|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-221 |
1.35e-123 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 348.96 E-value: 1.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:COG1136 3 PLLELRNLTKSYGtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIVG 221
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-219 |
3.24e-108 |
|
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: 309.81 E-value: 3.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVR 82
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-220 |
1.63e-85 |
|
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: 252.74 E-value: 1.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:COG4181 7 PIIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRAlrKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
1.66e-80 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.83 E-value: 1.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVR 82
Cdd:COG1135 2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:COG1135 82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVrRICDRVAVLENGRIV 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-220 |
7.97e-80 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 238.74 E-value: 7.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrNLTESQAADVR 82
Cdd:COG1126 1 MIEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFY-QGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:COG1126 77 -RKVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFArEVADRVVFMDGGRIV 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-220 |
8.48e-78 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 233.02 E-value: 8.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRs 83
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLElVDRMPKRVLELEDGRLV 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-220 |
7.70e-77 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 243.09 E-value: 7.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:PRK10535 3 ALLELKDIRRSYPsGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
21-217 |
2.93e-75 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 226.52 E-value: 2.93e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKD 100
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154823909 181 VMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:NF038007 180 VLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-214 |
3.75e-75 |
|
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: 225.57 E-value: 3.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSRE 85
Cdd:TIGR03608 1 LKNISKKFGDK---VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 86 IGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVIL 165
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154823909 166 ADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-220 |
1.37e-74 |
|
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: 225.15 E-value: 1.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPG-AQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADV 81
Cdd:cd03258 1 MIELKNVSKVFGDtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVkRICDRVAVMEKGEVV 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-219 |
7.18e-73 |
|
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: 220.09 E-value: 7.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpgaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrNLTESQAADVRs 83
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFY-QGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
8.42e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 218.81 E-value: 8.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQ-PLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesqaa 79
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 dvrSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:COG1116 79 ---GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVM-ELLKQVNKEGRTLIVVTHetSVAE---MCDR 210
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQdELLRLWQETGKTVLFVTH--DVDEavfLADR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-220 |
2.33e-71 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 217.62 E-value: 2.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADV 81
Cdd:COG3638 1 PMLELRNLSKRYPGGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQSFNLIAYKDAVENI---ALPlfYQGVGRALR-------KEKALKLLRAVGLEEWGHHLPSELSGGQKQRI 151
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVlagRLG--RTSTWRSLLglfppedRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEM-CDRTIHIRDGIIV 220
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
8.36e-69 |
|
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: 210.02 E-value: 8.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQ-PLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltesqaadvR 82
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 163 VILADEPTGALDSQTTLEVM-ELLKQVNKEGRTLIVVTHetSVAE---MCDR 210
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQeELLDIWRETGKTVLLVTH--DIDEavfLADR 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-217 |
1.07e-67 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 207.75 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKD 100
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154823909 181 VMELLKQVN-KEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK11629 184 IFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-220 |
4.20e-67 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 209.66 E-value: 4.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGA-QPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVR 82
Cdd:PRK11153 2 IELKNISKVFPQGgRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVkRICDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-220 |
2.21e-65 |
|
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: 202.03 E-value: 2.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRS 83
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAYKDAVENIALPLF-YQGVGRALR-------KEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIAR 155
Cdd:cd03256 79 Q-IGMIFQQFNLIERLSVLENVLSGRLgRRSTWRSLFglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 156 ALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIV 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-220 |
1.39e-64 |
|
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: 199.48 E-value: 1.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRslrNLTESQAADVR 82
Cdd:COG1122 1 IELENLSFSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGK---DITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQS-----FNLIAYKDavenIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:COG1122 75 -RKVGLVFQNpddqlFAPTVEED----VAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVLDDGRIV 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
20-220 |
8.71e-63 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 194.85 E-value: 8.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRsREIGFIFQSFNLIAYK 99
Cdd:TIGR02982 19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQAHNLLGFL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPL-FYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTT 178
Cdd:TIGR02982 98 TARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 179 LEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR02982 178 RDVVELMQKLAKEqGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-220 |
9.17e-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: 195.20 E-value: 9.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYpGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLdTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:COG1127 4 PMIEVRNLTKSF-GDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIGLL-RPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQ------SFNLIaykdavENIALPLF-YQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAI 153
Cdd:COG1127 80 LR-RRIGMLFQggalfdSLTVF------ENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 154 ARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHE-TSVAEMCDRTIHIRDGIIV 220
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
1.42e-62 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 193.84 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 5 ELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvRSR 84
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 85 EIGFIFQS-----FNLIAYKDavenIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:cd03225 76 KVGLVFQNpddqfFGPTVEEE----VAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDG 217
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-219 |
1.77e-62 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.54 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRnlteSQAADVR 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN----DPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 S--REIGFIFQSFNLIAYKDAVENIAL-PLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK09493 74 LirQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDGII 219
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
5.92e-62 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 192.35 E-value: 5.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqaadVRS 83
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
1.08e-61 |
|
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: 200.51 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP--GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:COG1123 260 LLEVRNLSKRYPvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQ----SFNliAYKDAVENIALPLFYQGVG-RALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIA 154
Cdd:COG1123 340 LR-RRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAvVRYIADRVAVMYDGRIV 484
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
2.44e-61 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 192.32 E-value: 2.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpgaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLT----ESQAA 79
Cdd:COG4598 9 LEVRDLHKSF---GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 D------VRSReIGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIA 152
Cdd:COG4598 86 DrrqlqrIRTR-LGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFArDVSSHVVFLHQGRI 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
3.82e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.24 E-value: 3.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaad 80
Cdd:COG3842 3 MPALELENVSKRY-GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vrsREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:COG3842 77 ---RNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEAlALADRIAVMNDGRIE 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-220 |
1.86e-59 |
|
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: 187.12 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVR 82
Cdd:TIGR02315 1 MLEVENLSKVYPNGK--QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNLIAYKDAVENIALP-LFYQGVGRAL-------RKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLlgrfseeDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAkKYADRIVGLKAGEIV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
1.38e-58 |
|
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: 184.25 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESQAAd 80
Cdd:cd03257 1 LLEVKNLSVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILGLLKP-TSGSIIFDGKDLLKLSRRLRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQ----SFNliAYKDAVENIALPLFYQGVGR--ALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAI 153
Cdd:cd03257 79 IRRKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 154 ARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSV-AEMCDRTIHIRDGIIV 220
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVvAKIADRVAVMYAGKIV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-220 |
2.54e-58 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 187.28 E-value: 2.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLR-NLtesqaaDVR 82
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNL------PPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTH---EtsVAEMCDRTIHIRDGIIV 220
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHdqeE--ALELADRVVVMNQGRIE 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-217 |
8.42e-58 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 182.29 E-value: 8.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 15 GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFN 94
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 95 LIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD 174
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154823909 175 SQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK10584 179 RQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-220 |
2.67e-57 |
|
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: 181.54 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltesQAADV 81
Cdd:COG1124 1 MLEVRNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQ----SFNliAYKDAVENIALPLFYQGVGRalRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARA 156
Cdd:COG1124 77 FRRRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAhLCDRVAVMQNGRIV 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-219 |
3.38e-57 |
|
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: 180.30 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRs 83
Cdd:cd03292 1 IEFINVTKTYPNGTA--ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGII 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
6.94e-57 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 180.01 E-value: 6.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRs 83
Cdd:cd03261 1 IELRGLTKSFGG---RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGV-GRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIVA 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
3.01e-56 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 178.58 E-value: 3.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesqaaDVRS 83
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL------PPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAlTMSDRIAVMNKGKIQ 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
5.96e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.95 E-value: 5.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRnlteSQAADVR 82
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLL-RPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:COG1131 73 RR-IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAErLCDRVAIIDKGRIV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
1.53e-55 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 184.34 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDK--GEYLLNGRSLRNLTESqa 78
Cdd:COG1123 3 PLLEVRDLSVRYPG-GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGRisGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 79 adVRSREIGFIFQ----SFNLIAYKDaveNIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:COG1123 80 --LRGRRIGMVFQdpmtQLNPVTVGD---QIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGvVAEIADRVVVMDDGRIV 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-210 |
2.61e-55 |
|
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: 178.71 E-value: 2.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP-GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLD--TFDKGEYLLNGRSLRNLTESQA 78
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 79 ADVRSREIGFIFQ----SFNliaykdAV----ENIALPLFY-QGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGG 146
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN------PVmtvgDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDR 210
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGvVAEIADR 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
8.03e-54 |
|
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: 170.45 E-value: 8.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAdvRS 83
Cdd:cd03229 1 LELKNVSKRYGQKT---VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLfyqgvgralrkekalkllravgleewghhlpselSGGQKQRIAIARALITEPKV 163
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDG 217
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAArLADRVVVLRDG 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-220 |
1.52e-53 |
|
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: 172.83 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKDAVEN 104
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 105 IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVM-E 183
Cdd:cd03294 123 VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQdE 202
|
170 180 190
....*....|....*....|....*....|....*...
gi 1154823909 184 LLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLV 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
3.73e-53 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 171.09 E-value: 3.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG-----EYLLNGRslRNLTE 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT---VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTA--RSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 SQAADVRSRE-IGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAI 153
Cdd:PRK11264 76 QKGLIRQLRQhVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 154 ARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIV 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
6.50e-52 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 168.50 E-value: 6.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPG-AQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltESQAA 79
Cdd:COG4525 1 MSMLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DvrsReiGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:COG4525 77 D---R--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQV-NKEGRTLIVVTHetSVAE 206
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITH--SVEE 197
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
4.12e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 168.71 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAAD 80
Cdd:COG3839 1 MASLELENVSKSY-GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vrsREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:COG3839 75 ---RNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETsvAE---MCDRTIHIRDGIIV 220
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQ--VEamtLADRIAVMNDGRIQ 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
5.90e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.22 E-value: 5.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADVRS 83
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK---PLSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAykDAV-ENIALPlfYQGVGRALRKEKALKLLRAVGLEE----WGHHlpsELSGGQKQRIAIARALI 158
Cdd:COG4619 75 Q-VAYVPQEPALWG--GTVrDNLPFP--FQLRERKFDRERALELLERLGLPPdildKPVE---RLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETSVAE-MCDRTIHIRDG 217
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIErVADRVLTLEAG 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
1.34e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.49 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRNltesqaa 79
Cdd:COG1121 4 MPAIELENLTVSY-GGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 dvRSREIGFIFQSFNLiaykdaveNIALPL---------FYQGVG-----RALRKEKALKLLRAVGLEEWGHHLPSELSG 145
Cdd:COG1121 73 --ARRRIGYVPQRAEV--------DWDFPItvrdvvlmgRYGRRGlfrrpSRADREAVDEALERVGLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGII 219
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-219 |
9.50e-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: 162.12 E-value: 9.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesqaaDVRS 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGR----ALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
3.10e-49 |
|
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: 158.32 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTEsqaADVR 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKlLLRLYDP-TSGEILIDGVDLRDLDL---ESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNLiaYKDAV-ENIalplfyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEP 161
Cdd:cd03228 76 KN-IAYVPQDPFL--FSGTIrENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQvNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-220 |
4.13e-49 |
|
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: 170.40 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTesqAADVR 82
Cdd:COG2274 474 IELENVSFRYPGDSPP-VLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLYEP-TSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNL----IAykdavENIALplfyqgvGRA-LRKEKALKLLRAVGLEEWGHHLP-----------SELSGG 146
Cdd:COG2274 549 RQ-IGVVLQDVFLfsgtIR-----ENITL-------GDPdATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGG 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
7.20e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 159.79 E-value: 7.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSL---RNLTESQAAD 80
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:COG4161 80 LR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRII 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-220 |
7.68e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.48 E-value: 7.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRS 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALF---DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 --REIGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK11124 80 lrRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIV 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
1.19e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 164.55 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTEsqaAD 80
Cdd:COG4987 332 PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLDP-QSGSITLGGVDLRDLDE---DD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSReIGFIFQS---FN-------LIAYKDAVEnialplfyqgvgralrkEKALKLLRAVGLEEWGHHLP---------- 140
Cdd:COG4987 407 LRRR-IAVVPQRphlFDttlrenlRLARPDATD-----------------EELWAALERVGLGDWLAALPdgldtwlgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 141 -SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
.
