.27 E-value: 2.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG---RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFL 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RR-NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 157 TLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHD 196
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-202 |
1.88e-84 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 249.71 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGR---QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKD-IPFL 77
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGLVNT 202
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAEY 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-200 |
1.99e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 231.12 E-value: 1.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ---ALQKVDFHLKRGEMafLG--GHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIP 75
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtALDDVSLTIEKGEI--FGiiGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVV 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-200 |
2.18e-70 |
|
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: 214.75 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ---ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFL 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVV 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-200 |
1.50e-69 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 216.21 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGR---QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFL 77
Cdd:PRK11153 1 MIELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVV 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-214 |
3.37e-65 |
|
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: 201.41 E-value: 3.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipaKDIPFLRRNI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQ--DHRLLMDrSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:COG1122 78 GLVFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVntrPQY--RHLELNQG 214
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLV---AELadRVIVLDDG 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-199 |
6.08e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.44 E-value: 6.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNV---ALPMR------IESISENEiKRRVSAALDKTGLLDKA--RClpSQLSGGEQQRVGIA 149
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagRLGRTstwrslLGLFPPED-RERALEALERVGLADKAyqRA--DQLSGGQQQRVAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGL 199
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
4.06e-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: 202.64 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRN 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 161 ADEPTGNLDPELSNR----VLRLFEEFnraGVTIILATHD 196
Cdd:COG3842 159 LDEPLSALDAKLREEmreeLRRLQREL---GITFIYVTHD 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
1.13e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.39 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYR---GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipakdipfL 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 158 LLLADEPTGNLDP----ELSNRVLRLFEEFNRagvTIILATHDI 197
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRLWQETGK---TVLFVTHDV 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-197 |
1.68e-63 |
|
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: 197.51 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRR 79
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEiLAIIGG-SGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIES-ISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLREHTdLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 159 LLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDL 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-198 |
5.18e-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: 195.98 E-value: 5.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITrIPAKDIPFLRRN 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL-PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIG 198
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMG 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-200 |
8.28e-61 |
|
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: 190.47 E-value: 8.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNV---ALPMR--IESI----SENEiKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAV 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRstWRSLfglfPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLA 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-197 |
8.91e-61 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 189.65 E-value: 8.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEE-FNRAGVTIILATHDI 197
Cdd:cd03259 155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQ 191
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
3.29e-59 |
|
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: 185.36 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 3 KFQQVSKAY-RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQ--DHRLLMDRsIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03225 78 GLVFQnpDDQFFGPT-VEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPQyRHLELNQG 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELAD-RVIVLEDG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
1.65e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 187.97 E-value: 1.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrR 79
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEfLVLLG-PSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDK---TGLLDKarcLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELlglEDLLDR---KPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 157 TLLLADEPTGNLDPELsnRV-LR--LFEEFNRAGVTIILATHD 196
Cdd:COG3839 153 KVFLLDEPLSNLDAKL--RVeMRaeIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-198 |
6.25e-58 |
|
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: 182.34 E-value: 6.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITrIPAKDIPFLRRNI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVAL-PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIG 198
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-197 |
1.16e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 182.19 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEM-AFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIfGLLG-PNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYL 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-199 |
3.16e-57 |
|
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: 181.09 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQA---LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIP----AKd 73
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 74 ipFLRRNIGIVFQDHRLLMDRSIFDNVALPMriESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV 153
Cdd:COG4181 87 --LRARHVGFVFQSFQLLPTLTALENVMLPL--ELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGL 199
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPAL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-200 |
4.19e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 188.57 E-value: 4.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAY----RGGRQALQKVDFHLKRGEmaFLG--GHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDI 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGE--TLGlvGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 75 PFLRRNIGIVFQDHRLLMD--RSIFDNVALPMRI-ESISENEIKRRVSAALDKTGL-LDKARCLPSQLSGGEQQRVGIAR 150
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNprMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVV 468
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-196 |
1.05e-56 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 179.74 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 162 DEPTGNLDPEL-SNRVLRLFEEFNRAGVTIILATHD 196
Cdd:cd03300 155 DEPLGALDLKLrKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-197 |
2.32e-56 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 178.43 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGR---QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflr 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 rnIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 159 LLADEPTGNLDP----ELSNRVLRLFEEfnrAGVTIILATHDI 197
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDI 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-197 |
6.21e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 177.69 E-value: 6.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEiLAIIGP-SGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESI-SENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDL 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-200 |
2.69e-55 |
|
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: 176.72 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNV---------ALPMRIESISENEiKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARA 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLA 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-197 |
2.67e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 170.66 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGL-----LDKarcLPSQLSGGEQQRVGIARAVVNR 155
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeeyRDR---YPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 156 PTLLLADEPTGNLDP----ELSNRVLRLFEEFNRagvTIILATHDI 197
Cdd:COG1125 155 PPILLMDEPFGALDPitreQLQDELLRLQRELGK---TIVFVTHDI 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-200 |
4.76e-52 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 167.68 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGR---QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFL 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMD--RSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCL---PSQLSGGEQQRVGIARAV 152
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryPHELSGGQRQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVV 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-200 |
1.66e-51 |
|
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: 166.90 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG---RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfL 77
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMD--RSIFDNVALPMRIESISEneIKRRVSAALDKTGL----LDKarcLPSQLSGGEQQRVGIARA 151
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHGLPD--REERIAELLEQVGLppsfLDR---YPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVV 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-197 |
2.63e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 166.86 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEM-AFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDI-TRIPAKDipflrR 79
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELvALLGP-SGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 160 LADEPTGNLD----PELsNRVLR-LFEEFnraGVTIILATHDI 197
Cdd:COG1118 156 LLDEPFGALDakvrKEL-RRWLRrLHDEL---GGTTVFVTHDQ 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
3.79e-50 |
|
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: 160.12 E-value: 3.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRRNIGIVFQDHRLLMDRSIF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD---ERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 98 DNVALPMRIESISENEIKRRVSAALDKTGLLDKA----RCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-196 |
7.61e-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: 162.51 E-value: 7.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrRNI 81
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRI----ESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 158 LLLADEPTGNLDP----ELSNRVLRLFEEFnraGVTIILATHD 196
Cdd:cd03296 157 VLLLDEPFGALDAkvrkELRRWLRRLHDEL---HVTTVFVTHD 196
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-196 |
8.10e-50 |
|
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: 161.24 E-value: 8.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN-IGI 83
Cdd:TIGR03608 2 KNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190
....*....|....*....|....*....|...
gi 1327051661 164 PTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-196 |
1.48e-49 |
|
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: 160.88 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrRNI 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAA---LDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVaelLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 159 LLADEPTGNLDPELsnRVlRLFEEFNR----AGVTIILATHD 196
Cdd:cd03301 152 FLMDEPLSNLDAKL--RV-QMRAELKRlqqrLGTTTIYVTHD 190
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-198 |
1.83e-49 |
|
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: 161.19 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLI-----CAIERPTDGRVWFNDHDItRIPAKDIPF 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDI-YDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQdHRLLMDRSIFDNVALPMRIESISEN-EIKRRVSAALDKTGLLD--KARCLPSQLSGGEQQRVGIARAVV 153
Cdd:cd03260 79 LRRRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAgVTIILATHDIG 198
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQ 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-203 |
4.01e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.64 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItRIPAKDIPFLRRN 80
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL-PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGL---VNTR 203
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFaekVASR 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-199 |
5.58e-49 |
|
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: 160.59 E-value: 5.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL-------PMRIESISENEIkrrVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV 153
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGL 199
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNL 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-197 |
7.41e-49 |
|
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: 160.16 E-value: 7.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDK--ARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 160 LADEPTGNLDP----ELSNRVLRLFEEFNRagvTIILATHDI 197
Cdd:cd03295 158 LMDEPFGALDPitrdQLQEEFKRLQQELGK---TIVFVTHDI 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-200 |
1.27e-48 |
|
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: 157.35 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpAKDIPFLRRNI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPmriesiseneikrrvsaaldktglldkarclpsqLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFN-RAGVTIILATHDIGLV 200
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEA 164
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-218 |
5.84e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 157.67 E-value: 5.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 6 QVSKAYRGGR---QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLR-RNI 81
Cdd:PRK11629 10 NLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLvnTRPQYRHLELNQGFLSE 218
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQL--AKRMSRQLEMRDGRLTA 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
1.68e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.05 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAkdiPFLRRNI 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPP---PEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDrSIFDNVALPMRIESISENEikRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLppdiLDKP---VERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDIGLVNtRPQYRHLELNQG 214
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIE-RVADRVLTLEAG 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-196 |
4.79e-46 |
|
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: 153.57 E-value: 4.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN-IGIVFQDHRLLMDRS 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP----E 171
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180
....*....|....*....|....*
gi 1327051661 172 LSNRVLRLFEEFNRagvTIILATHD 196
Cdd:cd03294 199 MQDELLRLQAELQK---TIVFITHD 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-200 |
6.51e-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: 152.21 E-value: 6.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflRRNIGIV 84
Cdd:cd03219 4 RGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIFDNVALPMRIESIS----------ENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-196 |
2.83e-45 |
|
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: 151.84 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEmaFLG--GHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIP 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGE--FVAiiGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQ--DHRLLMDrSIFDNVAL-PMRIeSISENEIKRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGI 148
Cdd:TIGR04521 79 DLRKKVGLVFQfpEHQLFEE-TVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHD 196
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHS 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-196 |
2.91e-45 |
|
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: 160.00 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-ALQKVDFHLKRGEM-AFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRR 79
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERvAIVGR-SGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLlMDRSIFDNVALPMriESISENEIKRrvsaALDKTGLLDKARCLP-----------SQLSGGEQQRVGI 148
Cdd:COG2274 550 QIGVVLQDVFL-FSGTIRENITLGD--PDATDEEIIE----AARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHD 196
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHR 669
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-197 |
4.35e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.91 E-value: 4.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrgGRQALQkVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRI-PAKdipflrR 79
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALpPAE------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIE-SISENEiKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV-NRPT 157
Cdd:COG3840 72 PVSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 158 LLLaDEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:COG3840 151 LLL-DEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDP 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-214 |
4.84e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipakdipfLRRN 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQdhRLLMDR----SIFDNVAL----PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAV 152
Cdd:COG1121 77 IGYVPQ--RAEVDWdfpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVntrPQY--RHLELNQG 214
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAV---REYfdRVLLLNRG 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-199 |
5.08e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.16 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDI---TRIPAKDIPFLR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHRLLMDRSIFDN-VALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGL 199
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-199 |
1.04e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDH--DITRIP-AKDIPFLR 78
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHRLLMDRSIFDN-VALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGL 199
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEV 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-196 |
1.06e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 153.18 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNI 81
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHD 196
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-200 |
1.60e-44 |
|
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: 146.76 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHrLLMDRSIFDNValpmriesiseneikrrvsaaldktglldkarclpsqLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03228 78 IAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHDIGLV 200
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTI 158
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
5.13e-44 |
|
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: 153.91 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGR-QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPT---DGRVWFNDHDITRIPAKDipf 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQDHRL-LMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLVNTRPQyRHLELNQGFLSE 218
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIAD-RVVVMDDGRIVE 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-200 |
1.31e-43 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 147.11 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflRRN 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA--RLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIES---------------ISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 146 VGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLV 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-200 |
9.77e-43 |
|
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: 146.35 E-value: 9.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGR---QALQKVDFHLKRGEMafLG--GHSGAGKSTLLKLICAIERP---TDGRVWFNDHDITRIPAK 72
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvKAVDGVSFDVRRGET--LGlvGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 73 DIPFLR-RNIGIVFQDHrllMD-----RSIFDNVALPMRI-ESISENEIKRRVSAALDKTGLLDKARCL---PSQLSGGE 142
Cdd:COG0444 79 ELRKIRgREIQMIFQDP---MTslnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327051661 143 QQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVV 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-196 |
1.56e-42 |
|
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: 143.63 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNIGIVFQDHRLLMDRSIF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 98 DNVALPMRIESISENEIKRRV---SAALDKTGLLDKArclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSN 174
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVleiAEMLGIDHLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180
....*....|....*....|...