gi 1154823909 220 V 220
Cdd:COG4987 548 V 548
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
1.09e-46 |
|
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: 154.38 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadVRs 83
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLE--EWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEIV 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-220 |
2.41e-46 |
|
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: 153.11 E-value: 2.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpgaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTF----DKGEYLLNGRSLRNLTESQA 78
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDLIpgapDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 79 AdVRsREIGFIFQSFNLIAyKDAVENIALPLFYQGV-GRALRKEKALKLLRAVGL-EEWGHHL-PSELSGGQKQRIAIAR 155
Cdd:cd03260 78 E-LR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 156 ALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTHE-TSVAEMCDRTIHIRDGIIV 220
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNmQQAARVADRTAFLLNGRLV 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-220 |
1.12e-45 |
|
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: 152.12 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRNLTESQaadv 81
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLL-KPSSGEVLLDGRDLASLSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQS----FNLIAYkDAVENIALPlfYQGVGRALRKE---KALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:COG1120 73 LARRIAYVPQEppapFGLTVR-ELVALGRYP--HLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHE-TSVAEMCDRTIHIRDGIIV 220
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDlNLAARYADRLVLLKDGRIV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-219 |
3.18e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 154.33 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvr 82
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK09452 86 -RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-220 |
4.33e-45 |
|
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: 150.39 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYpgaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDtFDKGEYLLNGRSLRnlteSQAADV 81
Cdd:COG4555 1 MIEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLK-PDSGSILIDGEDVR----KEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQSFNLIAYKDAVENIAL--PLFyqGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:COG4555 73 R-RQIGVLPDERGLYDRLTVRENIRYfaELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQeVEALCDRVVILHKGKVV 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-220 |
1.83e-44 |
|
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: 155.69 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESQaadvR 82
Cdd:COG4988 337 IELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFLPP-YSGSILINGVDLSDLDPAS----W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQS---FNL-IAykdavENIALplfyqgvGRALRKEKALK-LLRAVGLEEWGHHLP-----------SELSGG 146
Cdd:COG4988 410 RRQIAWVPQNpylFAGtIR-----ENLRL-------GRPDASDEELEaALEAAGLDEFVAALPdgldtplgeggRGLSGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-219 |
1.92e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.77 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqaadVRS 83
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------ARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIA-----LPLFYQGVGRALRKeKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKA-KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKEGR-TLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAmEVADRVVVMSQGNI 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-219 |
2.23e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.06 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEyLLNGRSLrnLTESQAaDVRsre 85
Cdd:PRK11247 15 LNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAP--LAEARE-DTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 86 igFIFQSFNLIAYKDAVENIALPLfyqgvgRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVIL 165
Cdd:PRK11247 85 --LMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 166 ADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
4.94e-44 |
|
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: 146.63 E-value: 4.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADvrs 83
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMtMADRIAVMNDGQIQ 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
6.01e-44 |
|
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: 147.96 E-value: 6.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGrsLRNLTESQAADVR 82
Cdd:TIGR04520 1 IEVENVSFSYPESEKP-ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnGLLLP-TSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQsfN----LIAykdAV--ENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARA 156
Cdd:TIGR04520 77 KK-VGMVFQ--NpdnqFVG---ATveDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-219 |
8.63e-44 |
|
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: 144.46 E-value: 8.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRnlteSQAADVR 82
Cdd:cd03230 1 IEVRNLSKRYGK---KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLL-KPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIalplfyqgvgralrkekalkllravgleewghhlpsELSGGQKQRIAIARALITEPK 162
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDGII 219
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAErLCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-214 |
8.94e-44 |
|
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: 145.75 E-value: 8.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRnltesqaaDVRSReIGFIFQSFNL--- 95
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLE--------KERKR-IGYVPQRRSIdrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 --IAYKDAVeniALPLFYQGVG----RALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:cd03235 83 fpISVRDVV---LMGLYGHKGLfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154823909 170 TGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHI 214
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
2.49e-43 |
|
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: 146.83 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPL--HVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAAD 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLLKP-TSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSReIGFIFQS-----FNLIAYKDavenIALPLFYQGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIA 154
Cdd:TIGR04521 80 LRKK-VGLVFQFpehqlFEETVYKD----IAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEdVAEYADRVIVMHKGKIV 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
6.79e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.13 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaQPLHvlkgINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvrs 83
Cdd:COG3840 2 LRLDDLTYRYGD-FPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALplfyqGVGRALR-----KEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIGL-----GLRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVADGRIA 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-220 |
1.15e-42 |
|
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: 150.61 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 15 GAQPLHVLKGINAQIQEGEMVAIMGASGSGKS-TLLNILGLLDT---FDKGEYLLNGRSLRNLTESQAADVRSREIGFIF 90
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDpaaHPSGSILFDGQDLLGLSERELRRIRGNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 91 Q----SFNliaykdavenialPLF------------YQGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRI 151
Cdd:COG4172 99 QepmtSLN-------------PLHtigkqiaevlrlHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGvVRRFADRVAVMRQGEIV 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
1.37e-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: 141.23 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 5 ELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvRSR 84
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----LRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 85 EIGFIFQsfnliaykdavenialplfyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEPKVI 164
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEM-CDRTIHIRDG 217
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-221 |
3.33e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTesqAADVR 82
Cdd:COG1132 340 IEFENVSFSYPGDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNlLLRFYDP-TSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNL----IAykdavENIALplfyqGVGRALRKE--KALkllRAVGLEEWGHHLP-----------SELSG 145
Cdd:COG1132 414 RQ-IGVVPQDTFLfsgtIR-----ENIRY-----GRPDATDEEveEAA---KAAQAHEFIEALPdgydtvvgergVNLSG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIVG 221
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-220 |
3.33e-42 |
|
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: 145.33 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 37 IMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesqAADVRSreIGFIFQSFNLIAYKDAVENIALPLFYQGVGR 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV----PPHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 117 ALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD----SQTTLEVMELLKQVnkeG 192
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---G 151
|
170 180
....*....|....*....|....*....
gi 1154823909 193 RTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:TIGR01187 152 ITFVFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-220 |
9.83e-42 |
|
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: 147.91 E-value: 9.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPG--------AQPLHVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTfdKGEYLLNGRSLRNL 73
Cdd:COG4172 275 LLEARDLKVWFPIkrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 74 TESQAADVRsREIGFIFQ----SFN---LIAykdavENIALPLFYQGVG--RALRKEKALKLLRAVGL-EEWGHHLPSEL 143
Cdd:COG4172 353 SRRALRPLR-RRMQVVFQdpfgSLSprmTVG-----QIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEF 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 144 SGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRaLAHRVMVMKDGKVV 505
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-221 |
2.60e-41 |
|
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: 139.74 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQ---EGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAY 98
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIALPLfyQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTT 178
Cdd:cd03297 90 LNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154823909 179 LEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIVG 221
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDLSEAEyLADRIVVMEDGRLQY 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-201 |
4.24e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.22 E-value: 4.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrnltesqAADVR 82
Cdd:PRK11248 1 MLQISHLYADYGG-KP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---------PVEGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK11248 69 GAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHE 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHD 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-219 |
4.31e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.49 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTES----------QAADVRSReIGFIF 90
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTR-LTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 91 QSFNLIAYKDAVENI-ALPLFYQGVGRALRKEKALKLLRAVGLEEWGH-HLPSELSGGQKQRIAIARALITEPKVILADE 168
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 169 PTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDGII 219
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKI 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-217 |
6.08e-41 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 140.15 E-value: 6.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG-----EYLLN-----GRSLRN 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALH---AVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRtvqreGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 73 LTESQAadvrsrEIGFIFQSFNLIAYKDAVENIAL------PLFYQGVG--RALRKEKALKLLRAVGLEEWGHHLPSELS 144
Cdd:PRK09984 81 IRKSRA------NTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 145 GGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNK-EGRTLIVVTHETSVA-EMCDRTIHIRDG 217
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYAlRYCERIVALRQG 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
8.81e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.78 E-value: 8.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqAAD 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVG----RALRKEkALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARA 156
Cdd:COG1129 76 AQAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGlidwRAMRRR-ARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 157 LITEPKVILADEPTGALDSQttlEVMELLKQVNK---EGRTLIVVTH---EtsVAEMCDR-TIhIRDGIIVG 221
Cdd:COG1129 155 LSRDARVLILDEPTASLTER---EVERLFRIIRRlkaQGVAIIYISHrldE--VFEIADRvTV-LRDGRLVG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-220 |
1.43e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.80 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 5 ELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRNLTESQAAdvrs 83
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKtLAGLL-KPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSfnliaykdavenialplfyqgvgralrkekalklLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03214 73 RKIAYVPQA----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAaRYADRVILLKDGRIV 177
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-210 |
4.67e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.48 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP--------GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLT 74
Cdd:COG4608 7 LLEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 75 ESQAADVRsREIGFIFQ----SFN---LIAykdavENIALPLFYQGVG-RALRKEKALKLLRAVGL-EEWGHHLPSELSG 145
Cdd:COG4608 87 GRELRPLR-RRMQMVFQdpyaSLNprmTVG-----DIIAEPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALD----SQttleVMELLKQVNKE-GRTLIVVTHETSVAE-MCDR 210
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ----VLNLLEDLQDElGLTYLFISHDLSVVRhISDR 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
4.80e-40 |
|
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: 134.31 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvRSREIGFIFQSFNLIAYKDA 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS----LRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 102 VENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHL----PSELSGGQKQRIAIARALITEPKVILADEPT 170
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-220 |
6.30e-40 |
|
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: 136.08 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQPLHvlkgINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGrslrnlTESQAADVRS 83
Cdd:cd03298 1 VRLDKIRFSY-GEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING------VDVTAAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03298 70 RPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKrLAQRVVFLDNGRIA 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-220 |
1.16e-39 |
|
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: 135.41 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesQAADVRs 83
Cdd:cd03245 3 IEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIaYKDAVENIALplfyqgvGRALRKEKALklLRAV---GLEEWGHHLP-----------SELSGGQKQ 149
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITL-------GAPLADDERI--LRAAelaGVTDFVNKHPngldlqigergRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 150 RIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
1.63e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 137.52 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG--EYLLNGRSLRNLTES--- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiEWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 77 ----------------QAADVRsREIGFIFQSFNLIAYKDAVE-NIALPLFYQGVGRALRKEKALKLLRAVGL-EEWGHH 138
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIR-RRVGVVFQFAEYQLFEQTIEkDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 139 LPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDG 217
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDG 241
|
...
gi 1154823909 218 IIV 220
Cdd:PRK13651 242 KII 244
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-220 |
2.19e-39 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 143.08 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesQAADVRs 83
Cdd:TIGR03375 464 IEFRNVSFAYPGQET-PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI---DPADLR- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIaYKDAVENIALplfyqGVgRALRKEKALKLLRAVGLEEWGHHLPS-----------ELSGGQKQRIA 152
Cdd:TIGR03375 539 RNIGYVPQDPRLF-YGTLRDNIAL-----GA-PYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-200 |
8.71e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.39 E-value: 8.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFD----KGEYLLNGRSLRNLTESQAAdVRSReIGFIFQSFN 94
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRMNDLIPgarvEGEILLDGEDIYDPDVDVVE-LRRR-VGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 95 LIA---YkdavENIALPLFYQGV-GRALRKEKALKLLRAVGLeeWG------HHLPSELSGGQKQRIAIARALITEPKVI 164
Cdd:COG1117 103 PFPksiY----DNVAYGLRLHGIkSKSELDEIVEESLRKAAL--WDevkdrlKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTH 200
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILEL-KKDYTIVIVTH 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-214 |
1.62e-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: 139.34 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTesqaADVR 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVDP-TEGSIAVNGVPLADAD----ADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSfNLIAYKDAVENIALPLFYQG---VGRALRKEKALKLLRAVGLeewGHHLP-----SELSGGQKQRIAIA 154
Cdd:TIGR02857 395 RDQIAWVPQH-PFLFAGTIAENIRLARPDASdaeIREALERAGLDEFVAALPQ---GLDTPigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-220 |
2.28e-38 |
|
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: 132.84 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRNLTESQaadvrsREIGFIFQSFNLIAYK 99
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFI-KPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTL 179
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 180 EVMELLKQVNKE-GRTLIVVTHE-TSVAEMCDRTIHIRDGIIV 220
Cdd:cd03299 167 KLREELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKLI 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-217 |
3.00e-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: 132.17 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYP----GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLL-----NILGlldtfDKGEYLLNGRS--- 69
Cdd:COG4778 3 TLLEVENLSKTFTlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYLP-----DSGSILVRHDGgwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 70 -LRNLTESQAADVRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHL-PSELSGGQ 147
Cdd:COG4778 78 dLAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 148 KQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDG 217
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREaVADRVVDVTPF 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-216 |
4.59e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.06 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRnltesQAADV 81
Cdd:COG4133 1 MMLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-----DARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQsfnLIAYKD---AVENIAlplFYQGV-GRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:COG4133 73 YRRRLAYLGH---ADGLKPeltVRENLR---FWAALyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEmCDRTIHIRD 216
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-220 |
1.51e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDtFDKGEYLLNGRSLrnlTESQAADV 81
Cdd:PRK13635 5 IIRVEHISFRYPDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLnGLLL-PEAGTITVGGMVL---SEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK13635 80 R-RQVGMVFQNPDNQFVGATVQDdVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKEGR-TLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-220 |
2.03e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 132.91 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 11 KTYPGAQP--LHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDkGEYLLNGRSLRNLTESQAADVRSrEIG 87
Cdd:PRK15079 24 KQWFWQPPktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKATD-GEVAWLGKDLLGMKDDEWRAVRS-DIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 88 FIFQ----SFN---LIAykdavENIALPL--FYQGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:PRK15079 102 MIFQdplaSLNprmTIG-----EIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEmcdrtiHIRDGIIV 220
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVK------HISDRVLV 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-200 |
2.35e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 15 GAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDT-FD-KGEYLLNGRSLRNLtesqaaDVRSREIGFIFQ 91
Cdd:COG4136 12 GGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPaFSaSGEVLLNGRRLTAL------PAEQRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 SFNLIAYKDAVENI--ALPlfyQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:COG4136 84 DDLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|..