gi 1327051661 175 RVLRLFEEFNRA-GVTIILATHD 196
Cdd:cd03299 167 KLREELKKIRKEfGVTVLHVTHD 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-201 |
1.75e-42 |
|
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: 140.84 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 3 KFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdIPFLRRNIG 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQdhrllmdrsifdnvalpmriesiseneikrrvsaaldktglldkarclpsqLSGGEQQRVGIARAVVNRPTLLLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 163 EPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVN 201
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAE 144
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-197 |
3.70e-42 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 140.61 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEiYGLLG-PNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE----VKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNValpmriesiseneikrrvsaaldktglldkarclpsQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIL 155
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-200 |
6.00e-42 |
|
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: 140.26 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNIGIV 84
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQdhrllmdrsifdnvalpmriesiseneikrrvsaALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEP 164
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 165 TGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLA 161
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-196 |
1.11e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 140.69 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSkAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERP---TDGRVWFNDHDITRIPAkdipfL 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-----E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRLLMDRSIFDNVALPMRiESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRL-FEEFNRAGVTIILATHD 196
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHD 193
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-196 |
1.76e-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: 143.40 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 33 LGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNIGIVFQDHRLLMDRSIFDNVALPMRIESISEN 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 113 EIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV-LRLFEEFNRAGVTII 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITFV 155
|
....*
gi 1327051661 192 LATHD 196
Cdd:TIGR01187 156 FVTHD 160
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-196 |
2.15e-41 |
|
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: 144.02 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNI 81
Cdd:TIGR03265 5 LSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-----KRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 162 DEPTGNLDPELsnRVlRLFEEF----NRAGVTIILATHD 196
Cdd:TIGR03265 159 DEPLSALDARV--RE-HLRTEIrqlqRRLGVTTIMVTHD 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-197 |
2.18e-41 |
|
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: 140.02 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRqALQKVDFHLKRGEMAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRNI 81
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMYGLLG-PNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNrAGVTIILATHDI 197
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIV 189
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-197 |
2.30e-41 |
|
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: 140.20 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEiFGLLGP-NGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYM 192
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-200 |
3.21e-41 |
|
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: 140.38 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEV 195
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-196 |
3.44e-41 |
|
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: 139.15 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAyRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:COG4133 2 MLEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEikRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-195 |
3.80e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEM-AFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETvALVG-PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHrLLMDRSIFDNVALPMriESISENEIKrrvsAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:COG1132 416 IGVVPQDT-FLFSGTIRENIRYGR--PDATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAH 533
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
3.84e-41 |
|
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: 147.21 E-value: 3.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDrSIFDNVALPMRieSISENEIKrrvsAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIAR 150
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLGRP--DASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHDIGLVNtrpQY-RHLELNQGFLSEVEDY 222
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA---QAdRILVLDDGRIVEQGTH 555
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-197 |
8.03e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 140.26 E-value: 8.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDiTRIPaKDIPFLRRN 80
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDE-ENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQ--DHRLLmdRSIF-DNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:TIGR04520 79 VGMVFQnpDNQFV--GATVeDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDI 197
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDM 197
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
8.40e-41 |
|
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: 137.94 E-value: 8.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFN----DHDitripAKDIPFLRRNIGIVFQ 86
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgeplDYS-----RKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 D-HRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:TIGR01166 76 DpDDQLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATHDIGL 199
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
1.61e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 139.23 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ---ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRiPAKDipfl 77
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 rRniGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG4525 78 -R--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 158 LLLADEPTGNLDP-------ELsnrVLRLfeeFNRAGVTIILATHDI 197
Cdd:COG4525 155 FLLMDEPFGALDAltreqmqEL---LLDV---WQRTGKGVFLITHSV 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-200 |
3.32e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 138.67 E-value: 3.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItRIPAKDIPFLRRN 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHrllmDRSIF-----DNVAL-PMRIeSISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:PRK13639 80 VGIVFQNP----DDQLFaptveEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLV 200
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-218 |
5.74e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 136.83 E-value: 5.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLR-RNIGIVFQDHRLLMDRSI 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 177 LRLFEEFNRA-GVTIILATHDIGLVnTRPQyRHLELNQGFLSE 218
Cdd:PRK10584 186 ADLLFSLNREhGTTLILVTHDLQLA-ARCD-RRLRLVNGQLQE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-197 |
1.19e-39 |
|
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: 137.91 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYrGGRQALQKVDFHLKRGE-MAFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRNIGIVFQD 87
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEvFGFLGP-NGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRK----VRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 HRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGN 167
Cdd:TIGR01188 75 ASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190
....*....|....*....|....*....|
gi 1327051661 168 LDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYM 184
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-196 |
1.38e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 142.98 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRG-GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG4987 334 LELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDrSIFDN--VALPmrieSISENEIKrrvsAALDKTGLLDKARCLP-----------SQLSGGEQQRVG 147
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENlrLARP----DATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 148 IARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHD 196
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHR 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-200 |
1.68e-39 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 134.97 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 3 KFQQVSKAYrGGRQALQKVDFHLKRGEmaFLG--GHSGAGKSTLLKLICAIERPTDGRVwfndhditRIPAKDIPFLRRN 80
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGE--FLAivGPNGAGKSTLLKAILGLLKPTSGSI--------RVFGKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQdhRLLMDR----SIFDNVAL----PMRIESISENEIKRRVSAALDKTGLLDKA-RCLpSQLSGGEQQRVGIARA 151
Cdd:cd03235 70 IGYVPQ--RRSIDRdfpiSVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELAdRQI-GELSGGQQQRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLV 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-196 |
5.18e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.52 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrRNI 81
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVA-----LPMRiESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAfgltvLPRR-ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 157 TLLLADEPTGNLDP----ELSNRVLRLFEEFNragVTIILATHD 196
Cdd:PRK10851 156 QILLLDEPFGALDAqvrkELRRWLRQLHEELK---FTSVFVTHD 196
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
9-198 |
1.58e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.77 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKD----------IPFLR 78
Cdd:COG4598 16 KSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqLQRIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHRLLMDRSIFDNVAL-PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG4598 95 TRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIG 198
Cdd:COG4598 175 VMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMG 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-196 |
1.87e-38 |
|
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: 132.94 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAY----RGGRQ--ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDH----DITRIP 70
Cdd:COG4778 4 LLEVENLSKTFtlhlQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 71 AKDIPFLRRN-IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALdktglldkAR-CLPSQL--------SG 140
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELL--------ARlNLPERLwdlppatfSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 141 GEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
2.83e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 133.72 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpflRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSI--FDnVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK13648 84 HIGIVFQNPDNQFVGSIvkYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDL 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
6.95e-38 |
|
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: 137.80 E-value: 6.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQdHRLLMDRSIFDNVALPMRieSISENEIKRrvsaALDKTGLLDKARCLP-----------SQLSGGEQQRVGIAR 150
Cdd:TIGR02857 399 AWVPQ-HPFLFAGTIAENIRLARP--DASDAEIRE----ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRaGVTIILATHDIGLV 200
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-209 |
9.63e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.70 E-value: 9.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDH------R 89
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPyaslnpR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LlmdrSIFDNVALPMRIESI-SENEIKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGN 167
Cdd:COG4608 112 M----TVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 168 LDPELSNRVLRLFEEF-NRAGVTIILATHDIGLVntrpqyRHL 209
Cdd:COG4608 188 LDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVV------RHI 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-197 |
1.09e-37 |
|
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: 130.70 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-ALQKVDFHLKRGE-MAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRR 79
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEiFGLLG-HNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA----ARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHDI 197
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSM 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-196 |
4.29e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.04 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdiPFlRRN 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP----PY-QRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 161 ADEPTGNLDPELSNRV-LRLFEEFNRAGVTIILATHD 196
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHD 209
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-198 |
5.87e-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: 129.72 E-value: 5.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKlicAIERPTD--------GRVWFNDHDITRiPAKDIPFLRRNIG 82
Cdd:TIGR00972 10 FYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLR---SLNRMNDlvpgvrieGKVLFDGQDIYD-KKIDVVELRRRVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQdHRLLMDRSIFDNVALPMRIESI-SENEIKRRVSAALDKTGLL----DKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:TIGR00972 86 MVFQ-KPNPFPMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWdevkDRLHDSALGLSGGQQQRLCIARALAVEPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATHDIG 198
Cdd:TIGR00972 165 VLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQ 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-200 |
1.35e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.04 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYRGG--------RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLR 78
Cdd:PRK10419 9 LSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHRLLMD--RSIFDNVALPMR-IESISENEIKRRVSAALDKTGL----LDKarcLPSQLSGGEQQRVGIARA 151
Cdd:PRK10419 89 RDIQMVFQDSISAVNprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLddsvLDK---RPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDIGLV 200
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLV 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-200 |
2.44e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 128.38 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG--------RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAK 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 73 DIPFLRRNIGIVFQDHRLLMD--RSIFDNVALPMR-IESISENEIKRRVSAALDKTGLLDK-ARCLPSQLSGGEQQRVGI 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNprMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFN-RAGVTIILATHDIGLV 200
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-218 |
2.45e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.16 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKD----------IPFLRRNIG 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQDHRLLMDRSIFDNV-ALPMRIESISENEIKRRVSAALDKTGLLDKARC-LPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVntrpqyRHLE-----LNQGFLSE 218
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFA------RHVSshvifLHQGKIEE 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-196 |
1.98e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.30 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripakDIPFLRRNIGIVFQ 86
Cdd:PRK11432 12 ITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-----HRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 DHRLLMDRSIFDNVALPMRIESISENEIKRRVSAAL---DKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALelvDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 164 PTGNLDPELsNRVLR--LFEEFNRAGVTIILATHD 196
Cdd:PRK11432 163 PLSNLDANL-RRSMRekIRELQQQFNITSLYVTHD 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-197 |
2.08e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.29 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDhdiTRIPAKDipfLRRNIGIVFQ 86
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 D--HRLLMDrSIFDNVALPMRIESISENeikrRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEP 164
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLKELDAGNE----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|...
gi 1327051661 165 TGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-196 |
2.55e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 128.04 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrRN 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAA---LDKTGLLDKArclPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAariLELEPLLDRK---PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 158 LLLADEPTGNLDPELsnRV---LRLFEEFNRAGVTIILATHD 196
Cdd:PRK11650 155 VFLFDEPLSNLDAKL--RVqmrLEIQRLHRRLKTTSLYVTHD 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-195 |
2.64e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdIPFL 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQ--DHRLLmDRSIFDNVALPMRIESISENEIKRRVSAA-----LDKTGLLDKArclPSQLSGGEQQRVGIAR 150
Cdd:PRK13637 82 RKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAmnivgLDYEDYKDKS---PFELSGGQKRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 151 AVVNRPTLLLADEPTGNLDP----ELSNRVLRLFEEFNragVTIILATH 195
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYN---MTIILVSH 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-192 |
2.67e-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: 124.47 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 10 AYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGIVFQDHR 89
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDRSIFDNVALPMRIesISENEIKRRVSAALDK-TGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:cd03224 86 IFPELTVEENLLLGAYA--RRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180
....*....|....*....|....
gi 1327051661 169 DPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILL 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-195 |
2.70e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.53 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 10 AYRGGRQALQKVDFHLKRGE-MAFLGgHSGAGKSTLLK-------LI--CAIErptdGRVWFNDHDItRIPAKDIPFLRR 79
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKvTALIG-PSGCGKSTLLRclnrmndLIpgARVE----GEILLDGEDI-YDPDVDVVELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQdhrllmdR------SIFDNVALPMRIESI-SENEIKRRVSAALDKTGLLD--KARcL---PSQLSGGEQQRVG 147
Cdd:COG1117 93 RVGMVFQ-------KpnpfpkSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevKDR-LkksALGLSGGQQQRLC 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327051661 148 IARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTH 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-197 |
1.51e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.63 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNdhditRIPAKDIpflRRNIGIVFQ 86
Cdd:PRK11247 18 VSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEA---REDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 DHRLLMDRSIFDNVALPMRiesiseNEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 167 NLDP----ELSNRVLRLFEEFnraGVTIILATHDI 197
Cdd:PRK11247 163 ALDAltriEMQDLIESLWQQH---GFTVLLVTHDV 194
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-197 |
1.81e-34 |
|
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: 126.12 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRI-PAKDIPFLRRNIGIVFQDHRLL 91
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP- 170
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPl 163
|
170 180 190
....*....|....*....|....*....|
gi 1327051661 171 ---ELSNRVLRLFEEFNRagvTIILATHDI 197
Cdd:TIGR01186 164 irdSMQDELKKLQATLQK---TIVFITHDL 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-197 |
1.86e-34 |
|
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: 122.57 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRiPAKDipflRRnigIVFQDHRLLMDRSIF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPD----RM---VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 98 DNVALPMR--IESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP----E 171
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgN 152
|
170 180
....*....|....*....|....*.
gi 1327051661 172 LSNRVLRLFEEfnrAGVTIILATHDI 197
Cdd:TIGR01184 153 LQEELMQIWEE---HRVTVLMVTHDV 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-192 |
8.72e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 120.86 E-value: 8.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSkAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRN 80
Cdd:COG0410 3 MLEVENLH-AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESiSENEIKRRVSAALD---KtgLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYElfpR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-195 |
9.08e-34 |
|
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: 120.39 E-value: 9.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDrSIFDNVALPMRieSISENEIKRrvsaALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGAP--LADDERILR----AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITH 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-198 |
2.56e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.24 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGgRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDI-TRIPAKD----IP 75
Cdd:PRK11264 3 AIEVKNLVKKFHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQDHRLLMDRSIFDNVAL-PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIG 198
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-200 |
2.74e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.11 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITrIPAKDIPFLRRN 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQ--DHRLLmDRSIFDNVALPMRIESISENEIKRRVSAALDKTGlLDKARCLPSQ-LSGGEQQRVGIARAVVNRPT 157
Cdd:PRK13636 84 VGMVFQdpDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTG-IEHLKDKPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIV 205
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
3.80e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSkAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG4559 1 MLEAENLS-VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL---PMRIESISENEIkrrVSAALDKTGLLDKA-RCLPsQLSGGEQQRVGIARA----- 151
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVALgraPHGSSAAQDRQI---VREALALVGLAHLAgRSYQ-TLSGGEQQRVQLARVlaqlw 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 152 --VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGL 199
Cdd:COG4559 153 epVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNL 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-200 |
8.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPFLRRNI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQD-HRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK13647 82 GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLA 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-196 |
1.10e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 124.45 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQA---LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFL 77
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RR-NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK10535 84 RReHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 157 TLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-200 |
1.61e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 123.26 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMafLG--GHSGAGKSTL----LKLIcaierPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQD--- 87
Cdd:COG4172 301 AVDGVSLTLRRGET--LGlvGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 ---HRLlmdrSIFDNVALPMRIESI--SENEIKRRVSAALDKTGLLDKARC-LPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:COG4172 374 slsPRM----TVGQIIAEGLRVHGPglSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVV 489
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-195 |
3.19e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.31 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPA-KDIPF 76
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQ-DHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTG----LLDKArclPSQLSGGEQQRVGIARA 151
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGisesLFEKN---PFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-195 |
3.27e-32 |
|
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: 116.44 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 22 DFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflrrnIGIVFQDHRLLMDRSIFDNVA 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-----VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 102 LPmRIESISENEIKR-RVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV-NRPTLLLaDEPTGNLDPELSNRVLRL 179
Cdd:cd03298 93 LG-LSPGLKLTAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVrDKPVLLL-DEPFAALDPALRAEMLDL 170
|
170
....*....|....*..
gi 1327051661 180 FEEFNR-AGVTIILATH 195
Cdd:cd03298 171 VLDLHAeTKMTVLMVTH 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-197 |
3.96e-32 |
|
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: 119.44 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPT------DGRVWFNDHDITRIPAKdipflRRNIGIVFQDHRLLMDR 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlGGEVLQDSARGIFLPPH-----RRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 95 SIFDNVALPMRIESISENEIKR-RVSAALDKTGLLDKArclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELS 173
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFdEVVELLGIGHLLDRR---PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180
....*....|....*....|....*...
gi 1327051661 174 NRVL----RLFEEFNragVTIILATHDI 197
Cdd:COG4148 170 AEILpyleRLRDELD---IPILYVSHSL 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-198 |
4.08e-32 |
|
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: 115.78 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripaKDIPFLRRnI 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRrvsaALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIG 198
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLS 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-196 |
4.70e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipaKDIPFLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQ--DHRLLmDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK13632 84 KIGIIFQnpDNQFI-GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHD 196
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHD 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-209 |
6.60e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.53 E-value: 6.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRG----GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPA-KDIP 75
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQ-DHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGIAR 150
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLadefWEKS---PFELSGGQMRRVAIAG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPQYRHL 209
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYL 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-195 |
8.17e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.17 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI-----ERPTDGRVWFNDHDITRIpakDIPFLRRNIGIVFQD 87
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM---DVIELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 HRLLMDRSIFDNVALPMRIESI--SENEIKRRVSAALDKTGLLDKAR----CLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK14247 91 PNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAgVTIILATH 195
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-195 |
8.35e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRR 79
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEvHALLG-ENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA--QAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVAL---PMRIESISENEIKRRVSAALDKTGL-LDkARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-197 |
9.11e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 116.79 E-value: 9.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLL 91
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDRSIFDNVALPMRIES-ISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP 170
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*...
gi 1327051661 171 ELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:PRK11831 177 ITMGVLVKLISELNSAlGVTCVVVSHDV 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-199 |
9.45e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 9.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAyRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:PRK13548 2 MLEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV------N 154
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNR---AGVTIILatHDIGL 199
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHergLAVIVVL--HDLNL 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-200 |
1.62e-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: 120.17 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKS----TLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLR-RNIGIVFQD 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 --------HRllmdrsIFDNVALPMRI-ESISENEIKRRVSAALDKTGLLDKARCL---PSQLSGGEQQRVGIARAVVNR 155
Cdd:COG4172 101 pmtslnplHT------IGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVV 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-195 |
1.66e-31 |
|
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: 115.02 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDhRLLMDRSIFDNVALpmriesiSENEIKR-RVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:cd03254 80 GVVLQD-TFLFSGTIMENIRL-------GRPNATDeEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHR 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-197 |
1.74e-31 |
|
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: 115.18 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSkAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDG-RVWFNDHDITRIpakDIPFLRR 79
Cdd:COG1119 3 LLELRNVT-VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE---DVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSI----------FDNVALPMRIEsiseNEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIA 149
Cdd:COG1119 79 RIGLVSPALQLRFPRDEtvldvvlsgfFDSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAG-VTIILATHDI 197
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHV 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-195 |
1.81e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.34 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ-----ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpaKDIP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQ--DHRLLMdrSIFD-NVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAV 152
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVA--TIVEeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATH 195
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-200 |
2.62e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.98 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEM-AFLGGHsGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdipflRR 79
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIfGLLGPN-GAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:COG4152 72 RIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELV 192
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
2.85e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDIPF 76
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQ--DHRLLmDRSIFDNVAL-PMRIeSISENEIKRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGIA 149
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLF-EETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLpeelLARS---PFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATH 195
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTH 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-197 |
3.50e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.70 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDIPF 76
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQ-DHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDK-ARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:PRK13641 83 LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNM 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-196 |
3.54e-31 |
|
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: 113.54 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 20 KVDFHLKRGEMAFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDH--DITRIPAkDIPFLRRNIGIVFQDHRLLMDRSIF 97
Cdd:cd03297 16 KIDFDLNEEVTGIFGA-SGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKI-NLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 98 DNVALPMRIESisENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVL 177
Cdd:cd03297 94 ENLAFGLKRKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180
....*....|....*....|...
gi 1327051661 178 ----RLFEEFNragVTIILATHD 196
Cdd:cd03297 172 pelkQIKKNLN---IPVIFVTHD 191
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-195 |
6.44e-31 |
|
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: 113.26 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipaKDIpflrRNI 81
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDL----HKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKrrvsAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:TIGR03740 73 GSLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-202 |
7.48e-31 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 113.35 E-value: 7.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRG-GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRRN 80
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHrLLMDRSIFDNVALPmriesiSENEIKRRVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:cd03252 78 VGVVLQEN-VLFNRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNrAGVTIILATHDIGLVNT 202
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-170 |
1.45e-30 |
|
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: 112.64 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdiPFLRRNI 81
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP----MHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVF--QDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03218 76 GIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170
....*....|.
gi 1327051661 160 LADEPTGNLDP 170
Cdd:cd03218 156 LLDEPFAGVDP 166
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-196 |
2.46e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.13 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflrRNI 81
Cdd:PRK11000 4 VTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAA---LDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVaevLQLAHLLDR---KPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 159 LLADEPTGNLDPELsnRV------LRLFEEFNRagvTIILATHD 196
Cdd:PRK11000 155 FLLDEPLSNLDAAL--RVqmrieiSRLHKRLGR---TMIYVTHD 193
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-197 |
4.71e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpflRRNIGIVFQ--DHRLLm 92
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV---RRQVGMVFQnpDNQFV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPEL 172
Cdd:PRK13635 96 GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180
....*....|....*....|....*.
gi 1327051661 173 SNRVLRLFEEFNR-AGVTIILATHDI 197
Cdd:PRK13635 176 RREVLETVRQLKEqKGITVLSITHDL 201
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-197 |
5.27e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.72 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDhditrIPAKDiPFLRRn 80
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEG-PGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 iGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 161 ADEPTGNLDP----ELSNRVLRLFEEfnrAGVTIILATHDI 197
Cdd:PRK11248 152 LDEPFGALDAftreQMQTLLLKLWQE---TGKQVLLITHDI 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-200 |
7.54e-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: 110.06 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripakdiPFLRRNI 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELV 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-198 |
1.03e-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: 110.50 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDhditRIPAKDIPFLRRNIGIVF-QDHRLLMDRS 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFDNVALPMRIESISENEIKRRV---SAALDKTGLLDK-ARclpsQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPE 171
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLdelSELLDLEELLDTpVR----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*...
gi 1327051661 172 LSNRVLRLFEEFNRA-GVTIILATHDIG 198
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMK 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-200 |
2.28e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 111.54 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERP----TDGRVWFNDHDITRIPAKDI-PFLRRNIGIVFQDHRL 90
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrKIIGREIAMIFQEPSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 91 LMDRS--IFDNValpmrIESISENEI-----------KRRVSAALDKTGLLDKARCL---PSQLSGGEQQRVGIARAVVN 154
Cdd:COG4170 101 CLDPSakIGDQL-----IEAIPSWTFkgkwwqrfkwrKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGLV 200
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-197 |
4.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.89 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGrvwfNDHDIT----RIPAKDIPF 76
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDN----PNSKITvdgiTLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQD-HRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDI 197
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDI 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-195 |
6.58e-29 |
|
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: 108.47 E-value: 6.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRRNI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDrSIFDNVALPMriESISENEIKRRVSAAldktGLLDKARCLPSQ-----------LSGGEQQRVGIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGR--PDATDEEVIEAAKAA----QIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEfNRAGVTIILATH 195
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAH 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-182 |
6.68e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRggRQALQkVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipflRRN 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVALPM----RIESisenEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLnpglKLNA----AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180
....*....|....*....|....*.
gi 1327051661 157 TLLLADEPTGNLDPELSNRVLRLFEE 182
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQ 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-193 |
8.92e-29 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.09 E-value: 8.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRG-GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDhRLLMDRSIFDNVALPMRiesiseNEIKRRVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:cd03251 78 IGLVSQD-VFLFNDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILA 193
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-197 |
9.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.05 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpflRRNIGIVFQD-HRLLMDRSI 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI---RHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180
....*....|....*....|..
gi 1327051661 177 LRLFEEF-NRAGVTIILATHDI 197
Cdd:PRK13650 180 IKTIKGIrDDYQMTVISITHDL 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-195 |
1.06e-28 |
|
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: 105.59 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNI 81
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA--RRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFqdhrllmdrsifdnvalpmriesiseneikrrvsaaldktglldkarclpsQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03216 78 AMVY---------------------------------------------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-193 |
1.54e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.36 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDhRLLMDRSIFDNValpmRI--ESISENEIKRRVSAALDKTGLLDKARCLP-------SQLSGGEQQRVGIARAV 152
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNI----RVgrPDATDEEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILA 193
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-195 |
1.57e-28 |
|
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: 105.76 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQA-LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLmDRSIFDNValpmriesiseneikrrvsaaldktglldkarclpsqLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
2.34e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIP----Akdipf 76
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 lRRNIGIVFQDHrllmdrSIF------DNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIAR 150
Cdd:COG1137 77 -RLGIGYLPQEA------SIFrkltveDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180
....*....|....*....|
gi 1327051661 151 AVVNRPTLLLADEPTGNLDP 170
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDP 169
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-200 |
2.46e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.03 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLLMD-- 93
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDNVALPMRI--ESISENEIKRRVSAALDKTGLLDKA--RcLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD 169
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLinR-YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 170 PELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVV 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-195 |
4.00e-28 |
|
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: 106.47 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAY--RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIcaiER---PTDGRVWFNDHDITRIpakDIPF 76
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDL---NLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQDhRLLMDRSIFDNVALPmRIESISENEIKRRVSAALDK--TGLLDK--ARCLP--SQLSGGEQQRVGIAR 150
Cdd:cd03249 75 LRSQIGLVSQE-PVLFDGTIAENIRYG-KPDATDEEVEEAAKKANIHDfiMSLPDGydTLVGErgSQLSGGQKQRIAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAH 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-200 |
5.65e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.74 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQD--HRLLMD 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDNVALPMRIE-SISENEIKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPE 171
Cdd:PRK11308 109 KKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190
....*....|....*....|....*....|...
gi 1327051661 172 LSNRVLRLF----EEFNRAGVTIilaTHDIGLV 200
Cdd:PRK11308 189 VQAQVLNLMmdlqQELGLSYVFI---SHDLSVV 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-200 |
7.43e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 7.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhdiTRIPAkdipflrRNIGIVFQdhRLLM 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGG-------ARVAYVPQ--RSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSifdnvaLPMRIESISE--------------NEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:NF040873 67 PDS------LPLTVRDLVAmgrwarrglwrrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 159 LLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-197 |
9.78e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 106.22 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDiTRIPAKdIPFLRRN 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSK-LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQD-HRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.66 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRipaKDIPFLRRN 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHrllmDRSIFD-----NVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:PRK13652 80 VGLVFQNP----DDQIFSptveqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDIGLVNTRPQY 206
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADY 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-200 |
1.69e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 105.30 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPFLRRNIGIVFQDHRLL 91
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE---YGDYKYRCKHIRMIFQDPNTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDRSIfdNVA----LPMRIES-ISENEIKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:COG4167 100 LNPRL--NIGqileEPLRLNTdLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 166 GNLDP----ELSNRVLRLFEEFnraGVTIILATHDIGLV 200
Cdd:COG4167 178 AALDMsvrsQIINLMLELQEKL---GISYIYVSQHLGIV 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-193 |
2.46e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRG-GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDhRLLMDRSIFDNVALPmRIESISENEIKRRVSAAldktGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:TIGR02203 408 VALVSQD-VVLFNDTIANNIAYG-RTEQADRAEIERALAAA----YAQDFVDKLPlgldtpigengVLLSGGQRQRLAIA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILA 193
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA 525
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-201 |
3.53e-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: 108.35 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAY----RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPF 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LR----RNIGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRV----SAALDK---TGLLDKarcLPSQLSGGEQQR 145
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVitlkMVGFDEekaEEILDK---YPDELSEGERHR 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 146 VGIARAVVNRPTLLLADEPTGNLDP----ELSNRVLRLFEEFNRagvTIILATHDIGLVN 201
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVL 492
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-192 |
1.39e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.26 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRN 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAlpMRIESISENEIKRRVSAALDKTGLLDKARCLPS-QLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLA--MGGFFAERDQFQERIKWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190
....*....|....*....|....*....|...
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-197 |
1.84e-26 |
|
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: 104.42 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 20 KVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAK-DIPFLRRNIGIVFQDHRLLMDRSIFD 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 99 NVALPMRIESISENEIK-RRVSAALDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVL 177
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180
....*....|....*....|....
gi 1327051661 178 ----RLFEEFNragVTIILATHDI 197
Cdd:TIGR02142 172 pyleRLHAEFG---IPILYVSHSL 192
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-218 |
2.57e-26 |
|
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: 101.83 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFND-----HDITRIPAKDIPFL-RRN 80
Cdd:TIGR02323 9 LSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQLSEAERRRLmRTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHR--LLMDRSIFDNVA-LPMRIESISENEIKRRVSAALDKTGLlDKARC--LPSQLSGGEQQRVGIARAVVNR 155
Cdd:TIGR02323 88 WGFVHQNPRdgLRMRVSAGANIGeRLMAIGARHYGNIRATAQDWLEEVEI-DPTRIddLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGLVNTRPQyRHLELNQGFLSE 218
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRdLGLAVIIVTHDLGVARLLAQ-RLLVMQQGRVVE 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-201 |
3.09e-26 |
|
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: 105.60 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQA-LQKVDFHLKRGEMafLG--GHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLR 78
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEV--LGviGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHRLLmDRSIFDNVAlpmRIESISENEIkrrVSAAldktgllDKARC------LP-----------SQLSGG 141
Cdd:COG4618 406 RHIGYLPQDVELF-DGTIAENIA---RFGDADPEKV---VAAA-------KLAGVhemilrLPdgydtrigeggARLSGG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 142 EQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVN 201
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA 531
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-196 |
5.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.28 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 35 GHSGAGKSTLLKLICAI------ERPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLMDRSIFDNVALPMRIES 108
Cdd:PRK14246 43 GPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIK---LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 109 ISEN-EIKRRVSAALDKTGLL----DKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEF 183
Cdd:PRK14246 120 IKEKrEIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170
....*....|...
gi 1327051661 184 NRAgVTIILATHD 196
Cdd:PRK14246 200 KNE-IAIVIVSHN 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-197 |
5.32e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGgRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI---ERPTDGRVWFNDHDITRIP--AKDIP 75
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 76 FLRRNIGIVFQDHRLLMDRSIFDNVAL------PMRIESIS--ENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVG 147
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 148 IARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQV 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-195 |
6.56e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEM-AFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDIpflR 78
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIhALLG-ENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAI---A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQdHRLLMDR-SIFDNVAL---PMRIESISENEIKRRVSAALDKTGL-LDKARcLPSQLSGGEQQRVGIARAVV 153
Cdd:COG3845 80 LGIGMVHQ-HFMLVPNlTVAENIVLglePTKGGRLDRKAARARIRELSERYGLdVDPDA-KVEDLSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.92e-25 |
|
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: 103.21 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQD-HrlLMDRSIFDNVALPMriESISENEikrrVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:TIGR02868 412 SVCAQDaH--LFDTTVRENLRLAR--PDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRaGVTIILATHD 196
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHH 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-197 |
2.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.16 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGR----QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRV-WF--NDHDITRIPA--- 71
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 72 ---------------KDIPFLRRNIGIVFQ-DHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGL----LDKA 131
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesyLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 132 rclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK13651 163 ---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-203 |
3.22e-25 |
|
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: 97.81 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItripAKDIPFLRRNIgiVFQDHR-- 89
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENI--LYLGHLpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDRSIFDNVALPMRIESISEneikRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD 169
Cdd:TIGR01189 84 LKPELSALENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 170 PELSNRVLRLFEEFNRAGVTIILATH-DIGLVNTR 203
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHqDLGLVEAR 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-169 |
3.50e-25 |
|
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: 102.59 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNI 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDrSIFDNVALPmRIESiSENEIKRRVSAAldktGLLDKARCLPSQ-----------LSGGEQQRVGIAR 150
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYG-RPDA-SEEEVEAAARAA----QIHDFIESLPDGydtrvgerglkLSGGEKQRVAIAR 507
|
170
....*....|....*....