gi 1154823909 170 TGALDSQTTLEVMEL-LKQVNKEGRTLIVVTH 200
Cdd:COG4136 161 FSKLDAALRAQFREFvFEQIRQRGIPALLVTH 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-220 |
7.87e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.81 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGA------QPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLT 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 75 ESQAADVRsREIGFIFQ----SFNliAYKDAVENIALPLFY-QGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQK 148
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdsisAVN--PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRT-LIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLVErFCQRVMVMDNGQIV 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-221 |
1.53e-36 |
|
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: 125.62 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRNLTESQAadvR 82
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFASPRDA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQsfnliaykdavenialplfyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEPK 162
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH---EtsVAEMCDRTIHIRDGIIVG 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHrldE--VFEIADRVTVLRDGRVVG 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-220 |
2.29e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKDA 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 102 VENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154823909 182 M-ELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK10070 204 QdELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVV 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-210 |
2.81e-36 |
|
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: 127.85 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRNLTESQAA 79
Cdd:COG0411 2 DPLLEVRGLTKRFGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY-RPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 D---VRSreigfiFQSFNLIAYKDAVENIALPLFYQ----------GVGRALRKE-----KALKLLRAVGLEEWGHHLPS 141
Cdd:COG0411 78 RlgiART------FQNPRLFPELTVLENVLVAAHARlgrgllaallRLPRARREEreareRAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 142 ELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDR 210
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDlVMGLADR 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-221 |
3.41e-36 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 126.91 E-value: 3.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVR 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK10908 79 -RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIVG 221
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLHG 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-210 |
4.36e-36 |
|
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: 126.78 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRNLTESQAAD-- 80
Cdd:cd03219 1 LEVRGLTKRFGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFL-RPTSGSVLFDGEDITGLPPHEIARlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 -VRSREIGFIFQSF----NL-IAYKDAVENIALPLFYQGVGRALRkEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:cd03219 77 iGRTFQIPRLFPELtvleNVmVAAQARTGSGLLLARARREEREAR-ERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDR 210
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVMSLADR 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-220 |
4.86e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 126.89 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPgAQPLH-VLKGINAQIQEGEMVAIMGASGSGKSTllnILGLLDTF---DKGEYLLNGRSLRNLTESqaa 79
Cdd:cd03249 1 IEFKNVSFRYP-SRPDVpILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFydpTSGEILLDGVDIRDLNLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRSReIGFIFQSFNL----IAykdavENIALPLFYQG---VGRALRKEKALKLLraVGLEEWGHHL----PSELSGGQK 148
Cdd:cd03249 74 WLRSQ-IGLVSQEPVLfdgtIA-----ENIRYGKPDATdeeVEEAAKKANIHDFI--MSLPDGYDTLvgerGSQLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-217 |
5.02e-36 |
|
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: 126.08 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRnlteSQAADVRs 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIalpLFY---QGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHL---RFYarlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEM-CDRTIHIRDG 217
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
5.76e-36 |
|
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: 126.43 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAadvrSREIgfIFQSFNLIAYKDA 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGP----DRMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 102 VENIALPLfyQGVGRALRKEKALKLLRA----VGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQT 177
Cdd:TIGR01184 72 RENIALAV--DRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154823909 178 TLEVMELLKQVNKEGR-TLIVVTHETSVAE-MCDRTIHIRDG 217
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRvTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-210 |
7.96e-36 |
|
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: 124.97 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTF-DKGEYLLNGRSLRnltesqaADVRSREIGFIFQsfnliay 98
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLD-------KRSFRKIIGYVPQ------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 kdavENIALPlfYQGVGRALRKEKALKllravgleewghhlpsELSGGQKQRIAIARALITEPKVILADEPTGALDSQTT 178
Cdd:cd03213 90 ----DDILHP--TLTVRETLMFAAKLR----------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190
....*....|....*....|....*....|....
gi 1154823909 179 LEVMELLKQVNKEGRTLIVVTHETS--VAEMCDR 210
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPSseIFELFDK 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-220 |
8.31e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 8.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 28 QIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRSLRNLTESQaadvrsREIGFIFQSFNLIAYKDAVENIA 106
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNlIAGFL-TPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 107 LplfyqGVGRALR-----KEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:PRK10771 94 L-----GLNPGLKlnaaqREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154823909 182 MELLKQVNKEGR-TLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK10771 169 LTLVSQVCQERQlTLLMVSHSLEdAARIAPRSLVVADGRIA 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
2.29e-35 |
|
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: 130.94 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAadvr 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLDP-LQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAyKDAVENIALplfyqgvGRA-LRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQR 150
Cdd:TIGR02868 408 RRRVSVCAQDAHLFD-TTVRENLRL-------ARPdATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNkEGRTLIVVTH 200
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITH 528
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
3.01e-35 |
|
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: 124.40 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRnlteSQAADVRs 83
Cdd:cd03265 1 IEVENLVKKYGDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEM-CDRTIHIRDGIIV 220
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQlCDRVAIIDHGRII 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-220 |
3.50e-35 |
|
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: 125.30 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYP------GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTE 75
Cdd:TIGR02769 1 SLLEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 SQAADVRsREIGFIFQ----SFNliAYKDAVENIALPL-FYQGVGRALRKEKALKLLRAVGLE-EWGHHLPSELSGGQKQ 149
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQdspsAVN--PRMTVRQIIGEPLrHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 150 RIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQsFCQRVAVMDKGQIV 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-205 |
7.36e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvr 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK11607 91 -RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154823909 163 VILADEPTGALDSQ----TTLEVMELLKQVnkeGRTLIVVTHETSVA 205
Cdd:PRK11607 170 LLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEA 213
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-220 |
1.43e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.79 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTY------PGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlt 74
Cdd:COG4167 2 SALLEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 75 ESQAADVRSREIGFIFQ----SFNliaykdavenialPlfYQGVGRAL--------------RKEKALKLLRAVGL-EEW 135
Cdd:COG4167 78 EYGDYKYRCKHIRMIFQdpntSLN-------------P--RLNIGQILeeplrlntdltaeeREERIFATLRLVGLlPEH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 136 GHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD----SQTTLEVMELLKqvnKEGRTLIVVTHETSVAEmcdrt 211
Cdd:COG4167 143 ANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDmsvrSQIINLMLELQE---KLGISYIYVSQHLGIVK----- 214
|
....*....
gi 1154823909 212 iHIRDGIIV 220
Cdd:COG4167 215 -HISDKVLV 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
3.80e-34 |
|
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: 121.15 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGeMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltesQAADVRS 83
Cdd:cd03264 1 LQLENLTKRYGK---KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03264 73 R-IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNkEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-220 |
8.16e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.05 E-value: 8.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 5 ELSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltesqAADVRSR 84
Cdd:cd03226 1 RIENISFSYKKGT--EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-------KAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 85 EIGFIFQSFNLIAYKDAVEN---IALPLFYQGVGRAlrkEKALKLLRAVGLEEWghHlPSELSGGQKQRIAIARALITEP 161
Cdd:cd03226 72 SIGYVMQDVDYQLFTDSVREellLGLKELDAGNEQA---ETVLKDLDLYALKER--H-PLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-217 |
8.41e-34 |
|
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: 119.24 E-value: 8.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLL-DTfdKGEYLLNGRSLRNLTESQaadv 81
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARlILGLLrPT--SGRVRLDGADISQWDPNE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQSFNLIAYKDAvENIalplfyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEP 161
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIA-ENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-201 |
9.48e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 123.99 E-value: 9.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaad 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDV---VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vrsREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK11000 75 ---RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1154823909 161 PKVILADEPTGALDS----QTTLEVMELLKQVnkeGRTLIVVTHE 201
Cdd:PRK11000 152 PSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHD 193
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-200 |
2.01e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 122.64 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesqaaD 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK11650 73 PADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154823909 161 PKVILADEPTGALDS----QTTLEVMELLKQVnkeGRTLIVVTH 200
Cdd:PRK11650 153 PAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTH 193
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-219 |
3.83e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 118.81 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 26 NAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvrsREIGFIFQSFNLIAYKDAVENI 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 106 ALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELL 185
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154823909 186 KQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGII 219
Cdd:TIGR01277 172 KQLCSErQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
9.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.41 E-value: 9.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP-GAQplhVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTfDKGEYLLNGRSLRnLTESQAAD 80
Cdd:PRK13639 1 ILETRDLKYSYPdGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKP-TSGEVLIKGEPIK-YDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQSFNLIAYKDAV-ENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK13639 76 VR-KTVGIVFQNPDDQLFAPTVeEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEM-CDRTIHIRDGIIVG 221
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIK 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-220 |
9.94e-33 |
|
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: 117.76 E-value: 9.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDtfdkGEYLLNGRSLRNLTESQAADVRSReIGFIFQSFNLIAYK 99
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVE----GGGTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIA----LPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDS 175
Cdd:cd03234 97 TVRETLTytaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154823909 176 QTTLEVMELLKQVNKEGRTLIVVTHE--TSVAEMCDRTIHIRDGIIV 220
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-210 |
1.16e-32 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 120.21 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKS-TLLNILGLL--DTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQ----SFNliA 97
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqTAFALMGLLaaNGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQdpmtSLN--P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 YKDAVENIALPL-FYQGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRIAIARALITEPKVILADEPTGAL 173
Cdd:PRK09473 113 YMRVGEQLMEVLmLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 174 DSQTTLEVMELLKQVNKEGRT-LIVVTHETS-VAEMCDR 210
Cdd:PRK09473 193 DVTVQAQIMTLLNELKREFNTaIIMITHDLGvVAGICDK 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-220 |
1.44e-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: 116.93 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvrs 83
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENialpLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:cd03268 72 RRIGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSeIQKVADRIGIINKGKLI 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
1.50e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNGRSLRnLTESQAAdv 81
Cdd:COG3845 5 ALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILyGLY-QPDSGEILIDGKPVR-IRSPRDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQSFNLIAYKDAVENIALPLfYQGVGRALRKEKALKLLRAVGlEEWGHHLP-----SELSGGQKQRIAIARA 156
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENIVLGL-EPTKGGRLDRKAARARIRELS-ERYGLDVDpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH---EtsVAEMCDR-TIhIRDGIIVG 221
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHklrE--VMAIADRvTV-LRRGKVVG 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-220 |
1.75e-32 |
|
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: 117.33 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadVRSReIGFIFQSFNLIAyK 99
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSM-IGVVLQDTFLFS-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALplfyqgvGRAL-RKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIAIARALITEPKVILAD 167
Cdd:cd03254 92 TIMENIRL-------GRPNaTDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 168 EPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-220 |
2.01e-32 |
|
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: 116.76 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFdKGEYLLNGRSLRNLtesqAADVR 82
Cdd:cd03224 1 LEVENLNAGYGK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPPR-SGSIRFDGRDITGL----PPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SRE-IGFIFQSFNLIAYKDAVENIALPLFYQG-VGRALRKEKALKLLRAvgLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:cd03224 73 ARAgIGYVPEGRRIFPELTVEENLLLGAYARRrAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRAYVLERGRVV 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-220 |
2.75e-32 |
|
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: 116.95 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqAADVRs 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQsfNLIAYKDAV-ENIALplfyqGVGRALRKEkALKLLRAVGLEEWGHHLP-----------SELSGGQKQRI 151
Cdd:cd03251 76 RQIGLVSQ--DVFLFNDTVaENIAY-----GRPGATREE-VEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-220 |
5.62e-32 |
|
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: 121.75 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqAADVR 82
Cdd:TIGR02203 330 DVEFRNVTFRYPGRD-RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQsfNLIAYKDAV-ENIALplfyqGVGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQR 150
Cdd:TIGR02203 406 -RQVALVSQ--DVVLFNDTIaNNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQR 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
9.93e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 9.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAADVRS 83
Cdd:PRK13647 5 IEVEDLHFRYKDGT--KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAYKDAV-ENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK13647 80 K-VGLVFQDPDDQVFSSTVwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVL 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-220 |
1.04e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 118.28 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKDAVEN 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 105 ialpLFYqGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:COG4148 98 ----LLY-GRKRAPRAERRISFDEVVELLGIGHLLdrrPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154823909 182 MELLKQVNKEGRTLIV-VTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG4148 173 LPYLERLRDELDIPILyVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
1.67e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 116.99 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYP-------GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNL 73
Cdd:PRK11308 3 QPLLQAIDLKKHYPvkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 74 TESQAADVRsREIGFIFQ----SFNLiayKDAVENI-ALPLFYQ-GVGRALRKEKALKLLRAVGLE-EWGHHLPSELSGG 146
Cdd:PRK11308 83 DPEAQKLLR-QKIQIVFQnpygSLNP---RKKVGQIlEEPLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEmcdrtiHIRDGIIV 220
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVE------HIADEVMV 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
6.61e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.03 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPL--HVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQaad 80
Cdd:COG1101 2 LELKNLSKTFNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSLPP-DSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vRSREIGFIFQ------SFNL-IAykdavENIALPL-------FYQGVGRALRKE--KALKLLRaVGLEewgHHLPSE-- 142
Cdd:COG1101 78 -RAKYIGRVFQdpmmgtAPSMtIE-----ENLALAYrrgkrrgLRRGLTKKRRELfrELLATLG-LGLE---NRLDTKvg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 -LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETSVA-EMCDRTIHIRDGII 219
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKiVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGRI 227
|
.
gi 1154823909 220 V 220
Cdd:COG1101 228 I 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
7.14e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.73 E-value: 7.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAAD 80
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLnGLLQP-TSGTVTIGERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVE-NIAL-PLFYqGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:PRK13634 82 PLRKKVGIVFQFPEHQLFEETVEkDICFgPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIVG 221
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEdAARYADQIVVMHKGTVFL 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.00e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLR--NLTESQa 78
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILtGLLKP-QSGEIKIDGITISkeNLKEIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 79 advrsREIGFIFQS----FNLIAYKDaveNIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:PRK13632 83 -----KKIGIIFQNpdnqFIGATVED---DIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEG-RTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-220 |
1.78e-30 |
|
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: 112.32 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadVRs 83
Cdd:cd03253 1 IEFENVTFAYDPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQS---FNL-----IAY------KDAVENIA-----------LPLFYQG-VGralrkEKALKLlravgleewgh 137
Cdd:cd03253 75 RAIGVVPQDtvlFNDtigynIRYgrpdatDEEVIEAAkaaqihdkimrFPDGYDTiVG-----ERGLKL----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 138 hlpselSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03253 139 ------SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDG 211
|
...