gi 1327051661 151 AVVNRPTLLLADEPTGNLD 169
Cdd:COG5265 508 TLLKNPPILIFDEATSALD 526
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-198 |
4.96e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.78 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYR------GGR--------------QALQKVDFHLKRGEM-AFLGGhSGAGKSTLLKLICAIERPTDGRV 59
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLKgalkglfrreyrevEAVDDISFTIEPGEIvGFIGP-NGAGKSTTIKMLTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 60 WFNDHDitriPAKDIPFLRRNIGIVF-QDHRLLMDRSIFDNVALPMRIESISENEIKRRV---SAALDKTGLLDK-ARcl 134
Cdd:COG4586 80 RVLGYV----PFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLdelVELLDLGELLDTpVR-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 135 psQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIG 198
Cdd:COG4586 154 --QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMD 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-200 |
5.40e-25 |
|
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: 97.93 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAY--RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItriPAKDIPFLRR 79
Cdd:cd03248 12 VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDhRLLMDRSIFDNVALPMRIESISeneikrRVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGI 148
Cdd:cd03248 89 KVSLVGQE-PVLFARSLQDNIAYGLQSCSFE------CVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAgVTIILATHDIGLV 200
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
5.78e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDrSIFDNVALPmrIESISENEIkrrvSAALDKTGL---LDKARCLPS-------QLSGGEQQRVGIAR 150
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA--APNASDEAL----IEVLQQVGLeklLEDDKGLNAwlgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRaGVTIILATH 195
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-195 |
7.18e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI-----ERPTDGRVWFNDHDITRiPAKDIPFLRRNIGI 83
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLLMDRSIFDNVALPMRIESI--SENEIKRRVSAALDKTGLLDKARC----LPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTH 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-195 |
1.03e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.05 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYR---GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfL 77
Cdd:cd03266 1 MITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFqDHRLLMDR-SIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:cd03266 77 RRRLGFVS-DSTGLYDRlTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 157 TLLLADEPTGNLDPeLSNRVLRLF-EEFNRAGVTIILATH 195
Cdd:cd03266 156 PVLLLDEPTTGLDV-MATRALREFiRQLRALGKCILFSTH 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-197 |
1.65e-24 |
|
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: 95.19 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflRRNIGIVF-----QDH 88
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD----AIRAGIAYvpedrKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 RLLMDRSIFDNVALPmriesiseneikrrvsaaldktglldkarclpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:cd03215 88 GLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180
....*....|....*....|....*....
gi 1327051661 169 DPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSEL 164
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-200 |
1.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDIPF 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIVFQ--DHRLLMD---RSI-FDNVALPMRIEsisenEIKRRVSAALDKTGL-LDKARCLPSQLSGGEQQRVGIA 149
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDtveREIiFGPKNFKMNLD-----EVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFN-RAGVTIILATHDIGLV 200
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEV 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-197 |
2.38e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFndhDITRIPAKDIPFLRRNIGIVFQD-HRLLMDRSI 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180
....*....|....*....|..
gi 1327051661 177 LRLFEEF-NRAGVTIILATHDI 197
Cdd:PRK13642 180 MRVIHEIkEKYQLTVLSITHDL 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-195 |
2.61e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItriPAKdIPFLRRNI 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSR-ARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-197 |
3.03e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 25 LKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRN-IGIVFQDHRLLMDRSIFDNVALP 103
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 104 MRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP----ELSNRVLRL 179
Cdd:PRK10070 131 MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtEMQDELVKL 210
|
170
....*....|....*...
gi 1327051661 180 FEEFNRagvTIILATHDI 197
Cdd:PRK10070 211 QAKHQR---TIVFISHDL 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-197 |
3.26e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKlicAIERPTD--------GRVWFNDHDITRiPAKDIPFLRRNIG 82
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLR---SINRMNDlnpevtitGSIVYNGHNIYS-PRTDTVDLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQD-HRLLMdrSIFDNVALPMRIESISENEI-KRRVSAALDKTGLLD--KARCLPSQ--LSGGEQQRVGIARAVVNRP 156
Cdd:PRK14239 90 MVFQQpNPFPM--SIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDevKDRLHDSAlgLSGGQQQRVCIARVLATSP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 157 TLLLADEPTGNLDPELSNRV----LRLFEEFnragvTIILATHDI 197
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIeetlLGLKDDY-----TMLLVTRSM 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-200 |
3.72e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWF-----NDHDITRIPAKDIPFL-R 78
Cdd:PRK11701 10 RGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERRRLlR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDHR--LLMDRSIFDNVAlpMRIESISEN---EIKRRVSAALDKTGLlDKARC--LPSQLSGGEQQRVGIARA 151
Cdd:PRK11701 89 TEWGFVHQHPRdgLRMQVSAGGNIG--ERLMAVGARhygDIRATAGDWLERVEI-DAARIddLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDIGLV 200
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
7.91e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 7.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 4 FQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFndhditripAKDIpflrrNIGI 83
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGL-----RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLLMDRSIFDNV--------ALPMRIESISEN------------------------EIKRRVSAALDKTGL---- 127
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEAKlaepdedlerlaelqeefealggwEAEARAEEILSGLGFpeed 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 128 LDKarcLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPElsnRVLRLfEEF--NRAGvTIILATHD 196
Cdd:COG0488 146 LDR---PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWL-EEFlkNYPG-TVLVVSHD 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-196 |
9.88e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLM 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DrSIFDNVALPMRIESISENEikRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALpdtiLTKN---IAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180
....*....|....*....|....*....
gi 1327051661 169 DPELSNRVLRLFEEFNR-AGVTIILATHD 196
Cdd:PRK10247 169 DESNKHNVNEIIHRYVReQNIAVLWVTHD 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
1.06e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG----RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAkdipF 76
Cdd:COG1101 1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LR-RNIGIVFQDHrlLM----DRSIFDNVALPMRIESiseneiKRRVSAALDKT--------------GLLDKARCLPSQ 137
Cdd:COG1101 77 KRaKYIGRVFQDP--MMgtapSMTIEENLALAYRRGK------RRGLRRGLTKKrrelfrellatlglGLENRLDTKVGL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 138 LSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDI 197
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNM 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-200 |
1.85e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAY--RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDhRLLMDRSIFDNVALPMRIESISEneikrrVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGI 148
Cdd:TIGR00958 556 QVALVGQE-PVLFSGSVRENIAYGLTDTPDEE------IMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAI 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPElSNRVLRlfEEFNRAGVTIILATHDIGLV 200
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAE-CEQLLQ--ESRSRASRTVLLIAHRLSTV 677
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-197 |
2.44e-23 |
|
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: 93.38 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 23 FHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhditRIPAKDIPFLRRNIGIVFQDHRLLMDRSI-FDNVA 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTV--------KVAGASPGKGWRHIGYVPQRHEFAWDFPIsVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 102 LPMRIESISENEIKRR-----VSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVadfaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180
....*....|....*....|.
gi 1327051661 177 LRLFEEFNRAGVTIILATHDI 197
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDL 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-200 |
2.55e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflrrNIGIV--FQDHRL 90
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA----RMGVVrtFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 91 LMDRSIFDN--VALPMRIES-------------ISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:PRK11300 92 FREMTVIENllVAQHQQLKTglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 156 PTLLLADEPTGNLDP----ELSNRVLRLFEEFnraGVTIILATHDIGLV 200
Cdd:PRK11300 172 PEILMLDEPAAGLNPketkELDELIAELRNEH---NVTVLLIEHDMKLV 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-197 |
2.59e-23 |
|
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: 93.33 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYR-GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:cd03244 3 IEFKNVSLRYRpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDhRLLMDRSIFDNVAlPmrIESISENEIKRrvsaALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLD-P--FGEYSDEELWQ----ALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLR-LFEEFnrAGVTIILATHDI 197
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKtIREAF--KDCTVLTIAHRL 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-200 |
4.10e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKST----LLKLIcaierPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDH 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 ------RLLMDRSIFDNVALPMRIESISENEikRRVSAALDKTGLLDKARC-LPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK15134 372 nsslnpRLNVLQIIEEGLRVHQPTLSAAQRE--QQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDIGLV 200
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVV 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-203 |
5.36e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.24 E-value: 5.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 10 AYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDItripakDIPFLRRNIgiVFQDHR 89
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEAC--HYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDR--SIFDNVALPMRIEsiseNEIKRRVSAALDKTGLLDKARcLPSQ-LSGGEQQRVGIAR-AVVNRPTLLLaDEPT 165
Cdd:PRK13539 82 NAMKPalTVAENLEFWAAFL----GGEELDIAAALEAVGLAPLAH-LPFGyLSAGQKRRVALARlLVSNRPIWIL-DEPT 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATH-DIGLVNTR 203
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLPGAR 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-195 |
5.96e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDhdiTRIPAKdIPFLRRNI 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPAR-ARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-195 |
8.44e-23 |
|
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: 90.84 E-value: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRG-GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipfLRRN 80
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLmDRSIFDNVALpmriesiseneikrrvsaaldktglldkarclpsQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLGR----------------------------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRaGVTIILATH 195
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-197 |
1.45e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLK-------LICAIErpTDGRVWFNDHDITRiPAKDIPFLRRNIGI 83
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYA-PDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLLmDRSIFDNVALPMRIESISENeIKRRVSAALDKTGLLD----KARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK14243 96 VFQKPNPF-PKSIYDNIAYGARINGYKGD-MDELVERSLRQAALWDevkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAgVTIILATHDI 197
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNM 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-170 |
3.00e-22 |
|
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: 90.80 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAkdipFLRRNIGIV 84
Cdd:TIGR04406 5 ENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPM----HERARLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FqdhrLLMDRSIF------DNV-ALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:TIGR04406 80 Y----LPQEASIFrkltveENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPK 155
|
170
....*....|...
gi 1327051661 158 LLLADEPTGNLDP 170
Cdd:TIGR04406 156 FILLDEPFAGVDP 168
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-197 |
4.62e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE---LAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL---PM---RIESisenEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfPYskgRLTA----EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 155 RPTLLLADEPTGNLDP----ELSNRVLRLFEEFNRagvTIILATHDI 197
Cdd:COG4604 153 DTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGK---TVVIVLHDI 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-214 |
5.12e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIC--------AIERPTDGRVWFndhditrIPAKdiPFLrrNIGivf 85
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF-------LPQR--PYL--PLG--- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 86 qdhrllmdrSIFDNVALPMRIESISENEIKrrvsAALDKTGL------LDKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:COG4178 441 ---------TLREALLYPATAEAFSDAELR----EALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEfNRAGVTIILATHDIGLvntrPQY--RHLELNQG 214
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTL----AAFhdRVLELTGD 559
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-197 |
5.53e-22 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 91.79 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIE----RPTDGRVWFNDHDITRI-PAKDIPFLRRNIGIVFQD 87
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLsPRERRKLVGHNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 HRLLMDRSifDNVALPMrIESISE-----------NEIKRRVSAALDKTGLLDKA---RCLPSQLSGGEQQRVGIARAVV 153
Cdd:PRK15093 98 PQSCLDPS--ERVGRQL-MQNIPGwtykgrwwqrfGWRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDI 197
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-195 |
6.58e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 6.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFND----HDITRIPA---------KDIPFLRRNIGI 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigDKKNNHELitnpyskkiKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQ--DHRLLMD---RSI-FDNVALpmrieSISENEIKRRVSAALDKTGL----LDKArclPSQLSGGEQQRVGIARAVV 153
Cdd:PRK13631 121 VFQfpEYQLFKDtieKDImFGPVAL-----GVKKSEAKKLAKFYLNKMGLddsyLERS---PFGLSGGQKRRVAIAGILA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-195 |
1.15e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.09 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 35 GHSGAGKSTLLKLICAIERPTDGRVWFNDH---DItripAKDI--PFLRRNIGIVFQDHRLLMDRSIFDNVALPMRIESI 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDA----EKGIclPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 110 SENEikrRVSAALDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD-P---ELSNRVLRLFEEFNr 185
Cdd:PRK11144 107 AQFD---KIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPrkrELLPYLERLAREIN- 179
|
170
....*....|
gi 1327051661 186 agVTIILATH 195
Cdd:PRK11144 180 --IPILYVSH 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-200 |
1.30e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYR---------------------GGRQALQKVDFHLKRGEmaFLG--GHSGAGKSTLLKLICAIERPTDG 57
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGE--SVGiiGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 58 RVWFNDhditRIPAkdiPFlrrNIGIVFQdhrllMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGL---LDkarcL 134
Cdd:COG1134 82 RVEVNG----RVSA---LL---ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELgdfID----Q 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327051661 135 P-SQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:COG1134 143 PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-197 |
2.04e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDH--------RLLMD--RSIFDNvaLPMRIESisenEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIAR 150
Cdd:PRK11231 78 LALLPQHHltpegitvRELVAygRSPWLS--LWGRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 151 AVVNRPTLLLADEPTGNLDpeLSNRV--LRLFEEFNRAGVTIILATHDI 197
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD--INHQVelMRLMRELNTQGKTVVTVLHDL 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-197 |
2.19e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYRGgRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflRRNIGIV 84
Cdd:PRK10895 7 KNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIFDNVALPMRI-ESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 164 PTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-202 |
2.86e-21 |
|
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: 85.96 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGrvwfndhDITRIPAKDIPFLrrni 81
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVKIGYF---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 givfqdhrllmdrsifdnvalpmriesiseneikrrvsaaldktglldkarclpSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03221 69 ------------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRagvTIILATHDIGLVNT 202
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQ 132
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-213 |
3.05e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIP---AKDIPFLRRNIGIvfqdH 88
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyHQDLLYLGHQPGI----K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 RLLmdrSIFDNVALPMRIESISENEikrRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:PRK13538 87 TEL---TALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 169 DPELSNRVLRLFEEFNRAGVTIILATH-DIGLVNtrPQYRHLELNQ 213
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTTHqDLPVAS--DKVRKLRLGQ 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-195 |
3.74e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.02 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIE--RPTDGRVWFN-----DHDITRIPAK-- 72
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalceKCGYVERPSKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 73 -------------DIPF----------LRRNIGIVFQ-DHRLLMDRSIFDNV--ALPmRIESISENEIKRRVSAaLDKTG 126
Cdd:TIGR03269 80 epcpvcggtlepeEVDFwnlsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVleALE-EIGYEGKEAVGRAVDL-IEMVQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 127 LLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATH 195
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSH 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-199 |
4.35e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflrRNIGIVFQDHRLL 91
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MD---RSIFDNVALPMRIESISENEIKRR-VSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGN 167
Cdd:PRK09536 90 FEfdvRQVVEMGRTPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 168 LDPELSNRVLRLFEEFNRAGVTIILATHDIGL 199
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-195 |
4.43e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.84 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLK-LICAIERPTD-GRVWFNDHDITRIPakdipfLRR 79
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGVsGEVLINGRPLDKRS------FRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDNValpmriesiseneikrRVSAALdktglldkarclpSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETL----------------MFAAKL-------------RGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-202 |
6.39e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGE-MAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDitripakdipflrr 79
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDrIGLIG-PNGAGKSTLLKLLAGELEPDSGTVKLGETV-------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLL-MDRSIFDNVAlpmrieSISENEIKRRVSAALDK---TGllDKARCLPSQLSGGEQQRVGIARAVVNR 155
Cdd:COG0488 379 KIGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRflfSG--DDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 156 PTLLLADEPTGNLDPElsnrVLRLFEEF--NRAGvTIILATHDIGLVNT 202
Cdd:COG0488 451 PNVLLLDEPTNHLDIE----TLEALEEAldDFPG-TVLLVSHDRYFLDR 494
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-200 |
7.11e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLLMD--R 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 95 SIFDNVALPMRIESISENE-IKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPEL 172
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180
....*....|....*....|....*....