gi 1154823909 218 IIV 220
Cdd:cd03253 212 RIV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-220 |
2.38e-30 |
|
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: 116.83 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTF--DKGEYLLN--------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 67 --------GRSLR-------NLTESQAADVRSReIGFIFQ-SFNLIAYKDAVENI--ALP-LFYQGvGRALrkEKALKLL 127
Cdd:TIGR03269 78 vgepcpvcGGTLEpeevdfwNLSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNVleALEeIGYEG-KEAV--GRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 128 RAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETSV-A 205
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEViE 233
|
250
....*....|....*
gi 1154823909 206 EMCDRTIHIRDGIIV 220
Cdd:TIGR03269 234 DLSDKAIWLENGEIK 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-220 |
3.11e-30 |
|
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: 111.81 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADVRs 83
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH---DLALADPAWLR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSfNLIAYKDAVENIALplfyqgVGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIA 152
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIAL------ADPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-220 |
3.37e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.85 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadV 81
Cdd:PRK11160 337 VSLTLNNVSFTYPD-QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---L 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSReIGFIFQS---FN-------LIAYKDAVEnialplfyqgvgralrkEKALKLLRAVGLEewgHHLPSE--------- 142
Cdd:PRK11160 413 RQA-ISVVSQRvhlFSatlrdnlLLAAPNASD-----------------EALIEVLQQVGLE---KLLEDDkglnawlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 ----LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHE-TSVAEMcDRTIHIRDG 217
Cdd:PRK11160 472 ggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRlTGLEQF-DRICVMDNG 549
|
...
gi 1154823909 218 IIV 220
Cdd:PRK11160 550 QII 552
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
4.29e-30 |
|
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: 110.92 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTY-PGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnlTESQAADV 81
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD----VVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSReIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:cd03266 77 RRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVV 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
5.85e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 112.91 E-value: 5.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALI---ELS---GIEKTypgaqPLHVLKGINAQIQEGEMVAIMGASGSGKS-TLLNILGLLD-----TFDKGEYllNGR 68
Cdd:PRK11022 1 MALLnvdKLSvhfGDESA-----PFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgrvMAEKLEF--NGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 69 SLRNLTESQAADVRSREIGFIFQ----SFNlIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHL---PS 141
Cdd:PRK11022 74 DLQRISEKERRNLVGAEVAMIFQdpmtSLN-PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 142 ELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVN-KEGRTLIVVTHETS-VAEMCDRTIHIRDGII 219
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLAlVAEAAHKIIVMYAGQV 232
|
.
gi 1154823909 220 V 220
Cdd:PRK11022 233 V 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-209 |
8.82e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.84 E-value: 8.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLHV--LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADV 81
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSREIGFIFQSFNLIAYKDAV-ENIAL-PLFYqGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVlKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCD 209
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYAD 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-220 |
8.94e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.19 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPL--------HVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTfdKGEYLLNGRSLRNL 73
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLINS--QGEIWFDGQPLHNL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 74 TESQAADVRSReIGFIFQSFN--LIAYKDAVENIA--LPLFYQGVGRALRKEKALKLLRAVGLE-EWGHHLPSELSGGQK 148
Cdd:PRK15134 353 NRRQLLPVRHR-IQVVFQDPNssLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGR-TLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRaLCHQVIVLRQGEVV 505
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-220 |
1.65e-29 |
|
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: 114.85 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFdKGEYLLNGRSLRNLTEsqaaDVR 82
Cdd:COG4618 331 LSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVWPPT-AGSVRLDGADLSQWDR----EEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNL----IAykdavENIAlplfyqgvgR--ALRKEKALKLLRAVGLEEWGHHLP-----------SELSG 145
Cdd:COG4618 405 GRHIGYLPQDVELfdgtIA-----ENIA---------RfgDADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-205 |
2.66e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.55 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLL-----DTFDKGEYLLNGRSLRNlTESQAADVRsREIGFIFQSFN 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 95 LIAYKDAVENIALPLFYQGVGRAL-----RKEKALKllRAVGLEEWGHHL---PSELSGGQKQRIAIARALITEPKVILA 166
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSKkeldeRVEWALK--KAALWDEVKDRLndyPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 167 DEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTHETSVA 205
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQA 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
2.86e-29 |
|
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: 108.92 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAqplHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFdKGEYLLNGRSLRNLtesqAA 79
Cdd:COG0410 1 MPMLEVENLHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLPPR-SGSIRFDGEDITGL----PP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRSRE-IGF------IFQSFNliaykdaV-ENIALPLFYQGVGRALRK--EKALKLL-RavgLEEWGHHLPSELSGGQK 148
Cdd:COG0410 73 HRIARLgIGYvpegrrIFPSLT-------VeENLLLGAYARRDRAEVRAdlERVYELFpR---LKERRRQRAGTLSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFAlEIADRAYVLERGRIV 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-205 |
4.30e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 111.35 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQaadVRS 83
Cdd:PRK11432 7 VVLKNITKRFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRS---IQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVA 205
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEA 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-220 |
4.56e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltESQAADVRSREiGFIFQS-FNLIAYK 99
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENLWDIRNKA-GMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTL 179
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154823909 180 EVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13633 182 EVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-217 |
5.35e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.44 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAAD 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQSFNLIAYKDAVEN-IALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK13650 79 IR-HKIGMVFQNPDNQFVGATVEDdVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-200 |
2.23e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILG-LLDTFDK----GEYLLNGRSLRNLTE 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrLIELYPEarvsGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 SQAadvrSREIGFIFQSFNLIAYKDAVENIALPLfyqGVGRALRKEKALK------LLRAVGLEEWGHHLPS---ELSGG 146
Cdd:PRK14247 78 IEL----RRRVQMVFQIPNPIPNLSIFENVALGL---KLNRLVKSKKELQervrwaLEKAQLWDEVKDRLDApagKLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTH 200
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-217 |
2.35e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 109.43 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 33 EMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKDAVENialpLFYq 112
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN----LRY- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 113 GVGRALRKEKAL---KLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVN 189
Cdd:TIGR02142 99 GMKRARPSERRIsfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH 178
|
170 180 190
....*....|....*....|....*....|
gi 1154823909 190 KEGRTLIV-VTHE-TSVAEMCDRTIHIRDG 217
Cdd:TIGR02142 179 AEFGIPILyVSHSlQEVLRLADRVVVLEDG 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-220 |
3.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAqPLHVLKGINAQIQEGEMVAIMGASGSGKST---LLNILGLLDTFDKGEYLLNGRslrNLTESQAAD 80
Cdd:PRK13640 6 VEFKHVSFTYPDS-KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI---TLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSReIGFIFQS-FNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK13640 82 IREK-VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-221 |
4.30e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 110.48 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG--EYLLNGRSLRNLTESQAA 79
Cdd:PRK10762 3 ALLQLKGIDKAFPGVK---ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsiLYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DvrsreIGFIFQSFNLIAYKDAVENIALPL-FYQGVGRALRKE---KALKLLRAVGLEEWGHHLPSELSGGQKQRIAIAR 155
Cdd:PRK10762 80 G-----IGIIHQELNLIPQLTIAENIFLGReFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 156 ALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRlKEIFEICDDVTVFRDGQFIA 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
5.63e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAADVRSRE-IGFIFQS-----F 93
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRKGLMKLREsVGMVFQDpdnqlF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKD---AVENIALPlfyqgvgRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPT 170
Cdd:PRK13636 97 SASVYQDvsfGAVNLKLP-------EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 171 GALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDiVPLYCDNVFVMKEGRVI 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-220 |
6.22e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.93 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESqaadvR 82
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLKP-QQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAYKdavenialplFYQGVGRalrkekalkllravgleewghhlpsELSGGQKQRIAIARALITEPK 162
Cdd:cd03247 74 SSLISVLNQRPYLFDTT----------LRNNLGR-------------------------RFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-220 |
9.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.29 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTfDKGEYLLNGRslrNLTESQA--ADVRsREIGFIFQS-----F 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLLKP-TSGKIIIDGV---DITDKKVklSDIR-KKVGLVFQYpeyqlF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKDavenIALPLFYQGVGRALRKEKALKLLRAVGL--EEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTG 171
Cdd:PRK13637 98 EETIEKD----IAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 172 ALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEdVAKLADRIIVMNKGKCE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-220 |
9.54e-28 |
|
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: 109.51 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 24 GINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGE-YLLNGRSLRNLTEsQAADVRSRE---IGFIFQSFNLIAY 98
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIaGVLEP-TSGEvNVRVGDEWVDMTK-PGPDGRGRAkryIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIAlplfyQGVGRALRKE----KALKLLRAVGLEEWG-----HHLPSELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:TIGR03269 380 RTVLDNLT-----EAIGLELPDElarmKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 170 TGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKIV 507
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-217 |
1.35e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.85 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLR--NLTESQA 78
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK---ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 79 ADvrsreIGFIFQSFNLIAYKDAVENI---ALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIAR 155
Cdd:PRK11288 79 AG-----VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 156 ALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDG 217
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
1.91e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 10 EKTypgAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG----EYLLNGRSLRNLTESQAADVRS-- 83
Cdd:PRK13631 33 EKQ---ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvGDIYIGDKKNNHELITNPYSKKik 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ------REIGFIFQSFNLIAYKDAVEN------IALplfyqGVGRALRKEKALKLLRAVGLEE-WGHHLPSELSGGQKQR 150
Cdd:PRK13631 110 nfkelrRRVSMVFQFPEYQLFKDTIEKdimfgpVAL-----GVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDGIIV 220
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
2.44e-27 |
|
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: 104.40 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGlldtfdkGE---------YLLnGRSLR 71
Cdd:COG1119 1 DPLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT-------GDlpptygndvRLF-GERRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 72 NLTesqAADVRSReIGFIFQSF-NLIAYKDAVENIALPLFYQGVGRALR-----KEKALKLLRAVGLEEWGHHLPSELSG 145
Cdd:COG1119 70 GED---VWELRKR-IGLVSPALqLRFPRDETVLDVVLSGFFDSIGLYREptdeqRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEG-RTLIVVTH--ETSVAEMcDRTIHIRDGIIV 220
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhvEEIPPGI-THVLLLKDGRVV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-220 |
4.20e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.87 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKS-TLLNILGLLDT----FDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQ---- 91
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQepmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 SFNLI--AYKDAVENIALplfYQGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRIAIARALITEPKVILA 166
Cdd:PRK15134 104 SLNPLhtLEKQLYEVLSL---HRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 167 DEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSiVRKLADRVAVMQNGRCV 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
4-220 |
4.55e-27 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 107.86 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILglLDTFD--KGEYLLNGRSLRNLtesQAADV 81
Cdd:TIGR02204 338 IEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLL--LRFYDpqSGRILLDGVDLRQL---DPAEL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSReIGFIFQSFNLIAyKDAVENIA---LPLFYQGVGRALRKEKALKLLRAvgLEEWGHHLPSE----LSGGQKQRIAIA 154
Cdd:TIGR02204 413 RAR-MALVPQDPVLFA-ASVMENIRygrPDATDEEVEAAARAAHAHEFISA--LPEGYDTYLGErgvtLSGGQRQRIAIA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETLMK-GRTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-201 |
4.86e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.08 E-value: 4.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSReIGFIFQSFNLIAYKDAVEN 104
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 105 IALPLF-YQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVME 183
Cdd:PRK11831 105 VAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170
....*....|....*....