gi 1327051661 173 SNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK10261 499 RGQIINLLLDLQRDfGIAYLFISHDMAVV 527
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-200 |
1.17e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITrIPAKDIPFLRRNIGIVFQDHrllmDRS 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDP----EQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IF-----DNVALPMRIESISENEIKRRVSAALDktgLLDKA--RCLPSQ-LSGGEQQRVGIARAVVNRPTLLLADEPTGN 167
Cdd:PRK13638 90 IFytdidSDIAFSLRNLGVPEAEITRRVDEALT---LVDAQhfRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190
....*....|....*....|....*....|...
gi 1327051661 168 LDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-200 |
2.06e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHditRIPA-----KDIPFLRRNIGIVFQ--DH 88
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDY---AIPAnlkkiKEVKRLRKEIGLVFQfpEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 RLLMDrSIFDNVAL-PMRIESiSENEIKRRVSAALDKTGL-LDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:PRK13645 102 QLFQE-TIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 167 NLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQV 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-197 |
2.28e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRqaLQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIcAIERPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLM 92
Cdd:COG4138 9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARM-AGLLPGQGEILLNGRPLSDWSAAE---LARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDNVALPMRiESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAV------VN-RPTLLLADEPT 165
Cdd:COG4138 83 AMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-195 |
3.01e-20 |
|
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: 85.40 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGE-MAFLGGhSGAGKSTLLKLI-CAIERP--TDGRVWFNDHDITRipakdiPFLRRNIGIVFQDHRL 90
Cdd:cd03234 20 ARILNDVSLHVESGQvMAILGS-SGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKP------DQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 91 L----MDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:cd03234 93 LpgltVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 1327051661 167 NLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-201 |
4.76e-20 |
|
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: 87.79 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRRNIGI 83
Cdd:TIGR01842 320 ENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW---DRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLlMDRSIFDNVAlpmRIEsisENEIKRRVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIARAV 152
Cdd:TIGR01842 397 LPQDVEL-FPGTVAENIA---RFG---ENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARAL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVN 201
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLG 518
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-200 |
5.95e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.23 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGG---RQ---ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPFLRRNIGIV 84
Cdd:PRK15112 16 YRTGwfrRQtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH---FGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMD--RSIFDNVALPMRIES-ISENEIKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:PRK15112 93 FQDPSTSLNprQRISQILDFPLRLNTdLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFN-RAGVTIILATHDIGLV 200
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMM 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-213 |
9.32e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.31 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFN---DHDITRIPAKDIPFLRRNIGIvfqDH 88
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNggpLDFQRDSIARGLLYLGHAPGI---KT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 RLlmdrSIFDNVALPMRIESISEneikrrVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:cd03231 87 TL----SVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 169 DPELSNRVLRLFEEFNRAGVTIILATH-DIGLVNTRpqYRHLELNQ 213
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAG--ARELDLGF 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-200 |
9.81e-20 |
|
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: 83.74 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 8 SKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWfndhditrIPAKDIPFLRRNIGivfqd 87
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT--------VRGRVSSLLGLGGG----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 hrLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLlDKARCLP-SQLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:cd03220 95 --FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 167 NLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI 205
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-197 |
1.17e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI-----ERPTDGRVWFNDHDI--TRIpakDI 74
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyeRRV---NL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 75 PFLRRNIGIVFQDHRLLmDRSIFDNVALPMRIESISEN-EIKRRVSAALDKTGLLD--KARCLPS--QLSGGEQQRVGIA 149
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDeiKHKIHKSalDLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFN-RAGVTIILATHDI 197
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNL 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-169 |
2.43e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.93 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHL-KRGEMAFLGgHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdipFLRRN 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVpSRGFVALVG-HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDrSIFDNVALPmriESISENeikrRVSAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIA 149
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLG---RDISEE----QVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALA 488
|
170 180
....*....|....*....|
gi 1327051661 150 RAVVNRPTLLLADEPTGNLD 169
Cdd:PRK10790 489 RVLVQTPQILILDEATANID 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-195 |
2.51e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLrrN 80
Cdd:PRK09700 5 YISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNV---ALPMR----IESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV 153
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-195 |
3.93e-19 |
|
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: 85.56 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIpakDIPFLRRNI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDhRLLMDRSIFDNVALPMRiESISENEIKRRVSAALDKT-------GLLDKARCLPSQLSGGEQQRVGIARAVVN 154
Cdd:TIGR01193 551 NYLPQE-PYIFSGSILENLLLGAK-ENVSQDEIWAACEIAEIKDdienmplGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 155 RPTLLLADEPTGNLDPELSNRVLRLFEEFNRAgvTIILATH 195
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAH 667
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-195 |
1.35e-18 |
|
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: 83.91 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripaKDIPFLRRNIGIVFQDHRLLMD 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE----TNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELS 173
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180
....*....|....*....|..
gi 1327051661 174 NRVLRLFEEFnRAGVTIILATH 195
Cdd:TIGR01257 1098 RSIWDLLLKY-RSGRTIIMSTH 1118
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-200 |
1.99e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.08 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKS----TLLKLICAIERpTDGRVWFNDHDITRIPAKDIPFLR-RNIGIVFQD---- 87
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPEKELNKLRaEQISMIFQDpmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 -----------HRLLM-----------DRSI--FDNVALPmriesisenEIKRRVsaaldktglldkaRCLPSQLSGGEQ 143
Cdd:PRK09473 110 lnpymrvgeqlMEVLMlhkgmskaeafEESVrmLDAVKMP---------EARKRM-------------KMYPHEFSGGMR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 144 QRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLF----EEFNRAgvtIILATHDIGLV 200
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTA---IIMITHDLGVV 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-192 |
2.38e-18 |
|
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: 80.26 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 10 AYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGIVFQDhr 89
Cdd:TIGR03410 8 VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 llmdRSIF------DNV-----ALPMRIESISEN---------EIKRRvsaaldKTGLLdkarclpsqlSGGEQQRVGIA 149
Cdd:TIGR03410 84 ----REIFprltveENLltglaALPRRSRKIPDEiyelfpvlkEMLGR------RGGDL----------SGGQQQQLAIA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDP---ELSNRVLRLFEEfnRAGVTIIL 192
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPsiiKDIGRVIRRLRA--EGGMAILL 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
3.47e-18 |
|
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: 78.35 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIC--------AIERPTDGRVWFndhditrIPAKd 73
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF-------LPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 74 iPFLrrnigivfqdhrllmdrsifdnvalpmriesiseneikrrvsaaldKTGLLDKARCLPSQ--LSGGEQQRVGIARA 151
Cdd:cd03223 73 -PYL----------------------------------------------PLGTLREQLIYPWDdvLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEfnrAGVTIILATH 195
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-195 |
7.51e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.34 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIE--RPTDGRVWFNDHDITRIPAKDIPflRRNIGIVFQ 86
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 DhrllmdrsifdnvalPMRIESISENEIKRRVSAAldktglldkarclpsqLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:cd03217 85 Y---------------PPEIPGVKNADFLRYVNEG----------------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180
....*....|....*....|....*....
gi 1327051661 167 NLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-197 |
8.82e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflrRNIGIV 84
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIFDNVA------LPMRIESISENEikRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:PRK10253 87 AQNATTPGDITVQELVArgryphQPLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 159 LLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDI 197
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDL 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-206 |
1.98e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhDITRIPAKDIpfLRRNI 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQA--LQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 gIVFQDHRLLMDRS---IFDNVAL-----PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVV 153
Cdd:PRK15056 80 -VAYVPQSEEVDWSfpvLVEDVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 154 NRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNTRPQY 206
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-200 |
2.57e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKS----TLLKLICAIERPTDGRVWFndhDITRIPAKDipfLR-RNIGIVFQDhrllmDRS 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLL---DGKPVAPCA---LRgRKIATIMQN-----PRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFdNVALPMR---IESISENEI---KRRVSAALDKTGLLDKARCL---PSQLSGGEQQRVGIARAVVNRPTLLLADEPTG 166
Cdd:PRK10418 91 AF-NPLHTMHthaRETCLALGKpadDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 167 NLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKrALGMLLVTHDMGVV 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-194 |
4.40e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDIpflRRNIGIVFQDHR-- 89
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAI---RAGIAYVPEDRKge 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 -LLMDRSIFDNVALPmRIESIS---------ENEIKRRVSAALD-KTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:COG1129 340 gLVLDLSIRENITLA-SLDRLSrgglldrrrERALAEEYIKRLRiKTPSPEQ---PVGNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327051661 159 LLADEPTgnldpelsnR---------VLRLFEEFNRAGVTIILAT 194
Cdd:COG1129 416 LILDEPT---------RgidvgakaeIYRLIRELAAEGKAVIVIS 451
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-200 |
5.39e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKS-TLLKLICAIERPtdGRVW-----FNDHDITRIPAKDipflRRNI-----GIV 84
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKE----RRNLvgaevAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIfdNVALPMrIESI------SENEIKRRVSAALDKTGLLDKARCL---PSQLSGGEQQRVGIARAVVNR 155
Cdd:PRK11022 95 FQDPMTSLNPCY--TVGFQI-MEAIkvhqggNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 156 PTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGLV 200
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALV 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-195 |
6.24e-17 |
|
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: 78.71 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI--ERPTDGRVWFNDHDITRIPAKDIPflRRNIGIVFQDHRL 90
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE--RAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 91 LMDRSIFDNVALPMRI----ESISENEIKRRVSAALDKTGLLDKARCLP-SQLSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:TIGR02633 90 VPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190
....*....|....*....|....*....|
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-195 |
1.01e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIE--RPTDGRVWFNDHDITRipakdipflrrnigivfqdhrllm 92
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR------------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDNVAlpmRIESIseNEIKRRVSAAldktGLLDKA--RCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP 170
Cdd:COG2401 99 EASLIDAIG---RKGDF--KDAVELLNAV----GLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*.
gi 1327051661 171 ELSNRVLRLFEEFNR-AGVTIILATH 195
Cdd:COG2401 170 QTAKRVARNLQKLARrAGITLVVATH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-200 |
1.30e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYRGGRQALQKVD---FHLKRGEMAFLGGHSGAGKS-TLLKLICAIERP----TDGRVWFNDHDITRIPAKDIPF 76
Cdd:PRK15134 9 ENLSVAFRQQQTVRTVVNdvsLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRN-IGIVFQD--------HRLlmDRSIFDNVAL--PMRIESiSENEIKRrvsaALDKTGLLDKARCL---PSQLSGGE 142
Cdd:PRK15134 89 VRGNkIAMIFQEpmvslnplHTL--EKQLYEVLSLhrGMRREA-ARGEILN----CLDRVGIRQAAKRLtdyPHQLSGGE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327051661 143 QQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGLV 200
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIV 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-195 |
1.65e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEM-AFLGGHsGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPfLRRNIGIVFQDHRLLMDRS 95
Cdd:NF033858 281 AVDHVSFRIRRGEIfGFLGSN-GCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIA-TRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNR 175
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|.
gi 1327051661 176 VLRLFEEFNR-AGVTIILATH 195
Cdd:NF033858 436 FWRLLIELSReDGVTIFISTH 456
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-193 |
2.03e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAY--RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFND-HDITRIpakDIPFLR 78
Cdd:PTZ00265 383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDI---NLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 79 RNIGIVFQDhRLLMDRSIFDNVALPM----RIESIS-----------ENEIKRR------------VSAALDKTGLL--- 128
Cdd:PTZ00265 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkDLEALSnyynedgndsqENKNKRNscrakcagdlndMSNTTDSNELIemr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 129 ---------------------DKARCLP-----------SQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:PTZ00265 539 knyqtikdsevvdvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250
....*....|....*....
gi 1327051661 177 LRLFEEF--NRAGVTIILA 193
Cdd:PTZ00265 619 QKTINNLkgNENRITIIIA 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-195 |
3.16e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIP-AKDIPFLRRNIGivfqdhrLLMDRSIFDN 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRFMAYLGHLPG-------LKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 100 VALpmrIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRL 179
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 1327051661 180 FEEFNRAGVTIILATH 195
Cdd:PRK13543 180 ISAHLRGGGAALVTTH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-171 |
5.27e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS---LRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDrSIFDNVALPmRIESISENEIKR--RVSAALDKTGLLDKArcLPS-------QLSGGEQQRVGIARA 151
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEaaRMAYAMDFINKMDNG--LDTvigengvLLSGGQRQRIAIARA 494
|
170 180
....*....|....*....|.