gi 1154823909 184 LLKQVNKE-GRTLIVVTHE 201
Cdd:PRK11831 185 LISELNSAlGVTCVVVSHD 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-219 |
5.81e-27 |
|
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: 107.43 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 14 PGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAdvrsREIGFIFQSF 93
Cdd:TIGR01842 328 GGKKP--TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKDAvENIALplfyqgVGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIAIARALITEPK 162
Cdd:TIGR01842 402 ELFPGTVA-ENIAR------FGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-220 |
8.74e-27 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 107.52 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADVRs 83
Cdd:TIGR01846 456 ITFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADPAWLR- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSfNLIAYKDAVENIALplfyqgVGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIA 152
Cdd:TIGR01846 531 RQMGVVLQE-NVLFSRSIRDNIAL------CNPGAPFEHVIHAAKLAGAHDFISELPqgyntevgekgANLSGGQRQRIA 603
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRACDRIIVLEKGQIA 670
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-200 |
1.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltESQAADV 81
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS--TSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RS--REIGFIFQSFNLIAYKDAV-ENIALPLFYQGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:PRK13649 81 KQirKKVGLVFQFPESQLFEETVlKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-220 |
1.36e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.64 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESqaaDVRs 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA---SLR- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLiaYKDAV-ENIAlplfYQGVGRALRK--EKALKLLRAVG-LEEWGHHLPSE-------LSGGQKQRIA 152
Cdd:PRK11176 417 NQVALVSQNVHL--FNDTIaNNIA----YARTEQYSREqiEEAARMAYAMDfINKMDNGLDTVigengvlLSGGQRQRIA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-220 |
1.54e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTfDKGEYLLNGRSLRNLTESQAAD 80
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEhqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqNINALLKP-TTGTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVE--------NIALPLfyQGVgralrKEKALKLLRAVGLEEWGHHL-PSELSGGQKQRI 151
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLFEDTVEreiifgpkNFKMNL--DEV-----KNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVN-KEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNeVARYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-220 |
2.06e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTfDKGEYLLNGRSLRNLTESQaaDV 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLLRP-QKGKVLVSGIDTGDFSKLQ--GI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQSFNLIAYKDAVE--------NIALPLFyqgvgrALRKeKALKLLRAVGLEEWGHHLPSELSGGQKQRIAI 153
Cdd:PRK13644 76 R-KLVGIVFQNPETQFVGRTVEedlafgpeNLCLPPI------EIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 154 ARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-220 |
2.65e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.90 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFD---KGEYLLNGRSLrnltESQAADVRSreiGFIFQSFNLI 96
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI----DAKEMRAIS---AYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AYKDAVENialpLFYQG---VGRAL----RKEKALKLLRAVGLEEWGH------HLPSELSGGQKQRIAIARALITEPKV 163
Cdd:TIGR00955 112 PTLTVREH----LMFQAhlrMPRRVtkkeKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS--VAEMCDRTIHIRDGIIV 220
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSseLFELFDKIILMAEGRVA 246
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-217 |
3.03e-26 |
|
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: 100.24 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLdTFDKGEYLLNGRS--------LRNLTesqaadVRsreigfifq 91
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGSIayvsqepwIQNGT------IR--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 sfnliaykdavENIalpLFyqgvGRALRKEKALKLLRAVGLEE----WGHHLPSE-------LSGGQKQRIAIARALITE 160
Cdd:cd03250 84 -----------ENI---LF----GKPFDEERYEKVIKACALEPdleiLPDGDLTEigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 161 PKVILADEPTGALDSQTTLEVME-LLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
3.28e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSL---RNLTESQAADVRsREIGFIFQSFNLIA 97
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLR-KEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 YKDAVENIALPLFYQGVGRALRKEKALK-LLRAVGLEEWGHHL----PSELSGGQKQRIAIARALITEPKVILADEPTGA 172
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154823909 173 LDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-220 |
3.59e-26 |
|
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: 105.29 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 14 PGAQPLHV--------------------LKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRN 72
Cdd:COG5265 346 PDAPPLVVgggevrfenvsfgydperpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYDV-TSGRILIDGQDIRD 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 73 LTEsqaADVRsREIGFIFQS---FNL-----IAY------KDAVENIA-----------LPLFYQ-GVGralrkEKALKL 126
Cdd:COG5265 425 VTQ---ASLR-AAIGIVPQDtvlFNDtiaynIAYgrpdasEEEVEAAAraaqihdfiesLPDGYDtRVG-----ERGLKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 127 lravgleewghhlpselSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAE 206
Cdd:COG5265 496 -----------------SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIV 557
|
250
....*....|....
gi 1154823909 207 MCDRTIHIRDGIIV 220
Cdd:COG5265 558 DADEILVLEAGRIV 571
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-200 |
5.36e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.40 E-value: 5.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLL---NILG-LLDTFD-KGEYLLNGRSLrNLTESQAADVRSReIGFIFQSFNLI 96
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNdLIPGFRvEGKVTFHGKNL-YAPDVDPVEVRRR-IGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AyKDAVENIALP---LFYQG-----VGRALR--------KEKalklLRAVGLEewghhlpseLSGGQKQRIAIARALITE 160
Cdd:PRK14243 104 P-KSIYDNIAYGariNGYKGdmdelVERSLRqaalwdevKDK----LKQSGLS---------LSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTH 200
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTH 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
5.52e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.48 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPgaqPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVr 82
Cdd:PRK09700 5 YISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 srEIGFIFQSFNLIAYKDAVENIAlplfyqgVGRALRK--------------EKALKLLRAVGLEEWGHHLPSELSGGQK 148
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLY-------IGRHLTKkvcgvniidwremrVRAAMMLLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSVC 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-220 |
1.68e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAAD 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSP-DSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VR-----SREIGFIFqsfnliaykdAVENI----ALPLfyqgvGRALRKEKAL--KLLRAVGLEEWGHHLPSELSGGQKQ 149
Cdd:PRK13548 77 RRavlpqHSSLSFPF----------TVEEVvamgRAPH-----GLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 150 RIAIARALI------TEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETSVAEM-CDRTIHIRDGIIV 220
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLV 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-210 |
2.14e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 101.14 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 18 PLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLD-----TFDKgeYLLNGRSLRNLTESQAADVRSREIGFIFQ 91
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwhvTADR--FRWNGIDLLKLSPRERRKIIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 sfNLIAYKDAVENI------ALP------LFYQgvGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRIAIARA 156
Cdd:COG4170 97 --EPSSCLDPSAKIgdqlieAIPswtfkgKWWQ--RFKWRKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIV-VTHE-TSVAEMCDR 210
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDlESISQWADT 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
2.31e-25 |
|
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: 98.12 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTfDKGEYLLNGRSLrnltesqAADVR 82
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIrMILGIILP-DSGEVLFDGKPL-------DIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSFNLiaYKDavENIALPLFYQGVGRALRKEKALK----LLRAVGLEEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:cd03269 70 NR-IGYLPEERGL--YPK--MKVIDQLVYLAQLKGLKKEEARRrideWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIV 220
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-217 |
5.15e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 14 PGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGE----------------YLLNGrSLRNLtesq 77
Cdd:COG4178 373 PDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiarpagarvlflpqrpYLPLG-TLREA---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 78 aadvrsreigfifqsfnlIAYKDAVENIALplfyqgvgralrkEKALKLLRAVGLEEWGHHL------PSELSGGQKQRI 151
Cdd:COG4178 446 ------------------LLYPATAEAFSD-------------AELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQvNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
5.25e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAAD 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGS--KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRsREIGFIFQSFNLIAYKDAVE-NIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK13652 76 VR-KFVGLVFQNPDDQIFSPTVEqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIVG 221
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIVA 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-219 |
6.34e-25 |
|
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: 96.35 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAadvRSREIGFI---------FQ 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedrkreglVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 SFNLIaykdavENIALPLFyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEPKVILADEPTG 171
Cdd:cd03215 92 DLSVA------ENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154823909 172 ALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGII 219
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-220 |
8.14e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.64 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTfDKGEYLLNGRSLRnltesqaADVR 82
Cdd:COG4152 2 LELKGLTKRF-GDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILAP-DSGEVLWDGEPLD-------PEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFifqsfnliaykdaveniaLP--------------LFY----QGVGRALRKEKALKLLRAVGLEEWGHHLPSELS 144
Cdd:COG4152 71 RR-IGY------------------LPeerglypkmkvgeqLVYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 145 GGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH--EtSVAEMCDRTIHIRDGIIV 220
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHqmE-LVEELCDRIVIINKGRKV 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-220 |
8.81e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.72 E-value: 8.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTllnILGLLDTF---DKGEYLLNGRSLRNLtesqaa 79
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLyqpTGGQVLLDGVPLVQY------ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRS--REIGFIFQSFNLIAyKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLP-----SELSGGQKQRIA 152
Cdd:TIGR00958 549 DHHYlhRQVALVGQEPVLFS-GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgSQLSGGQKQRIA 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQvnkEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-220 |
1.07e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.46 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIekTYPGAQPLhvLKGINAQIQEGEMVAIMGASGSGKStlLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRS 83
Cdd:PRK10418 5 IELRNI--ALQAAQPL--VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQ----SFN--LIAYKDAVENIAlplfyqGVGRALRKEKALKLLRAVGLEEWGHHL---PSELSGGQKQRIAIA 154
Cdd:PRK10418 79 RKIATIMQnprsAFNplHTMHTHARETCL------ALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGvVARLADDVAVMSHGRIV 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-220 |
1.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSL-RNLTESQAAD 80
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVE-NIALPLFYQGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEkDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETsvaemcDRTIHIRDGIIV 220
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNM------DQVLRIADEVIV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-219 |
1.28e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYpGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNgrslRNLT------ESQAA 79
Cdd:COG0488 1 LENLSKSF-GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRigylpqEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRS-REigFIFQSFN----LIAYKDAVEniALPLFYQGVGRALRK--------------EKALKLLRAVGLEEWGHHLP 140
Cdd:COG0488 74 DDLTvLD--TVLDGDAelraLEAELEELE--AKLAEPDEDLERLAElqeefealggweaeARAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 141 -SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTT--LEvmELLKqvNKEGrTLIVVTHETS-VAEMCDRTIHIRD 216
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIewLE--EFLK--NYPG-TVLVVSHDRYfLDRVATRILELDR 224
|
...
gi 1154823909 217 GII 219
Cdd:COG0488 225 GKL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-220 |
3.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPL--HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD 80
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAV-ENIALPLFYQGVGRALRKEKALKLLRAVGL-EEWGHHLPSELSGGQKQRIAIARALI 158
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVlKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH-ETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-220 |
4.26e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.53 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfdKGEYLLNGRSLRNLTESQAadvr 82
Cdd:PRK11174 350 IEAEDLEILSPDGKTL--AGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFLPY--QGSLKINGIELRELDPESW---- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGFIFQSFNLIAyKDAVENIALplfyqgvGR-ALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQR 150
Cdd:PRK11174 422 RKHLSWVGQNPQLPH-GTLRDNVLL-------GNpDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQvNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-212 |
5.43e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 5.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 13 YPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfdkgeylLNGRSLRnltesqaadVRSREIGFIFQ 91
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRP-------TSGTVRR---------AGGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 SFNL-----IAYKDAVeniALPLF-YQGVGRALRKEKALKL---LRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:NF040873 63 RSEVpdslpLTVRDLV---AMGRWaRRGLWRRLTRDDRAAVddaLERVGLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTI 212
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-219 |
9.83e-24 |
|
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: 94.53 E-value: 9.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESQaadvR 82
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYmIVGLVKP-DSGKILLDGQDITKLPMHK----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SRE-IGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:cd03218 73 ARLgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH---ETsvAEMCDRTIHIRDGII 219
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHnvrET--LSITDRAYIIYEGKV 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-220 |
1.06e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.99 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYpgaQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGE--YLLNGRSLRNLTESQAAD 80
Cdd:PRK11701 6 LLSVRGLTKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VR--SR-EIGFIFQSfNLIAYKDAVE---NIALPLFYQGV---GRaLRkEKALKLLRAVGLEEWG-HHLPSELSGGQKQR 150
Cdd:PRK11701 83 RRrlLRtEWGFVHQH-PRDGLRMQVSaggNIGERLMAVGArhyGD-IR-ATAGDWLERVEIDAARiDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQ-VNKEGRTLIVVTHETSVAEM-CDRTIHIRDGIIV 220
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.23e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltESQAADV 81
Cdd:PRK13537 6 APIDFRNVEKRY-GDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSReIGFIFQSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:PRK13537 79 RQR-VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDRTIHIRDG 217
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErLCDRLCVIEEG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-217 |
1.23e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFD-----KGEYLLNGRSLRNlTESQAADVRsREIGFIFQS---F 93
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PRTDTVDLR-KEIGMVFQQpnpF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYkdavENIALPLFYQGVGRALRKEKALK--LLRAVGLEEWGHHLPSE---LSGGQKQRIAIARALITEPKVILADE 168
Cdd:PRK14239 99 PMSIY----ENVVYGLRLKGIKDKQVLDEAVEksLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 169 PTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVA-EMCDRTIHIRDG 217
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQAsRISDRTGFFLDG 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-219 |
1.47e-23 |
|
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: 94.07 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 12 TYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltesQAADVR--SREIGFI 89
Cdd:cd03248 20 AYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI------SQYEHKylHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 90 FQSFNLIAyKDAVENIALPLfyQGVGRALRKEKALK-------LLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:cd03248 94 GQEPVLFA-RSLQDNIAYGL--QSCSFECVKEAAQKahahsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNkEGRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-206 |
3.59e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 19 LHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRsREIGFIFQS--FNLI 96
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AYKDAVENIALPLFYQGV--GRALRKEKALkLLRAVGLE-EWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGAL 173
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlpGKAAAARVAW-LLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190
....*....|....*....|....*....|....
gi 1154823909 174 DSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE 206
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVE 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-220 |
4.06e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.54 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 9 IEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAdvrsREIGF 88
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 89 IFQSF---------NLIAYKdavENIALPLFyqgvGRALRKEKAL--KLLRAVGLEEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:PRK11231 81 LPQHHltpegitvrELVAYG---RSPWLSLW----GRLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVM 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-200 |
5.29e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.94 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIA-YKdaVE 103
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPhYK--VR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 104 -NialpLFYqGVGRAlRKEKALKLLRAVGLEewgHHL---PSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTL 179
Cdd:PRK11144 95 gN----LRY-GMAKS-MVAQFDKIVALLGIE---PLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180
....*....|....*....|..