gi 1327051661 152 VV-NRPTLLLaDEPTGNLDPE 171
Cdd:PRK11176 495 LLrDSPILIL-DEATSALDTE 514
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-200 |
6.03e-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: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 16 QALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLMD-- 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQDPTLFSGti 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDnvalpmRIESISENEIKrrvsAALDKTGlldkarcLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPE-- 171
Cdd:cd03369 99 RSNLD------PFDEYSDEEIY----GALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAtd 161
|
170 180 190
....*....|....*....|....*....|
gi 1327051661 172 -LSNRVLRlfEEFNraGVTIILATHDIGLV 200
Cdd:cd03369 162 aLIQKTIR--EEFT--NSTILTIAHRLRTI 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-195 |
9.38e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEM-AFLGGhSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdiPFLRR 79
Cdd:PRK15439 11 LLCARSISKQY-SGVEVLKGIDFTLHAGEVhALLGG-NGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGI--VFQDHRLLMDRSIFDNVALPMRiesiSENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK15439 85 QLGIylVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-195 |
1.58e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIcAIERPTD----GRVWFNDHDITRipakdiPFLRRNIGIVFQD 87
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKGvkgsGSVLLNGMPIDA------KEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 88 HRLLMDRSIFD--NVALPMRI-ESISENEIKRRVSAALDKTGLLDKARCL---PSQ---LSGGEQQRVGIARAVVNRPTL 158
Cdd:TIGR00955 108 DLFIPTLTVREhlMFQAHLRMpRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 159 LLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
1.79e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYRGGRQALQkvDFHLKRGEMAFLG--GHSGAGKSTLLKLICAIERPTDGRVWfndhditriPAKDIpflrrNIG 82
Cdd:TIGR03719 8 NRVSKVVPPKKEILK--DISLSFFPGAKIGvlGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPGI-----KVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQDHRLLMDRSIFDNVALPM--------RIESISEN----------------EIKRRVSAA----LDKTglLDKA--- 131
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVaeikdaldRFNEISAKyaepdadfdklaaeqaELQEIIDAAdawdLDSQ--LEIAmda 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 132 -RCLP-----SQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnrAGvTIILATHD 196
Cdd:TIGR03719 150 lRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHD 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-198 |
2.17e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDI---TRIPAKDIPFLRRNIGIVFQDHR 89
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLmDRSIFDNVALPMRIES-ISENEIKRRVSAALDKTGLLDKARCL----PSQLSGGEQQRVGIARAVVNRPTLLLADEP 164
Cdd:PRK14271 112 PF-PMSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 165 TGNLDPELSNRVlrlfEEFNRA---GVTIILATHDIG 198
Cdd:PRK14271 191 TSALDPTTTEKI----EEFIRSladRLTVIIVTHNLA 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-196 |
2.62e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.91 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGIVFQD-HR- 89
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--RRLGVAYIPEDrLGr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 -LLMDRSIFDNVAL---------------PMRIESISENEIKR-RVSAAldktGLLDKARclpsQLSGGEQQRVGIARAV 152
Cdd:COG3845 346 gLVPDMSVAENLILgryrrppfsrggfldRKAIRAFAEELIEEfDVRTP----GPDTPAR----SLSGGNQQKVILAREL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327051661 153 VNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISED 461
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-197 |
3.16e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIeRPTDGRVWFNDHDITRIpakDIPFLRRNIGIVFQDHRLLmD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDNVALPMriESISENEIKrrvsAALDKTGLLDKARCLP-----------SQLSGGEQQRVGIARAVVNRPTLLLAD 162
Cdd:PRK11174 437 GTLRDNVLLGN--PDASDEQLQ----QALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 163 EPTGNLDPELSNRVLRLFEEfNRAGVTIILATHDI 197
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQL 544
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
4.00e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhditripaKDIPFLRrn 80
Cdd:PRK09544 4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQdhRLLMDRSIFDNVALPMRIE-SISENEIK---RRVSAAldktGLLDKarclPSQ-LSGGEQQRVGIARAVVNR 155
Cdd:PRK09544 69 IGYVPQ--KLYLDTTLPLTVNRFLRLRpGTKKEDILpalKRVQAG----HLIDA----PMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327051661 156 PTLLLADEPTGNLDpelSNRVLRLFEEFNRA----GVTIILATHDIGLV 200
Cdd:PRK09544 139 PQLLVLDEPTQGVD---VNGQVALYDLIDQLrrelDCAVLMVSHDLHLV 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-195 |
1.00e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIeRPT---DGRVWFNDHDITRIPAKDIPflRRNIGIVFQDHR 89
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDTE--RAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDRSIFDNVAL---PMRIESISENEIKRRVSAALDKTGlLDKARCLP-SQLSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:PRK13549 93 LVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLK-LDINPATPvGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-195 |
1.63e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 4 FQQVSKAYRGGRqALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGI 83
Cdd:PRK11288 7 FDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA--LAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDHRLLMDRSIFDNV---ALPMRIESISENEIKRRVSAALDKTGL-LDKARCLPSqLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVdIDPDTPLKY-LSIGQRQMVEIAKALARNARVI 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-225 |
2.25e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPFLRRNI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLlmdrsiFDNVALPMRIESISEneikrRVSAALDKTGLLDK-----ARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK10522 400 SAVFTDFHL------FDQLLGPEGKPANPA-----LVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 157 TLLLADEPTGNLDPELsNRV--LRLFEEFNRAGVTIILATHDiglvntrPQY-----RHLELNQGFLSEVEDYGRE 225
Cdd:PRK10522 469 DILLLDEWAADQDPHF-RREfyQVLLPLLQEMGKTIFAISHD-------DHYfihadRLLEMRNGQLSELTGEERD 536
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-195 |
2.43e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIeRPT---DGRVWFND-----HDItripaKDIPflRRNIGIV 84
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGevcrfKDI-----RDSE--ALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIFDNVAL---PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:NF040905 84 HQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-225 |
2.97e-14 |
|
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: 70.98 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ----ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHditRIPAKDIPFL 77
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 RRNIGIVFQDHRL---LMDRsifDNVALPMRIES-ISENEIKRRVSaaldktglLDKARCLPSQLSGGEQQRVGIARAVV 153
Cdd:COG4615 405 RQLFSAVFSDFHLfdrLLGL---DGEADPARARElLERLELDHKVS--------VEDGRFSTTDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 154 -NRPTLLLaDEPTGNLDPELsnRvlRLF--E---EFNRAGVTIILATHDiglvntrPQY-----RHLELNQGFLSEVEDY 222
Cdd:COG4615 474 eDRPILVF-DEWAADQDPEF--R--RVFytEllpELKARGKTVIAISHD-------DRYfdladRVLKMDYGKLVELTGP 541
|
...
gi 1327051661 223 GRE 225
Cdd:COG4615 542 AAL 544
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-194 |
4.77e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-----RIPAKDIPF 76
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarhrRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 ----LRRNigivfqdhrLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAV 152
Cdd:NF033858 81 mpqgLGKN---------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327051661 153 VNRPTLLLADEPTGNLDPeLSNR-----VLRLFEEfnRAGVTIILAT 194
Cdd:NF033858 152 IHDPDLLILDEPTTGVDP-LSRRqfwelIDRIRAE--RPGMSVLVAT 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-199 |
5.51e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKdiPFLRRnigivfqdhrllmd 93
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK--AFARK-------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 rsifdnVA-LPMRI---ESISENEI-------------------KRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIAR 150
Cdd:PRK10575 87 ------VAyLPQQLpaaEGMTVRELvaigrypwhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 151 AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA-GVTIILATHDIGL 199
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINM 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-196 |
1.50e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDI-TRIPAKDIpflrrNIGIVF--QDHR---LLMDR 94
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGL-----ANGIVYisEDRKrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 95 SIFDNVALP-MRIESISENEIKRR--VSAALD-------KTGLLDKARCLpsqLSGGEQQRVGIARAVVNRPTLLLADEP 164
Cdd:PRK10762 346 SVKENMSLTaLRYFSRAGGSLKHAdeQQAVSDfirlfniKTPSMEQAIGL---LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 165 TGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-196 |
1.59e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYRGGRQALQkvDFHLkrgemAFL-----G--GHSGAGKSTLLKLICAIERPTDGRVWfndhditriPAKDIpfl 77
Cdd:PRK11819 10 NRVSKVVPPKKQILK--DISL-----SFFpgakiGvlGLNGAGKSTLLRIMAGVDKEFEGEAR---------PAPGI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 78 rrNIGIVFQDHRLLMDRSIFDNV--------ALPMRIESISEN------------EIKRRVSAALDKTGL------LDKA 131
Cdd:PRK11819 71 --KVGYLPQEPQLDPEKTVRENVeegvaevkAALDRFNEIYAAyaepdadfdalaAEQGELQEIIDAADAwdldsqLEIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 132 ----RCLP-----SQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPElsnRVLRLfEEF--NRAGvTIILATHD 196
Cdd:PRK11819 149 mdalRCPPwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWL-EQFlhDYPG-TVVAVTHD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-197 |
3.00e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipflRRNIGIVF-----QDHRLLMDRS 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFDNVA------LPMRIESISENEIKRRVSAALD-KTGLLDKArclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNL 168
Cdd:PRK15439 358 LAWNVCalthnrRGFWIKPARENAVLERYRRALNiKFNHAEQA---ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180
....*....|....*....|....*....
gi 1327051661 169 DPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDL 463
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-169 |
3.61e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLIcAIERPTD-GRVWF-NDHDITRIPaKDIPflrRNI-GIVF--------- 85
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-NGEVLLDdGRIIYeQDLIVARLQ-QDPP---RNVeGTVYdfvaegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 86 ------QDHRLL-------MDRsifdNVALPMRIESISENE----IKRRVSAALDKTGLldKARCLPSQLSGGEQQRVGI 148
Cdd:PRK11147 94 qaeylkRYHDIShlvetdpSEK----NLNELAKLQEQLDHHnlwqLENRINEVLAQLGL--DPDAALSSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLD 169
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-200 |
3.82e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQvskaYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKS-TLLKLICAIERP----TDGRVWFNDH-----DITRIPA 71
Cdd:PRK10261 20 IAFMQ----EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRsrqviELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 72 KDIPFLR-RNIGIVFQDHRLLMDR--SIFDNVALPMRI-ESISENEIKRRVSAALDKTGLLDKARCL---PSQLSGGEQQ 144
Cdd:PRK10261 96 AQMRHVRgADMAMIFQEPMTSLNPvfTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327051661 145 RVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNR-AGVTIILATHDIGLV 200
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-209 |
6.07e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPA---KDIPFLRRNIGIvfQDHRLLMDR 94
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyqKQLCFVGHRSGI--NPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 95 SIFDnvalpmrIESISEN-EIKRRVSaaLDKTGLLDKARClpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELS 173
Cdd:PRK13540 95 CLYD-------IHFSPGAvGITELCR--LFSLEHLIDYPC--GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 174 NRVLRLFEEFNRAGVTIILATH-DIGLVNTRPQYRHL 209
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHqDLPLNKADYEEYHL 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-216 |
6.24e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 23 FHLKRGEMAFLGGHSGAGKSTLLKLICAIeRPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLMDRSIFDNVAL 102
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAE---LARHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 103 ---PMRIESISENEIkRRVSAALdktGLLDK-ARCLpSQLSGGEQQRVGIArAVV------NRP--TLLLADEPTGNLDP 170
Cdd:PRK03695 93 hqpDKTRTEAVASAL-NEVAEAL---GLDDKlGRSV-NQLSGGEWQRVRLA-AVVlqvwpdINPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327051661 171 ELSNRVLRLFEEFNRAGVTIILATHDigLVNTrpqYRH----LELNQGFL 216
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHD--LNHT---LRHadrvWLLKQGKL 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-195 |
1.08e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 7 VSKAYRGGRqALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGIVFQ 86
Cdd:PRK10982 4 ISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 87 DHRLLMDRSIFDNVAL---PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 164 PTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-200 |
5.09e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLK-LICAIERPTDGRVWFNDHDI-TRIPAKDIpflRRNIGIVFQD---HR 89
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVdIRNPAQAI---RAGIAMVPEDrkrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDRSIFDNVALP--------MRIESISENEIkrrVSAALDKTGLLDKARCLP-SQLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:TIGR02633 350 IVPILGVGKNITLSvlksfcfkMRIDAAAELQI---IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 161 ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEV 466
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-197 |
5.21e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.65 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripaKDIPFLRR 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQ---DHRLLMDRsifDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:TIGR01257 2013 NMGYCPQfdaIDDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327051661 157 TLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-197 |
5.99e-12 |
|
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: 63.20 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 22 DFHL-------KRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRV-WFNDhDITRIPAKDIP--------FLRRNIGIVF 85
Cdd:cd03237 12 EFTLeveggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeIELD-TVSYKPQYIKAdyegtvrdLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 86 QDhrllmdrSIFDN-VALPMRIESISENEIkrrvsaaldktglldkarclpSQLSGGEQQRVGIArAVVNRPT-LLLADE 163
Cdd:cd03237 91 TH-------PYFKTeIAKPLQIEQILDREV---------------------PELSGGELQRVAIA-ACLSKDAdIYLLDE 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 164 PTGNLDPE---LSNRVLRLFEEFNRAGVTIIlaTHDI 197
Cdd:cd03237 142 PSAYLDVEqrlMASKVIRRFAENNEKTAFVV--EHDI 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-195 |
7.18e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.96 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQDHRLLMDr 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 95 SIFDNVALPMRIESISENEIKRRVSAALDktgllDKARcLPS-----------QLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:PRK10789 404 TVANNIALGRPDATQQEIEHVARLASVHD-----DILR-LPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190
....*....|....*....|....*....|..
gi 1327051661 164 PTGNLDPELSNRVLRLFEEFnRAGVTIILATH 195
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQW-GEGRTVIISAH 508
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-195 |
9.61e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 30 MAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGivfqdhrLLMDRSIFDNVALPMRIESI 109
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFENLKFWSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 110 SENeikrrVSAALDK---TGLLDKaRCLpsQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRA 186
Cdd:PRK13541 101 AET-----LYAAIHYfklHDLLDE-KCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANS 172
|
....*....
gi 1327051661 187 GVTIILATH 195
Cdd:PRK13541 173 GGIVLLSSH 181
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-195 |
7.12e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 28 GEMAFLGGHSGAGKSTLLKLICAIERPTD--GRVWFNDHDITRipakdiPFLRRnIGIVFQDHRL---LMDRSIFDNVAL 102
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK------QILKR-TGFVTQDDILyphLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 103 PMRIESISENEIKRRVSAALDKTGLldkARC--------LPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSN 174
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELGL---TKCentiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|.
gi 1327051661 175 RVLRLFEEFNRAGVTIILATH 195
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-196 |
2.47e-10 |
|
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: 59.56 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDhditripakdipflRRNI 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE--------------TVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVFQDHRLLMD-RSIFDNVALPMRIESISENEIKRR--VSAALDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRPTL 158
Cdd:TIGR03719 388 AYVDQSRDALDPnKTVWEEISGGLDIIKLGKREIPSRayVGRFNFKGSDQQK---KVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 159 LLADEPTGNLDPElsnrVLRLFEE--FNRAGVTIILaTHD 196
Cdd:TIGR03719 465 LLLDEPTNDLDVE----TLRALEEalLNFAGCAVVI-SHD 499
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-197 |
3.40e-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: 57.73 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 14 GRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLLMD 93
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 94 RSIFDNVALPMRIEsiseneiKRRVSAALDKTGLLDKARCLPS-----------QLSGGEQQRVGIARAVVNRPTLLLAD 162
Cdd:cd03290 93 ATVEENITFGSPFN-------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 163 EPTGNLDPELSNR-----VLRLFEEFNRagvTIILATHDI 197
Cdd:cd03290 166 DPFSALDIHLSDHlmqegILKFLQDDKR---TLVLVTHKL 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-169 |
3.46e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTD------GRVWFNDHDITRIPAKdipfLRRNI--GIVFQDHR 89
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEgkikhsGRISFSPQTSWIMPGT----IKDNIifGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LlmdRSIFDNVALPMRIESISENeikrrvsaalDKTGLLDKArclpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD 169
Cdd:TIGR01271 518 Y---TSVIKACQLEEDIALFPEK----------DKTVLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-200 |
8.39e-10 |
|
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: 56.32 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNdhditripakdipflrRNIGIVFQDhRLLMDRSI 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP----------------GSIAYVSQE-PWIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNVALPMRIEsiseneiKRRVSAALDKTGLLDKARCLPSQ-----------LSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:cd03250 83 RENILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 166 GNLDPELSNRVL-RLFEEFNRAGVTIILATHDIGLV 200
Cdd:cd03250 156 SAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLL 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-197 |
8.45e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 15 RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITriPAKDIPFLRRNIGIVFQDHR---LL 91
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESRRdngFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDRSIFDNVALPMRIES---------ISENEIKRRVSAALDKTGLldkaRCLP-----SQLSGGEQQRVGIARAVVNRPT 157
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLAL----KCHSvnqniTELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327051661 158 LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-196 |
1.10e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndHDITRIpakDIPFlrrnigivFQDHRLLM 92
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKL---EVAY--------FDQHRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 D--RSIFDNVAlpmriESISENEIKRRVSAALdktGLLD-------KARCLPSQLSGGEQQRVGIARAVVNRPTLLLADE 163
Cdd:PRK11147 395 DpeKTVMDNLA-----EGKQEVMVNGRPRHVL---GYLQdflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 164 PTGNLDPElsnrVLRLFEEF--NRAGvTIILATHD 196
Cdd:PRK11147 467 PTNDLDVE----TLELLEELldSYQG-TVLLVSHD 496
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
77-195 |
1.31e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.05 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 77 LRRNIGIvfqdHRLLMD--RSIF---DNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARA 151
Cdd:NF000106 83 LRRTIG*----HRPVR*grRESFsgrENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1327051661 152 VVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-196 |
1.42e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFndhditripAKDIpflrrN 80
Cdd:PRK10636 312 LLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI-----K 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGiVFQDHRLLMDRSifDNVALpMRIESISENEIKRRVSAALDKTGLL-DKARCLPSQLSGGEQQRVGIARAVVNRPTLL 159
Cdd:PRK10636 377 LG-YFAQHQLEFLRA--DESPL-QHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327051661 160 LADEPTGNLDPELSNRVLRLFEEFNRAgvtIILATHD 196
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHD 486
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-197 |
1.71e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 56 DGRVWFNDHDITRIPAKDIpflrRNIGIVFQDHRLLMDRSIFDNVALPMriESISENEIKRRVS-AALDKTglldkARCL 134
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYENIKFGK--EDATREDVKRACKfAAIDEF-----IESL 1344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 135 PSQ-----------LSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEF-NRAGVTIILATHDI 197
Cdd:PTZ00265 1345 PNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRI 1419
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-191 |
1.95e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 NIGIVFQDHRLLMDRSIFDnvalpmrIESISENEiKRRVSAALDKTGLLDKARCLPSQL-----------SGGEQQRVGI 148
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFN-------IDPFSEHN-DADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSL 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLD---PELSNRVLRlfEEFNRAGVTII 191
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDvrtDSLIQRTIR--EEFKSCTMLVI 1426
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-196 |
2.86e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDIT-RIPAKDI-------PFLRRNIGIVfqdhrllM 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIragimlcPEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDNVALPMR---------IESISENEIKRRVSAALD-KTgllDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLAD 162
Cdd:PRK11288 345 VHSVADNINISARrhhlragclINNRWEAENADRFIRSLNiKT---PSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 163 EPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-195 |
3.06e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGgRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPflRRN 80
Cdd:PRK10762 4 LLQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ--EAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFDNVAL----PMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 157 TLLLADEPTGNL-DPELSN--RVLRlfeEFNRAGVTIILATH 195
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESlfRVIR---ELKSQGRGIVYISH 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-169 |
3.41e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPT---DGRVWFNDHDItripAKDIPFLRRNIGIVFQDH 88
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY----KEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 89 R---LLMDRSIFDNVAlpmrieSISENEIKRRVsaaldktglldkarclpsqlSGGEQQRVGIARAVVNRPTLLLADEPT 165
Cdd:cd03233 93 VhfpTLTVRETLDFAL------RCKGNEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNST 146
|
....
gi 1327051661 166 GNLD 169
Cdd:cd03233 147 RGLD 150
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-196 |
4.48e-09 |
|
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: 53.87 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 6 QVSKAYRggrQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERptdgrvwfndhdiTRIPAKDIPflrrnigiVF 85
Cdd:cd03238 2 TVSGANV---HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASG-------------KARLISFLP--------KF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 86 QDHRLLMdrsifdnvalpmrIESISeneikrrvsaALDKTGL--LDKARCLPSqLSGGEQQRVGIAR--AVVNRPTLLLA 161
Cdd:cd03238 58 SRNKLIF-------------IDQLQ----------FLIDVGLgyLTLGQKLST-LSGGELQRVKLASelFSEPPGTLFIL 113
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-192 |
4.83e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 21 VDFHLKRGEMAFLGGHSGAGKSTLLK-LICAIERPTDGRVWFNDHDIT-RIPAKDIpflRRNIGIVFQD---HRLLMDRS 95
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKiRNPQQAI---AQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 96 IFDNVALP--------MRI-----ESISENEIKR-RVSAAldkTGLLDKARclpsqLSGGEQQRVGIARAVVNRPTLLLA 161
Cdd:PRK13549 358 VGKNITLAaldrftggSRIddaaeLKTILESIQRlKVKTA---SPELAIAR-----LSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190
....*....|....*....|....*....|.
gi 1327051661 162 DEPTGNLDPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIV 460
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-195 |
6.57e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICaiERPTDGRVwfnDHDITRIPAKDIPFLRRNIGIVFQdhrll 91
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVI---TGEILINGRPLDKNFQRSTGYVEQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDrsifdnVALPMR--IESIseneikrRVSAALdktglldkarclpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD 169
Cdd:cd03232 87 QD------VHSPNLtvREAL-------RFSALL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 1327051661 170 PELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-195 |
9.06e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI--------ERPTDGRVWFndhditrIPAK 72
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY-------VPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 73 diPFLRRnigivfqdhRLLMDRSIFDNVALPMRIESISENEIKR-----RVSAALDKTGLLDKARCLPSQLSGGEQQRVG 147
Cdd:TIGR00954 524 --PYMTL---------GTLRDQIIYPDSSEDMKRRGLSDKDLEQildnvQLTHILEREGGWSAVQDWMDVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327051661 148 IARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFnraGVTIILATH 195
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-197 |
1.03e-08 |
|
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: 54.92 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 8 SKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAI-----ERPTDGRVWfndHDITripakdIPFLRRNIG 82
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLlstegEIQIDGVSW---NSVT------LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQdhRLLMDRSIFDNVALPMriESISENEIKRrvsaALDKTGLLDKARCLPSQL-----------SGGEQQRVGIARA 151
Cdd:TIGR01271 1296 VIPQ--KVFIFSGTFRKNLDPY--EQWSDEEIWK----VAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 152 VVNRPTLLLADEPTGNLDPeLSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-169 |
1.56e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.71 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDG------RVWFNDHDITRIPAKdipfLRRNI--GIVFQDHR 89
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGkikhsgRISFSSQFSWIMPGT----IKENIifGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LlmdRSIFDNVALPMRIESISENEikrrvSAALDKTGLldkarclpsQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLD 169
Cdd:cd03291 129 Y---KSVVKACQLEEDITKFPEKD-----NTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-199 |
1.98e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRqALQKVDFHLKRGEMAFLGGHSGAGKSTLLKL----ICAIERP----TDGRVWFNDHDITRIPAK 72
Cdd:PRK13547 1 MLTADHLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPrgarVTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 73 DIPFLRrniGIVFQDHRLLMDRSIFDNVALPMRIESISENEIKRR----VSAALDKTGLLDKARCLPSQLSGGEQQRVGI 148
Cdd:PRK13547 80 RLARLR---AVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 149 ARAVVN---------RPTLLLADEPTGNLDPELSNRVL----RLFEEFNRAGVTIIlatHDIGL 199
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLdtvrRLARDWNLGVLAIV---HDPNL 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-195 |
8.31e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKayrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKliCAIERPTDGRVWFNDHdITRIPAKDIPFLRRnIGIV 84
Cdd:TIGR00956 769 VKIKK---EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN--VLAERVTTGVITGGDR-LVNGRPLDSSFQRS-IGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 85 FQDHRLLMDRSIFDNVALPMRI---ESISENEIKRRVSAALDKTGLLDKARCL----PSQLSGGEQQRVGIARAVVNRPT 157
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327051661 158 LLL-ADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-201 |
1.00e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.68 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 35 GHSGAGKSTL---LKLICAIERPTDGRVWFNDHDITRIPAKdipflRRNIGIVFQD---HRLLMDRS--IFDNVALpmri 106
Cdd:cd03240 29 GQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEV-----RAQVKLAFENangKKYTITRSlaILENVIF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 107 esISENEIkrrvsaalDKTGLLDKARClpsqlSGGEQQ------RVGIARAV-VNRPTLLLaDEPTGNLDPE-LSNRVLR 178
Cdd:cd03240 100 --CHQGES--------NWPLLDMRGRC-----SGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEEnIEESLAE 163
|
170 180
....*....|....*....|....
gi 1327051661 179 LFEEFNRAGV-TIILATHDIGLVN 201
Cdd:cd03240 164 IIEERKSQKNfQLIVITHDEELVD 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-200 |
2.12e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 18 LQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWfndhditripakdipfLRRNIGIVFQdHRLLMDRSIF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------------AERSIAYVPQ-QAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 98 DNVALpmriesiSENEIKRRVSAALDKTGLLDKARCLPS-----------QLSGGEQQRVGIARAV-VNRPTLLLaDEPT 165
Cdd:PTZ00243 739 GNILF-------FDEEDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVyANRDVYLL-DDPL 810
|
170 180 190
....*....|....*....|....*....|....*
gi 1327051661 166 GNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLV 200
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVHVV 845
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-201 |
2.15e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 25 LKRGEMafLG--GHSGAGKSTLLKLICAIERPTDGRVwfnDHDItRIPAK------DIP-----FLRRNIGIVFQDhrll 91
Cdd:COG1245 363 IREGEV--LGivGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KISYKpqyispDYDgtveeFLRSANTDDFGS---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 mdrSIFDN-VALPMRIESISENEIKrrvsaaldktglldkarclpsQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDP 170
Cdd:COG1245 433 ---SYYKTeIIKPLGLEKLLDKNVK---------------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190
....*....|....*....|....*....|....
gi 1327051661 171 E---LSNRVLRLFEEfNRaGVTIILATHDIGLVN 201
Cdd:COG1245 489 EqrlAVAKAIRRFAE-NR-GKTAMVVDHDIYLID 520
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-174 |
3.04e-07 |
|
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: 50.71 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLmdrsifdNVALPMRIESISENEiKRRVSAALDKTGLLDKARCLPSQL-----------SGGEQQRVGIA 149
Cdd:TIGR00957 1362 ITIIPQDPVLF-------SGSLRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLA 1433
|
170 180
....*....|....*....|....*
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSN 174
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDN 1458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-172 |
3.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 4 FQQVSKAYRGGRQ-ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITripAKDIPFLRRNIG 82
Cdd:PTZ00243 1311 FEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 83 IVFQDhRLLMDRSIFDNVAlPMRIESISEneikrrVSAALDKTGLLDK---------ARCLP--SQLSGGEQQRVGIARA 151
Cdd:PTZ00243 1388 MIPQD-PVLFDGTVRQNVD-PFLEASSAE------VWAALELVGLRERvasesegidSRVLEggSNYSVGQRQLMCMARA 1459
|
170 180
....*....|....*....|..
gi 1327051661 152 VVNRPT-LLLADEPTGNLDPEL 172
Cdd:PTZ00243 1460 LLKKGSgFILMDEATANIDPAL 1481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-177 |
4.31e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAierptdgrvwfnDH------DIT-----RIPAKDIPFLRRNI 81
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHpqgysnDLTlfgrrRGSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 82 GIVfqDHRLLMD---RSIFDNVALPMRIESISeneIKRRVSAA--------LDKTGLLDKARCLPSQ-LSGGEQQRVGIA 149
Cdd:PRK10938 339 GYV--SSSLHLDyrvSTSVRNVILSGFFDSIG---IYQAVSDRqqklaqqwLDILGIDKRTADAPFHsLSWGQQRLALIV 413
|
170 180
....*....|....*....|....*...