gi 1154823909 180 EVMELLKQVNKEGRTLIV-VTH 200
Cdd:PRK11144 166 ELLPYLERLAREINIPILyVSH 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-220 |
7.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFDkGEYLLNGRslrNLTESQAADV 81
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIdGLFEEFE-GKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsREIGFIFQS-FNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK13642 80 R-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQV-NKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-220 |
8.05e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.74 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAdvrsREIGFIFQSFNL---IA 97
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTpgdIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 YKDAVENIALPlfYQGVGRALRKEKA---LKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD 174
Cdd:PRK10253 98 VQELVARGRYP--HQPLFTRWRKEDEeavTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 175 SQTTLEVMELLKQVNKE-GRTLIVVTHETSVAemCDRTIH---IRDGIIV 220
Cdd:PRK10253 176 ISHQIDLLELLSELNREkGYTLAAVLHDLNQA--CRYASHliaLREGKIV 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-217 |
8.77e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.69 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 16 AQPLHVLKGINAQIQEGEMVAIMGASGSGKS-TLLNILGLLD----TFDKGEYLLNGRS-----LRNLTESQAADVRSRE 85
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEqaggLVQCDKMLLRRRSrqvieLSEQSAAQMRHVRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 86 IGFIFQ----SFNLI--AYKDAVENIALplfYQGVGR--ALRKEK-ALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARA 156
Cdd:PRK10261 106 MAMIFQepmtSLNPVftVGEQIAESIRL---HQGASReeAMVEAKrMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDG 217
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-220 |
1.82e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.68 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNlTESqaaDVRS 83
Cdd:COG4604 2 IEIKNVSKRY-GGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPS---RELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQS--FNL-IAYKDAVenialplfyqGVGR------ALRKE------KALKLLravGLEEWGHHLPSELSGGQK 148
Cdd:COG4604 75 KRLAILRQEnhINSrLTVRELV----------AFGRfpyskgRLTAEdreiidEAIAYL---DLEDLADRYLDELSGGQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETSVAE-MCDRTIHIRDGIIV 220
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFAScYADHIVAMKDGRVV 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-220 |
2.47e-22 |
|
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: 94.42 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAadvrSREIGFIFQSfNLIAYKD 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYLPQE-PYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIALplfyqGVGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:TIGR01193 564 ILENLLL-----GAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 170 TGALDSQTTLEVMELLkqVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:TIGR01193 639 TSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-220 |
3.26e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.01 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESqaadVRS 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS----VLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 REIGFIFQSFNLIAykDAV-ENIALplfyqgvGRALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRI 151
Cdd:PRK10790 415 QGVAMVQQDPVVLA--DTFlANVTL-------GRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSvaemcdrTIHIRDGIIV 220
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLS-------TIVEADTILV 546
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
4.21e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlTESQAADVR 82
Cdd:PRK13648 7 IIVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 sREIGFIFQS----F--NLIAYKDA--VENIALPlfYQGVgralrKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:PRK13648 83 -KHIGIVFQNpdnqFvgSIVKYDVAfgLENHAVP--YDEM-----HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGR-TLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKG 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-217 |
4.30e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 17 QPLHVLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTfDKGEYLLNGRSLrNLTESQAADVRsREIGFIFQSFNL 95
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRP-QKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 -IAYKDAVENIALPLFYQGVGR---ALRKEKALKLLRAVGLEewghHLPSE-LSGGQKQRIAIARALITEPKVILADEPT 170
Cdd:PRK13638 89 qIFYTDIDSDIAFSLRNLGVPEaeiTRRVDEALTLVDAQHFR----HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1154823909 171 GALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDG 217
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDlIYEISDAVYVLRQG 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-198 |
5.59e-22 |
|
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: 89.89 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESQAAdvrSREIGFIFQSFNLIAY 98
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLPV-KSGSIRLDGEDITKLPPHERA---RAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIALPLFYQGVGRALRKEKALKLLRAvgLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTT 178
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180
....*....|....*....|
gi 1154823909 179 LEVMELLKQVNKEGRTLIVV 198
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILL 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-217 |
7.48e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 92.93 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL------GlldTFDkGEYLLNG--RSLRNLT 74
Cdd:NF040905 1 ILEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphG---SYE-GEILFDGevCRFKDIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 75 ESQAadvrsREIGFIFQSFNLIAYKDAVENIALplfyqGVGRALR--------KEKALKLLRAVGLEEWGHHLPSELSGG 146
Cdd:NF040905 74 DSEA-----LGIVIIHQELALIPYLSIAENIFL-----GNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGAL---DSQTTLevmELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDG 217
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALneeDSAALL---DLLLELKAQGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-215 |
1.00e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.94 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRN-LTESQAADV-RSREIGFIFQSFnliayk 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYVpQSEEVDWSFPVL------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 daVENIALPLFYQGVG---RALRKEKAL--KLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD 174
Cdd:PRK15056 97 --VEDVVMMGRYGHMGwlrRAKKRDRQIvtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154823909 175 SQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIR 215
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-200 |
1.45e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.02 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 2 ALIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADV 81
Cdd:COG4674 9 PILYVEDLTVSFDG---FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsreIGFIFQsfnliayKDAV-------ENIALPL-FYQGVGRALR-------KEKALKLLRAVGLEEWGHHLPSELSGG 146
Cdd:COG4674 86 G---IGRKFQ-------KPTVfeeltvfENLELALkGDRGVFASLFarltaeeRDRIEEVLETIGLTDKADRLAGLLSHG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 147 QKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEgRTLIVVTH 200
Cdd:COG4674 156 QKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEH 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-200 |
1.99e-21 |
|
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: 87.58 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLD-TFDKGEYLLNGRSLRNLTesqaADVRSRE-IGFIFQSfnlia 97
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLP----PEERARLgIFLAFQY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 ykdavenialPLFYQGVgralrkeKALKLLRAVGLeewghhlpsELSGGQKQRIAIARALITEPKVILADEPTGALDSQT 177
Cdd:cd03217 86 ----------PPEIPGV-------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|...
gi 1154823909 178 TLEVMELLKQVNKEGRTLIVVTH 200
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITH 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
2.25e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.53 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLL---DTFDkGEYLLNGRSLR--NLTE 75
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALD---NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphGTYE-GEIIFEGEELQasNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 SQAADvrsreIGFIFQSFNLIAYKDAVENIALplfyqgvGRALRK----------EKALKLLRAVGLEEWGHHLPSELSG 145
Cdd:PRK13549 79 TERAG-----IAIIHQELALVKELSVLENIFL-------GNEITPggimdydamyLRAQKLLAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGRHIG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-169 |
3.33e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLtesqAA 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVGLVKP-DSGRIFLDGEDITHL----PM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRSRE-IGF------IFQsfnliayKDAVE-NIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRI 151
Cdd:COG1137 73 HKRARLgIGYlpqeasIFR-------KLTVEdNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170
....*....|....*...
gi 1154823909 152 AIARALITEPKVILADEP 169
Cdd:COG1137 146 EIARALATNPKFILLDEP 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-220 |
3.34e-21 |
|
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: 87.77 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTY------------------PGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLL 65
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 66 NG-----RSLRNLtesqaadvrsREIGFIF-QSFNLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHL 139
Cdd:cd03267 81 AGlvpwkRRKKFL----------RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 140 PSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHET-SVAEMCDRTIHIRDG 217
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMkDIEALARRVLVIDKG 230
|
...
gi 1154823909 218 IIV 220
Cdd:cd03267 231 RLL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-220 |
3.90e-21 |
|
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: 87.55 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRslrNLTESQAADVR 82
Cdd:cd03244 3 IEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVEL-SSGSILIDGV---DISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SReIGFIFQSfnliaykdavenialPLFYQGvgrALRK----------EKALKLLRAVGLEEWGHHLP-----------S 141
Cdd:cd03244 78 SR-ISIIPQD---------------PVLFSG---TIRSnldpfgeysdEELWQALERVGLKEFVESLPggldtvveeggE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 142 ELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHE-TSVAEmCDRTIHIRDGIIV 220
Cdd:cd03244 139 NLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRlDTIID-SDRILVLDKGRVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-220 |
4.32e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVr 82
Cdd:PRK15439 11 LLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 srEIGFIFQSFNLIAYKDAVENIALPLfyqgVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PRK15439 87 --GIYLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 163 VILADEPTGALdsqTTLEVMELLKQVNK---EGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK15439 161 ILILDEPTASL---TPAETERLFSRIREllaQGVGIVFISHKLPeIRQLADRISVMRDGTIA 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-202 |
5.53e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.40 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 24 GINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAADVRSreIGfifqsfNLIAYKD-- 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILaGLARP-DAGEVLWQGEPIRRQRDEYHQDLLY--LG------HQPGIKTel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 -AVENIAlplFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTL 179
Cdd:PRK13538 90 tALENLR---FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|...
gi 1154823909 180 EVMELLKQVNKEGRTLIVVTHET 202
Cdd:PRK13538 167 RLEALLAQHAEQGGMVILTTHQD 189
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-210 |
5.73e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltESQAADVRS 83
Cdd:PRK13536 42 IDLAGVSKSY-GDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAYKDAVENiaLPLFYQGVGRALRKEKAL--KLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEP 161
Cdd:PRK13536 115 R-IGVVPQFDNLDLEFTVREN--LLVFGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 162 KVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDR 210
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErLCDR 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-214 |
7.07e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.69 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQaadvRSREIGFIFQSFNLiaYKD 100
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI----YRQQVSYCAQTPTL--FGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AV-ENIALPlfYQGVGRALRKEKALKLLRAVGLEEwgHHLP---SELSGGQKQRIAIARALITEPKVILADEPTGALDSQ 176
Cdd:PRK10247 96 TVyDNLIFP--WQIRNQQPDPAIFLDDLERFALPD--TILTkniAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 177 TTLEVMELLKQVNKE-GRTLIVVTHETSVAEMCDRTIHI 214
Cdd:PRK10247 172 NKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-220 |
7.71e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYP------GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltES 76
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL----HF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 77 QAADVRSREIGFIFQ--SFNLIAYKDAVENIALPLFYQGVGRALRKEKALKL-LRAVGL-EEWGHHLPSELSGGQKQRIA 152
Cdd:PRK15112 80 GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIEtLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 153 IARALITEPKVILADEPTGALDSQTTLEVMELLKQVN-KEGRTLIVVTHETSVAEmcdrtiHIRDGIIV 220
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMK------HISDQVLV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-221 |
1.13e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAadVRSReIGFI---FQSFNLI 96
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA--IRAG-IAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AYKDAVENIALPLFyQGVGRAL----RKEKAL--KLLRAVGLEEWGHHLP-SELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:COG1129 343 LDLSIRENITLASL-DRLSRGGlldrRRERALaeEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 170 T-----GAldsqtTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIVG 221
Cdd:COG1129 422 TrgidvGA-----KAEIYRLIRELAAEGKAVIVISSELPeLLGLSDRILVMREGRIVG 474
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-219 |
1.90e-20 |
|
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: 85.53 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGR--SLRNLtesqaad 80
Cdd:TIGR03740 1 LETKNLSKRF-GKQ--TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMItGILRP-TSGEIIFDGHpwTRKDL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vrsREIGFIFQSFNLIAYKDAVENIALPLFYQGvgraLRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:TIGR03740 70 ---HKIGSLIESPPLYENLTARENLKVHTTLLG----LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 161 PKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGII 219
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSeVQQLADHIGIISEGVL 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
2.79e-20 |
|
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: 88.34 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLL---DTFDkGEYLLNGRSLrnltesQAA 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALD---GIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphGTWD-GEIYWSGSPL------KAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRSRE---IGFIFQSFNLIAYKDAVENIAL--PLFYQG--VGRALRKEKALKLLRAVGLEEWGHHLP-SELSGGQKQRI 151
Cdd:TIGR02633 71 NIRDTEragIVIIHQELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQHVA 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-214 |
3.45e-20 |
|
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: 83.36 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnltesqaadvrs 83
Cdd:cd03223 1 IELENLSLATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 rEIGFIFQsfnliaykdaveniaLPLFYQGVgralrkekalklLRAVGLEEWGHhlpsELSGGQKQRIAIARALITEPKV 163
Cdd:cd03223 65 -DLLFLPQ---------------RPYLPLGT------------LREQLIYPWDD----VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQvnkEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE---LGITVISVGHRPSLWKFHDRVLDL 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
5.51e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MA-LIELSGIEKTYP-------------------GAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDK 60
Cdd:COG1134 1 MSsMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 61 GEYLLNGR--SLrnLtesqaadvrsrEIGFIFQSfNLIAYkdavENIALplfyqgVGRAL--RKEKALKLLRAV----GL 132
Cdd:COG1134 81 GRVEVNGRvsAL--L-----------ELGAGFHP-ELTGR----ENIYL------NGRLLglSRKEIDEKFDEIvefaEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 133 EEWGhHLP-SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDR 210
Cdd:COG1134 137 GDFI-DQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMgAVRRLCDR 215
|
250
....*....|
gi 1154823909 211 TIHIRDGIIV 220
Cdd:COG1134 216 AIWLEKGRLV 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-203 |
5.78e-20 |
|
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: 83.45 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 17 QPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFD--KGEYLLNGRSLR-NLTesqaadvrsREIGFIFQsf 93
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDkNFQ---------RSTGYVEQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 nliaykdavENIALPLfyQGVGRALRKEkalKLLRAVGLEewghhlpselsggQKQRIAIARALITEPKVILADEPTGAL 173
Cdd:cd03232 87 ---------QDVHSPN--LTVREALRFS---ALLRGLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190
....*....|....*....|....*....|
gi 1154823909 174 DSQTTLEVMELLKQVNKEGRTLIVVTHETS 203
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCTIHQPS 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
7.63e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYpGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEYLLNGRSLRNLTESQAa 79
Cdd:PRK09536 1 MPMIDVSDLSVEF-GDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTLTP-TAGTVLVAGDDVEALSARAA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 dvrSREIGFIFQ----SFNLiAYKDAVENIALPLF--YQGVGRALRK--EKALKllrAVGLEEWGHHLPSELSGGQKQRI 151
Cdd:PRK09536 76 ---SRRVASVPQdtslSFEF-DVRQVVEMGRTPHRsrFDTWTETDRAavERAME---RTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 152 AIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSV-AEMCDRTIHIRDGII 219
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRV 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-220 |
7.88e-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: 84.12 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 8 GIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrnltesqaadVRSR-EI 86
Cdd:cd03220 24 GILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------------VSSLlGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 87 GFIFQSfNLIAYkdavENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHhLP-SELSGGQKQRIAIARALITEPKVIL 165
Cdd:cd03220 92 GGGFNP-ELTGR----ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFID-LPvKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 166 ADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH-ETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHdPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-220 |
9.33e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 9.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 32 GEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnltESQAADVRSREIGFIFQSF---------NLIAYKDAV 102
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL----ESWSSKAFARKVAYLPQQLpaaegmtvrELVAIGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 103 ENIALPLFyqGVGRALRKEKALKLlraVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVM 182
Cdd:PRK10575 113 WHGALGRF--GAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 183 ELLKQVNKE-GRTLIVVTHETSV-AEMCDRTIHIRDGIIV 220
Cdd:PRK10575 188 ALVHRLSQErGLTVIAVLHDINMaARYCDYLVALRGGEMI 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
1.59e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQPLHvlkGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAAD 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALH---EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK---DITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 VRSREIGFIFQSFNLIAYKDAVENIALPLFYqgvgrALRKEKALKLLRAVGL----EEWGHHLPSELSGGQKQRIAIARA 156
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAMGGFF-----AERDQFQERIKWVYELfprlHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVA-EMCDRTIHIRDGIIV 220
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQAlKLADRGYVLENGHVV 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
2.55e-19 |
|
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: 80.57 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnltesqaadvrs 83
Cdd:cd03221 1 IELENLSKTY-GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 rEIGFIFQsfnliaykdavenialplfyqgvgralrkekalkllravgleewghhlpseLSGGQKQRIAIARALITEPKV 163
Cdd:cd03221 64 -KIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 164 ILADEPTGALD--SQTTLEvmELLKqvNKEGrTLIVVTHETS-VAEMCDRTIHIRDG 217
Cdd:cd03221 92 LLLDEPTNHLDleSIEALE--EALK--EYPG-TVILVSHDRYfLDQVATKIIELEDG 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-200 |
4.29e-19 |
|
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: 81.39 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlteSQAADVRSREIGFIFQSFNLIAYKD 100
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIAlplFYQGVGRALRKEKALKllrAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:cd03231 90 VLENLR---FWHADHSDEQVEEALA---RVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 1154823909 181 VMELLKQVNKEGRTLIVVTH 200
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-220 |
5.75e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 13 YPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTEsqaADVRsREIGFIFQS 92
Cdd:PRK13657 344 YDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR---ASLR-RNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 FNLIAyKDAVENIAlplfyqgVGR--ALRKEKALKLLRAVGLE--------------EWGhhlpSELSGGQKQRIAIARA 156
Cdd:PRK13657 418 AGLFN-RSIEDNIR-------VGRpdATDEEMRAAAERAQAHDfierkpdgydtvvgERG----RQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-200 |
1.55e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLD-TFDKGEYLLNGRSLRNLTesqaADVRSRE-IGFIFQS----- 92
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKyEVTSGSILLDGEDILELS----PDERARAgIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 ----FNLIayKDAVENIALPLFYqgvGRALRKEkALKLLRAVGLEEwgHHLPSEL----SGGQKQRIAIARALITEPKVI 164
Cdd:COG0396 91 gvsvSNFL--RTALNARRGEELS---AREFLKL-LKEKMKELGLDE--DFLDRYVnegfSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
12-220 |
3.04e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.45 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 12 TYPGAQPlHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLtesQAADVRSR-----EI 86
Cdd:PRK10789 322 TYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvsQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 87 GFIFQsfnliaykDAV-ENIAL------PLFYQGVGR-ALRKEKALKLLRAVGLE--EWGhhlpSELSGGQKQRIAIARA 156
Cdd:PRK10789 398 PFLFS--------DTVaNNIALgrpdatQQEIEHVARlASVHDDILRLPQGYDTEvgERG----VMLSGGQKQRISIARA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVnKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-200 |
4.19e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDkGEYLLNGRSL---RNLTESQAADVR-SREIGFIFQSFNLI 96
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEffnQNIYERRVNLNRlRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 ---AYKDAVENIALPLFYQGVGRALRKEKALKllravGLEEWG------HHLPSELSGGQKQRIAIARALITEPKVILAD 167
Cdd:PRK14258 101 pmsVYDNVAYGVKIVGWRPKLEIDDIVESALK-----DADLWDeikhkiHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....
gi 1154823909 168 EPTGALDSQTTLEVMELLKQVN-KEGRTLIVVTH 200
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlRSELTMVIVSH 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-206 |
4.82e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILglldtfdKGEYllngrslRNLTESQAADVRSREIGfifQSFNLIayk 99
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-------AGAL-------KGTPVAGCVDVPDNQFG---REASLI--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 davenialplfyQGVGRALRKEKALKLLRAVGLEEWGHHL--PSELSGGQKQRIAIARALITEPKVILADEPTGALDSQT 177
Cdd:COG2401 104 ------------DAIGRKGDFKDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190
....*....|....*....|....*....|
gi 1154823909 178 TLEV-MELLKQVNKEGRTLIVVTHETSVAE 206
Cdd:COG2401 172 AKRVaRNLQKLARRAGITLVVATHHYDVID 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-200 |
8.98e-18 |
|
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: 77.78 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLrnlteSQAADVRSREIGFIFQSFNLIAYKD 100
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIAlplFYQGVGRALRKEkALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:TIGR01189 90 ALENLH---FWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 1154823909 181 VMELLKQVNKEGRTLIVVTH 200
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-210 |
1.09e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD-- 80
Cdd:PRK11300 5 LLSVSGLMMRFGG---LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 -VRSreigfiFQSFNLIAYKDAVEN-----------------IALPLFYQGVGRALrkEKALKLLRAVGLEEWGHHLPSE 142
Cdd:PRK11300 82 vVRT------FQHVRLFREMTVIENllvaqhqqlktglfsglLKTPAFRRAESEAL--DRAATWLERVGLLEHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDR 210
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKlVMGISDR 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-200 |
1.51e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfdKGEYLLNGRSLRNLTESQAADVRS-----REIGFIFQSFNL 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLLPG--QGEILLNGRPLSDWSAAELARHRAylsqqQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 IAykdavenialpLFYQGVGRALRKEKAL-KLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT-------EPKVILAD 167
Cdd:COG4138 90 LA-----------LHQPAGASSEAVEQLLaQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1154823909 168 EPTGALD--SQTTLEvmELLKQVNKEGRTLIVVTH 200
Cdd:COG4138 159 EPMNSLDvaQQAALD--RLLRELCQQGITVVMSSH 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
2.52e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDtfDK-------GEYLLNGRSLRNLTEsqAADVRsREIGFIFQSF 93
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN--DKvsgyrysGDVLLGGRSIFNYRD--VLEFR-RRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKDAVENIALPLFYQGVGRALRKEKALKLLRAVGL----EEWGHHLPSELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 170 TGALDSQTTLEVMELLKQVnKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAqAARISDRAALFFDGRLV 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-217 |
4.81e-17 |
|
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: 76.60 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 19 LHVLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTFDKGEYLLNgrSLRNLTESQAADVRSR-EIGFIFQSFNLI 96
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSN--KNESEPSFEATRSRNRySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AyKDAVENIALplfyqgvGRALRKEKALKLLRAVGLEEWGHHLPS-----------ELSGGQKQRIAIARALITEPKVIL 165
Cdd:cd03290 92 N-ATVEENITF-------GSPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1154823909 166 ADEPTGALDSQTTLEVME--LLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-221 |
1.04e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 12 TYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqAADVRSREIGFI-- 89
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRERRRLGVAYIpe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 90 -FQSFNLIAYKDAVENIALPLFYQ---GVGRALRKEKALKLLRAVgLEEW-----GHHLP-SELSGGQKQRIAIARALIT 159
Cdd:COG3845 341 dRLGRGLVPDMSVAENLILGRYRRppfSRGGFLDRKAIRAFAEEL-IEEFdvrtpGPDTPaRSLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDGIIVG 221
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDeILALSDRIAVMYEGRIVG 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-203 |
1.54e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.84 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDT--FDKGEYLLNGRSL-----RNLTESQAADVRSREIGfIFQS 92
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTgvITGGDRLVNGRPLdssfqRSIGYVQQQDLHLPTST-VRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 FNLIAYkdavenIALPlfyQGVGRALRKEKALKLLRAVGLEEWGHHL---PSE-LSGGQKQRIAIARALITEPKVIL-AD 167
Cdd:TIGR00956 857 LRFSAY------LRQP---KSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154823909 168 EPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS 203
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPS 963
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-220 |
1.70e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGaqpLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLnGRSLRnltesqaadv 81
Cdd:COG0488 315 VLELEGLSKSYGD---KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGEL-EPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 rsreIGFIFQSF-NLIAYKDAVENIalplfyQGVGRALRKEKALKLLRAVGLEEWGHHLP-SELSGGQKQRIAIARALIT 159
Cdd:COG0488 380 ----IGYFDQHQeELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 160 EPKVILADEPTGALDSQtTLEVME-LLKqvNKEGrTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG0488 450 PPNVLLLDEPTNHLDIE-TLEALEeALD--DFPG-TVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-220 |
3.47e-16 |
|
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: 73.84 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 8 GIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFDK--GEYLLNGrslrnLTESQAADVRSR 84
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNG-----IPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 85 EIGFIFQSFNLIAYKDavenialplfyqgVGRALrkEKALKLLravgleewGHHLPSELSGGQKQRIAIARALITEPKVI 164
Cdd:cd03233 84 EIIYVSEEDVHFPTLT-------------VRETL--DFALRCK--------GNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS--VAEMCDRTIHIRDGIIV 220
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-220 |
7.15e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAd 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 81 vrSREIGFIFQSFNLIAYKDAVENI-ALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALIT 159
Cdd:PRK10895 77 --RRGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDGIIV 220
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLI 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-217 |
7.80e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILG--LLDTFDKGEYLLNGRSLRNLTesqaadvrSREIGFIFQSFNLIAY 98
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTKQI--------LKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIALPLFYQgVGRALRKEKALKLLRAV----GLEEW-----GHHLPSELSGGQKQRIAIARALITEPKVILADEP 169
Cdd:PLN03211 155 LTVRETLVFCSLLR-LPKSLTKQEKILVAESViselGLTKCentiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 170 TGALDSQTTLEVMELLKQVNKEGRTLIVVTHETS--VAEMCDRTIHIRDG 217
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSsrVYQMFDSVLVLSEG 283
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
20-200 |
8.86e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.45 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFD--KGEYLLNGRSLRNLTesqaADVRSREiGfIFQSFNlia 97
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELE----PDERARA-G-LFLAFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 YKDAVENIALPLFYQGVGRALRKEKALKllrAVGLEEWGHHLPSEL------------------SGGQKQRIAIARALIT 159
Cdd:TIGR01978 85 YPEEIPGVSNLEFLRSALNARRSARGEE---PLDLLDFEKLLKEKLalldmdeeflnrsvnegfSGGEKKRNEILQMALL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-220 |
2.24e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLdTFDKGEYLLNG-----RSLRNLtesqaadvrsREIGFIF--- 90
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVRVLGyvpfkRRKEFA----------RRIGVVFgqr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 91 ----------QSFNLIA--YkdavenialplfyqGVGRALRKEKaLKLLRAV-GLEEWGHHLPSELSGGQKQRIAIARAL 157
Cdd:COG4586 105 sqlwwdlpaiDSFRLLKaiY--------------RIPDAEYKKR-LDELVELlDLGELLDTPVRQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 158 ITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDdIEALCDRVIVIDHGRII 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-217 |
6.76e-15 |
|
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: 73.12 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltesqAADVRSREIGFIFQSFNLIAYKDAVEN 104
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-----NLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 105 IalpLFY-QGVGRAlrKEKALKLLRAVgLEEWG-HHLPSE----LSGGQKQRIAIARALITEPKVILADEPTGALDSQTT 178
Cdd:TIGR01257 1024 I---LFYaQLKGRS--WEEAQLEMEAM-LEDTGlHHKRNEeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 179 LEVMELLKQVnKEGRTLIVVTHETSVAEMC-DRTIHIRDG 217
Cdd:TIGR01257 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLgDRIAIISQG 1136
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-210 |
1.05e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.76 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 18 PLHVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLD-----TFDKgeYLLNGRSLRNLTESQAADVRSREIGFIFQ 91
Cdd:PRK15093 19 WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwrvTADR--MRFDDIDLLRLSPRERRKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 92 SFNliAYKDAVENIALPL------------FYQGVGraLRKEKALKLLRAVGLEEWG---HHLPSELSGGQKQRIAIARA 156
Cdd:PRK15093 97 EPQ--SCLDPSERVGRQLmqnipgwtykgrWWQRFG--WRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 157 LITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLI-VVTHETS-VAEMCDR 210
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDLQmLSQWADK 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-219 |
1.27e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 23 KGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGR---------SLRN----LTESQaadvrsREIGFi 89
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldAVKKgmayITESR------RDNGF- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 90 FQSFNLiaykdaVENIALPLFYQGVG--------------RALRKEKALKLLRAVGLEEwghhLPSELSGGQKQRIAIAR 155
Cdd:PRK09700 353 FPNFSI------AQNMAISRSLKDGGykgamglfhevdeqRTAENQRELLALKCHSVNQ----NITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 156 ALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGII 219
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-220 |
3.34e-14 |
|
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: 68.59 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPlHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADVRS 83
Cdd:cd03369 7 IEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI---DISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSfnliaykdavenialPLFYQGVGRA----LRKEKALKLLRAVGLEEWGhhlpSELSGGQKQRIAIARALIT 159
Cdd:cd03369 83 S-LTIIPQD---------------PTLFSGTIRSnldpFDEYSDEEIYGALRVSEGG----LNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 160 EPKVILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-219 |
6.86e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREIGFIFQSFNLIAYKD 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIALplfyqgvgralrkEKALKLLRAVGLEEWGHHlPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:PLN03232 713 AIDVTAL-------------QHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 181 VMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
39-212 |
8.20e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 39 GASGSgKSTLLNILG--LLDTFDKGEYllNGRSLRNLTEsqaadVRSREIGFifqsFNLIAYkdavENIALplfyqGVGR 116
Cdd:PTZ00265 1264 GGSGE-DSTVFKNSGkiLLDGVDICDY--NLKDLRNLFS-----IVSQEPML----FNMSIY----ENIKF-----GKED 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 117 ALRkEKALKLLRAVGLEEWGHHLPSE-----------LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELL 185
Cdd:PTZ00265 1323 ATR-EDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
170 180
....*....|....*....|....*...