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPelSNRVL 177
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDP--LNRQL 439
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-169 |
5.11e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVSKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVW---------FNDHDITRIPA 71
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavFSQHHVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 72 KDIPFLrrnigivfqdhrlLMDRSiFDNVAlpmriesiseneiKRRVSAALDKTGLLDKARCLPS-QLSGGEQQRVGIAR 150
Cdd:PLN03073 588 SSNPLL-------------YMMRC-FPGVP-------------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAK 640
|
170
....*....|....*....
gi 1327051661 151 AVVNRPTLLLADEPTGNLD 169
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLD 659
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-202 |
9.15e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGGRQ-------------------ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfn 62
Cdd:PRK13545 5 VKFEHVTKKYKMYNKpfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 63 dhditripakDIPFLRRNIGIvfqDHRLLMDRSIFDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGE 142
Cdd:PRK13545 82 ----------DIKGSAALIAI---SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 143 QQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNT 202
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-191 |
1.19e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDipfLRRN 80
Cdd:PLN03130 1238 IKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDHRLLMDRSIFD--------NVALPMRIESISENEIKRRVSAALD----KTGlldkarclpSQLSGGEQQRVGI 148
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNldpfnehnDADLWESLERAHLKDVIRRNSLGLDaevsEAG---------ENFSVGQRQLLSL 1385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLD---PELSNRVLRlfEEFNRAGVTII 191
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDvrtDALIQKTIR--EEFKSCTMLII 1429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-197 |
1.33e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 25 LKRGEMafLG--GHSGAGKSTLLKLICAIERPTDGRVwfnDHDIT------RI-PAKDIP---FLRRNIGIvfqdhrllM 92
Cdd:PRK13409 362 IYEGEV--IGivGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisykpqYIkPDYDGTvedLLRSITDD--------L 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDN-VALPMRIESISENEIKrrvsaaldktglldkarclpsQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPE 171
Cdd:PRK13409 429 GSSYYKSeIIKPLQLERLLDKNVK---------------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*....
gi 1327051661 172 ---LSNRVLRLFEEFNRAGVTIIlaTHDI 197
Cdd:PRK13409 488 qrlAVAKAIRRIAEEREATALVV--DHDI 514
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-197 |
1.49e-06 |
|
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: 47.93 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 13 GGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERpTDGRVWFNDHDITRIPAKDipfLRRNIGIVFQdhRLLM 92
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQK---WRKAFGVIPQ--KVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 93 DRSIFDNVALPMriESISENEIKRrvsaALDKTGLLDKARCLPSQL-----------SGGEQQRVGIARAVVNRPTLLLA 161
Cdd:cd03289 89 FSGTFRKNLDPY--GKWSDEEIWK----VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 162 DEPTGNLDPeLSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:cd03289 163 DEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
24-201 |
1.60e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.77 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 24 HLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLLMDRSI--FDNVA 101
Cdd:pfam13304 117 ELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVrgLKLAD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 102 LPMRIESISENEIKRRVSAALDKTGLL---DKARCLP-SQLSGGEQQ---RVGIARAVVNRPTLLLADEPTGNLDPELSN 174
Cdd:pfam13304 197 LNLSDLGEGIEKSLLVDDRLRERGLILlenGGGGELPaFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLR 276
|
170 180
....*....|....*....|....*..
gi 1327051661 175 RVLRLFEEFNRAGVTIILATHDIGLVN 201
Cdd:pfam13304 277 RLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-196 |
1.69e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 5 QQVSKAYrGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRV-WFNDHditripakdipflrrNIGI 83
Cdd:PRK15064 323 ENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENA---------------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 VFQDH--RLLMDRSIFDNVALPMR-------IESI------SENEIKRRVSAaldktglldkarclpsqLSGGEQQRVGI 148
Cdd:PRK15064 387 YAQDHayDFENDLTLFDWMSQWRQegddeqaVRGTlgrllfSQDDIKKSVKV-----------------LSGGEKGRMLF 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 149 ARAVVNRPTLLLADEPTGNLDPElS----NRVLRLFEefnraGvTIILATHD 196
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDME-SieslNMALEKYE-----G-TLIFVSHD 494
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
106-197 |
2.09e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.36 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 106 IESISENEIKRRVSAALDKTGLLDKArclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNR 185
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAE 187
|
90
....*....|..
gi 1327051661 186 AGVTIILATHDI 197
Cdd:cd03236 188 DDNYVLVVEHDL 199
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-174 |
4.67e-06 |
|
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: 46.06 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYRGG-RQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPakdIPFLRRN 80
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 81 IGIVFQDhRLLMDRSIFDNVAlPMRIESISeneikrRVSAALDKTGLLDKARCLPSQL-----SGGEQQRVG------IA 149
Cdd:cd03288 97 LSIILQD-PILFSGSIRFNLD-PECKCTDD------RLWEALEIAQLKNMVKSLPGGLdavvtEGGENFSVGqrqlfcLA 168
|
170 180
....*....|....*....|....*
gi 1327051661 150 RAVVNRPTLLLADEPTGNLDPELSN 174
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATEN 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-222 |
7.66e-06 |
|
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: 46.48 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 12 RGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhditripakdipFLRRNIGIVFQDHRLL 91
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------------HMKGSVAYVPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 92 MDrSIFDNVALPMRIEsiseneiKRRVSAALDKTGLLDKARCLPS-----------QLSGGEQQRVGIARAVVNRPTLLL 160
Cdd:TIGR00957 712 ND-SLRENILFGKALN-------EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327051661 161 ADEPTGNLDPELSNRVlrlFE-----EFNRAGVTIILATHDIGLVntrPQYRH-LELNQGFLSEVEDY 222
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHI---FEhvigpEGVLKNKTRILVTHGISYL---PQVDViIVMSGGKISEMGSY 845
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-192 |
1.05e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVWFNDHDITRIPAKDIpfLRRNIGIVFQDHRllmDRSI 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA--INHGFALVTEERR---STGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNValpmrieSISENEIKRRVSAALDKTGLLDKARC--------------LPSQ------LSGGEQQRVGIARAVVNRP 156
Cdd:PRK10982 338 YAYL-------DIGFNSLISNIRNYKNKVGLLDNSRMksdtqwvidsmrvkTPGHrtqigsLSGGNQQKVIIGRWLLTQP 410
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327051661 157 TLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
1.12e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 2 IKFQQVSKAYrGGRQALQKVDFHLKRGemAFLG--GHSGAGKSTLLKLICAIERPTDGRVWFNDhditriPAKdipflrr 79
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPG--GIVGiiGPNGAGKSTLFKMITGQEQPDSGTIKIGE------TVK------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 80 nIGIVFQDHRLLMD-RSIFDNVALPMRIESISENEIKRR--VSAALDKTGLLDKarcLPSQLSGGEQQRVGIARAVVNRP 156
Cdd:PRK11819 389 -LAYVDQSRDALDPnKTVWEEISGGLDIIKVGNREIPSRayVGRFNFKGGDQQK---KVGVLSGGERNRLHLAKTLKQGG 464
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327051661 157 TLLLADEPTGNLDPElsnrVLRLFEE--FNRAGVTIILaTHD 196
Cdd:PRK11819 465 NVLLLDEPTNDLDVE----TLRALEEalLEFPGCAVVI-SHD 501
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-208 |
1.84e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAieRP----TDGRVWFNDHDITRIPAKDipflRRNIGI- 83
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEE----RAHLGIf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 84 -VFQ---------DHRLLM----DRSIFDNvaLPmRIESISENEIkrrVSAALDKTGLLDK--ARCLPSQLSGGEQQRVG 147
Cdd:CHL00131 88 lAFQypieipgvsNADFLRlaynSKRKFQG--LP-ELDPLEFLEI---INEKLKLVGMDPSflSRNVNEGFSGGEKKRNE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327051661 148 IARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVN-TRPQYRH 208
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyIKPDYVH 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-196 |
2.14e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 2.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 137 QLSGGEQQRVGIA-----RAVVNRPTLLLaDEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-200 |
2.48e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 17 ALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAIERPTDGrvwfndhDITRipAKDIPFLRRNIGIVFQdhrllmdRSI 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDR--NGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 97 FDNVALPMRIESISENEIKRRVSAALDKTGLLDKARCLPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRV 176
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|....
gi 1327051661 177 LRLFEEFNRAGVTIILATHDIGLV 200
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQV 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-197 |
5.49e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 35 GHSGAGKSTLLKLICAIERPTDGrvwfndhDITRIPAKDiPFLRRNIGIVFQDH-RLLMDRSIfdNVAL-PMRIESISEn 112
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPNLG-------DYDEEPSWD-EVLKRFRGTELQDYfKKLANGEI--KVAHkPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 113 EIKRRVSAALDKT---GLLDKA-----------RCLpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLR 178
Cdd:COG1245 175 VFKGTVRELLEKVderGKLDELaeklglenildRDI-SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVAR 253
|
170
....*....|....*....
gi 1327051661 179 LFEEFNRAGVTIILATHDI 197
Cdd:COG1245 254 LIRELAEEGKYVLVVEHDL 272
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-202 |
9.93e-05 |
|
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: 42.22 E-value: 9.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327051661 138 LSGGEQQRVGIARAVVNR---PTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNT 202
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-197 |
1.55e-04 |
|
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: 41.02 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327051661 138 LSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPEL---SNRVLRLFEEFNRAgvTIILATHDI 197
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQrlnAARAIRRLSEEGKK--TALVVEHDL 132
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-196 |
1.71e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 27 RGEMAFLGGHSGAGKSTLLKLICAIERPTDGRVwfndhditripakdipflrrnigivfqdhrllmdrsifdnvalpmri 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 107 ESISENEIKRRVSAALDKTGLLDKarclPSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLR------LF 180
Cdd:smart00382 34 IYIDGEDILEEVLDQLLLIIVGGK----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170
....*....|....*.
gi 1327051661 181 EEFNRAGVTIILATHD 196
Cdd:smart00382 110 LLKSEKNLTVILTTND 125
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-196 |
2.47e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 1 MIKFQQVsKAYRGGRQALQKVDFHLKRGEMAFLGGHSGAGKSTLLKLICAiERPTDG----------RVWFNDHditrIP 70
Cdd:PRK10636 1 MIVFSSL-QIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGgsytfpgnwqLAWVNQE----TP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 71 AKDIPFLR------RNIGIVFQDHRLLMDRSIFDNVA-LPMRIESISENEIKRRVSAALDKTGLLDKARCLP-SQLSGGE 142
Cdd:PRK10636 75 ALPQPALEyvidgdREYRQLEAQLHDANERNDGHAIAtIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGW 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327051661 143 QQRVGIARAVVNRPTLLLADEPTGNLDpelSNRVLRLFEEFNRAGVTIILATHD 196
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHD 205
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
11-195 |
5.87e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 11 YRGgrqaLQKVDFHLKRGEMAFLGgHSGAGKSTLLKLICAIERPTDGRVwFNDHDITRIPAKDIPFLRrnIGIVFQDH-R 89
Cdd:COG3593 11 FRS----IKDLSIELSDDLTVLVG-ENNSGKSSILEALRLLLGPSSSRK-FDEEDFYLGDDPDLPEIE--IELTFGSLlS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 90 LLMDRSIFDNVALPMR--IESISE------NEIKRRVSAALDKTG------------------------LLDKARCLPSQ 137
Cdd:COG3593 83 RLLRLLLKEEDKEELEeaLEELNEelkealKALNELLSEYLKELLdgldlelelsldeledllkslslrIEDGKELPLDR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327051661 138 LSGGEQQRVGIA-------RAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATH 195
Cdd:COG3593 163 LGSGFQRLILLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-192 |
9.34e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 9.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 137 QLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIIL 192
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-202 |
9.64e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 9.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327051661 137 QLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDpelSNRVLRLFEEFNRAGVTIILATHDIGLVNT 202
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNT 406
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-197 |
1.26e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 9 KAYRGGrqalQKVDFhlkRGEMAFLGGHSGAGKSTLLKLIC----------------AIERPTDG--------------R 58
Cdd:COG0419 11 RSYRDT----ETIDF---DDGLNLIVGPNGAGKSTILEAIRyalygkarsrsklrsdLINVGSEEasvelefehggkryR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 59 VWFNDHDITRIPAKDIPFLRRNIGIVFQDHRLlmdRSIFDNVAlpmRIESISENEIKRRVSAALDKTGLLDKARCL--PS 136
Cdd:COG0419 84 IERRQGEFAEFLEAKPSERKEALKRLLGLEIY---EELKERLK---ELEEALESALEELAELQKLKQEILAQLSGLdpIE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327051661 137 QLSGGEQQRVGIARAVVnrptlLLADepTGNLDPElsnRVLRLFEEFNRAGVTiilaTHDI 197
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEE---RLERLLDALEELAII----THVI 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
136-223 |
2.07e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 136 SQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDpelSNRVLRLFEEFNRAGVTIILATHDiglvntrpqyRHlelnqgF 215
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNSTMIIISHD----------RH------F 214
|
90
....*....|....
gi 1327051661 216 LSEV------EDYG 223
Cdd:PRK15064 215 LNSVcthmadLDYG 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
102-196 |
2.38e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 102 LPMRIESISE--NEIKRRVSAALDkTGL--LDKARCLPSqLSGGEQQRVGIAR---AVVNRPTLLLaDEPTGNLDPELSN 174
Cdd:PRK00635 439 LPSKSLSIEEvlQGLKSRLSILID-LGLpyLTPERALAT-LSGGEQERTALAKhlgAELIGITYIL-DEPSIGLHPQDTH 515
|
90 100
....*....|....*....|..
gi 1327051661 175 RVLRLFEEFNRAGVTIILATHD 196
Cdd:PRK00635 516 KLINVIKKLRDQGNTVLLVEHD 537
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
114-196 |
2.39e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.01 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 114 IKRRVSAALD-KTGLLDKARCLPSqLSGGEQQRVGIARAVVNRPT--LLLADEPTGNLDPELSNRVLRLFEEFNRAGVTI 190
Cdd:cd03270 114 IRERLGFLVDvGLGYLTLSRSAPT-LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTV 192
|
....*.
gi 1327051661 191 ILATHD 196
Cdd:cd03270 193 LVVEHD 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
106-197 |
2.63e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.25 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 106 IESISENEIKRRVSAALDKTGLLDKARclpSQLSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNR 185
Cdd:PRK13409 184 LKKVDERGKLDEVVERLGLENILDRDI---SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE 260
|
90
....*....|..
gi 1327051661 186 aGVTIILATHDI 197
Cdd:PRK13409 261 -GKYVLVVEHDL 271
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
136-201 |
3.16e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 3.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 136 SQLSGGEQQRVGIARAVVN---RPTLLLADEPTGNLDPELSNRVLRLF-EEFNRAGVTIILATHDIGLVN 201
Cdd:COG1106 201 SEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFlDLANKNNAQLIFTTHSTELLD 270
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
21-63 |
4.08e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.62 E-value: 4.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1327051661 21 VDFHLKR--GEMAFLGGhSGAGKSTLLKLICAIERPTDGRVWFND 63
Cdd:COG3451 196 FDFHDGLdnGNTLILGP-SGSGKSFLLKLLLLQLLRYGARIVIFD 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-202 |
6.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 6.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 136 SQLSGGEQQRVGIAR---AVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDIGLVNT 202
Cdd:PRK00635 808 SSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKV 877
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
138-197 |
8.56e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 36.88 E-value: 8.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327051661 138 LSGGEQQRVGIARAVVNRPTLLLADEPTGNLDPELSNRVLRLFEEFNRAGVTIILATHDI 197
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL 800
|
|
| |