gi 1154823909 186 KQV-NKEGRTLIVVTHETSVAEMCDRTI 212
Cdd:PTZ00265 1402 VDIkDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
1.29e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFdKGEYLLNGRslrnltESQAADVRSReigfifqsfnlIAY- 98
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIaGLLPPA-AGTIKLDGG------DIDDPDVAEA-----------CHYl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 --KDAV-------ENIAlplFYQGV--GRALRKEKALKllrAVGLeewGH--HLP-SELSGGQKQRIAIARALITEPKVI 164
Cdd:PRK13539 79 ghRNAMkpaltvaENLE---FWAAFlgGEELDIAAALE---AVGL---APlaHLPfGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-214 |
1.34e-13 |
|
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: 66.19 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNilglldtfdkgeyllngrslrnltESQAADVRSREIGFifqsfnliayk 99
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------------EGLYASGKARLISF----------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 daveniaLPLFYQGVGRALRKekaLKLLRAVGLEewghHLP-----SELSGGQKQRIAIARALITEPK--VILADEPTGA 172
Cdd:cd03238 54 -------LPKFSRNKLIFIDQ---LQFLIDVGLG----YLTlgqklSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1154823909 173 LDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-203 |
1.37e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGR--------------- 68
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 69 --------------------SLRNLTESQAADVRSREIGFIFQS---------------FNLIAYK-DAVENIALPLFYQ 112
Cdd:PTZ00265 463 gvvsqdpllfsnsiknnikySLYSLKDLEALSNYYNEDGNDSQEnknkrnscrakcagdLNDMSNTtDSNELIEMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 113 gvgrALRKEKALKLLRAVGLEEWGHHLP-----------SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:PTZ00265 543 ----TIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|...
gi 1154823909 182 MELLKQVN-KEGRTLIVVTHETS 203
Cdd:PTZ00265 619 QKTINNLKgNENRITIIIAHRLS 641
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-221 |
1.73e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGiektyPGaqplhvLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLLNGRSLRNLTESQAA 79
Cdd:PRK10762 258 LKVDNLSG-----PG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DvrsreigfifqsfNLIAY------KDAV-------ENI---ALPLFYQGVGRALRKEKALkllrAVG--LEEWGHHLPS 141
Cdd:PRK10762 326 A-------------NGIVYisedrkRDGLvlgmsvkENMsltALRYFSRAGGSLKHADEQQ----AVSdfIRLFNIKTPS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 142 ------ELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHI 214
Cdd:PRK10762 389 meqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVM 468
|
....*..
gi 1154823909 215 RDGIIVG 221
Cdd:PRK10762 469 HEGRISG 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-219 |
2.06e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDKGEYLLNGRslrnltesqAADVRsrEIGFIFQS------ 92
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---------VAYVP--QVSWIFNAtvrdni 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 -----FNLIAYKDAVENIALplfyqgvgralrkEKALKLLRAVGLEEWGHHlPSELSGGQKQRIAIARALITEPKVILAD 167
Cdd:PLN03130 700 lfgspFDPERYERAIDVTAL-------------QHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 168 EPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-200 |
4.09e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFD--KGEYLLNGRSLRNLTesqaADVRSReIGfIFQSFNLIAY 98
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE----PEERAH-LG-IFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIA-LPLFYQGVGRALRKEKALKL---------LRAVGLEE--WGHHLPSELSGGQKQRIAIARALITEPKVILA 166
Cdd:CHL00131 96 IPGVSNADfLRLAYNSKRKFQGLPELDPLefleiinekLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190
....*....|....*....|....*....|....
gi 1154823909 167 DEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-210 |
4.17e-13 |
|
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: 67.73 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQPLHVLKgINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRS-LRNLTEsqaadv 81
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISD------ 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 rsreigfIFQSFNLIAYKDAVENIALP---LFYQGVGRALRKEKALKL----LRAVGLEEWGHHLPSELSGGQKQRIAIA 154
Cdd:TIGR01257 2010 -------VHQNMGYCPQFDAIDDLLTGrehLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 155 RALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAE-MCDR 210
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTR 2139
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-219 |
5.50e-13 |
|
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: 67.66 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNilGLLDTFDK--GEYLLNGrslrnltesqaadvrsrEIGFIFQSfNLIAYK 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMDKveGHVHMKG-----------------SVAYVPQQ-AWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIalpLFyqgvGRALRKEKALKLLRAVGLEEWGHHLPS-----------ELSGGQKQRIAIARALITEPKVILADE 168
Cdd:TIGR00957 714 SLRENI---LF----GKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 169 PTGALDSQTTLEVMEllKQVNKEG----RTLIVVTHETSVAEMCDRTIHIRDGII 219
Cdd:TIGR00957 787 PLSAVDAHVGKHIFE--HVIGPEGvlknKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-200 |
4.27e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfdKGEYLLNGRSLRNLTESQAADVRsreiGFIFQSFNLIaykdave 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLArMAGLLPG--SGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPP------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 104 nIALPLF-----YQGVGRALRK-EKAL-KLLRAVGLEEWGHHLPSELSGGQKQRIAIA-------RALITEPKVILADEP 169
Cdd:PRK03695 82 -FAMPVFqyltlHQPDKTRTEAvASALnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 1154823909 170 TGALD--SQTTLEvmELLKQVNKEGRTLIVVTH 200
Cdd:PRK03695 161 MNSLDvaQQAALD--RLLSELCQQGIAVVMSSH 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-201 |
4.62e-12 |
|
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: 64.57 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYPGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEyllngrslrnltesqAADVRSRE 85
Cdd:TIGR03719 7 MNRVSKVVPPKK--EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---------------ARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 86 IGFIFQSFNLIAYKDAVENIAlplfyQGVGRALRKEKAL---------------KLLRAVG-----LEEWGHH------- 138
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVE-----EGVAEIKDALDRFneisakyaepdadfdKLAAEQAelqeiIDAADAWdldsqle 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 139 -------LP------SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnkEGrTLIVVTHE 201
Cdd:TIGR03719 145 iamdalrCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHD 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-220 |
6.90e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 17 QPLHVLKGINAQIQEGEMVAIMGASGSGKSTLLNilGLLDTFD--KGEyLLNGRSLRNLTEsQA----ADVRSrEIGFiF 90
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLLSQFEisEGR-VWAERSIAYVPQ-QAwimnATVRG-NILF-F 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 91 QSFNLIAYKDAVenialplfyqgvgRALRKEKALKLLRAvGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPT 170
Cdd:PTZ00243 745 DEEDAARLADAV-------------RVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1154823909 171 GALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PTZ00243 811 SALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-217 |
7.57e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDkGEYLLNGRslrnltesqaadvrsreIGFIFQsFNLIAYK 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSE-GKIKHSGR-----------------ISFSPQ-TSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLFYQgvgralrKEKALKLLRAVGLEEWGHHLPSE-----------LSGGQKQRIAIARALITEPKVILADE 168
Cdd:TIGR01271 502 TIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 169 PTGALDSQTTLEVME--LLK-QVNKegrTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEscLCKlMSNK---TRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-217 |
8.46e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYPGAQplhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADvrsRE 85
Cdd:PRK10982 1 MSNISKSFPGVK---ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 86 IGFIFQSFNLIAYKDAVENIAL---PL--FYQGVGRALRKEKALklLRAVGLEEWGHHLPSELSGGQKQRIAIARALITE 160
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDNMWLgryPTkgMFVDQDKMYRDTKAI--FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 161 PKVILADEPTGALdsqTTLEVMELLKQVNK---EGRTLIVVTHET-SVAEMCDRTIHIRDG 217
Cdd:PRK10982 153 AKIVIMDEPTSSL---TEKEVNHLFTIIRKlkeRGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-200 |
1.19e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQpLHVLKGinaQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGE------------YLlngrsl 70
Cdd:COG1245 341 LVEYPDLTKSYGGFS-LEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedlkisykpqYI------ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 71 rnlteSQAADVRSREigFIFQsfnliAYKDAVENialPLFYQGVGRALRKEKALKllRAVgleewghhlpSELSGGQKQR 150
Cdd:COG1245 411 -----SPDYDGTVEE--FLRS-----ANTDDFGS---SYYKTEIIKPLGLEKLLD--KNV----------KDLSGGELQR 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 151 IAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTH 200
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-214 |
1.21e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 30 QEGEMVAIMGASGSGKSTLLNIL-GLL--------DTFDKGEYLlngRSLRNlTESQA--ADVRSREIGfifqsfnlIAY 98
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsGELkpnlgdydEEPSWDEVL---KRFRG-TELQDyfKKLANGEIK--------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 K-DAVENIalPLFYQGVGRALRKE-----KALKLLRAVGLEE-WGHHLpSELSGGQKQRIAIARALITEPKVILADEPTG 171
Cdd:COG1245 165 KpQYVDLI--PKVFKGTVRELLEKvdergKLDELAEKLGLENiLDRDI-SELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 172 ALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHI 284
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-204 |
1.53e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 19 LHVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDT--FDKGEYLLNGRSLRNLTESQAA------DVRSREI---- 86
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETFARISgyceqnDIHSPQVtvre 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 87 GFIFQSFnliaykdavenIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLP--SELSGGQKQRIAIARALITEPKVI 164
Cdd:PLN03140 973 SLIYSAF-----------LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 165 LADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSV 204
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-217 |
1.70e-11 |
|
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: 62.18 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGlldtfdkgeyllngrslrNLTESQAADVRSREIGFIFQsFNLIAYK 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLmLILG------------------ELEPSEGKIKHSGRISFSSQ-FSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLFYQgvgralrKEKALKLLRAVGLEEWGHHLPSE-----------LSGGQKQRIAIARALITEPKVILADE 168
Cdd:cd03291 113 TIKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154823909 169 PTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-217 |
2.03e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 14 PGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGrslRNLTESQAADVRsREIGFIFQS- 92
Cdd:PLN03232 1246 PGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD---CDVAKFGLTDLR-RVLSIIPQSp 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 --------FNLIAYKDavENIAlplfyqGVGRALRKEKALKLLR--AVGLEEWGHHLPSELSGGQKQRIAIARALITEPK 162
Cdd:PLN03232 1320 vlfsgtvrFNIDPFSE--HNDA------DLWEALERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKEGrTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSC-TMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-220 |
4.18e-11 |
|
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: 61.74 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLH--VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnLTESQAADV 81
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RSReIGFIFQSFNliaykdavenialpLF---YQGVGRALRkEKALKLLRAVGLE-----EWGHHLPSELSGGQKQRIAI 153
Cdd:COG4615 405 RQL-FSAVFSDFH--------------LFdrlLGLDGEADP-ARARELLERLELDhkvsvEDGRFSTTDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 154 ARALITEPKVILADE------P-------TgaldsqttlevmELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:COG4615 469 LVALLEDRPILVFDEwaadqdPefrrvfyT------------ELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-217 |
7.42e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPgAQPLHVlKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnLTESQAADVRS 83
Cdd:PRK10522 323 LELRNVTFAYQ-DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 ReIGFIFQSFNLIAY-----KDAVENIAlplfyqgVGRALRKekaLKLLRAVGLEEwGHHLPSELSGGQKQRIAIARALI 158
Cdd:PRK10522 398 L-FSAVFTDFHLFDQllgpeGKPANPAL-------VEKWLER---LKMAHKLELED-GRISNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 159 TEPKVILADEPTGALDSQTTLEV-MELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-220 |
8.34e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-----------GLLDTfdkGEYLLNGRSLRNLTESQAADVRS-----R 84
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaprGARVT---GDVTLNGEPLAAIDAPRLARLRAvlpqaA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 85 EIGFIFQSFNLIA---YKDAVENIALPLFYQGVG-RALRKEKALKLL-RAVgleewghhlpSELSGGQKQRIAIARAL-- 157
Cdd:PRK13547 93 QPAFAFSAREIVLlgrYPHARRAGALTHRDGEIAwQALALAGATALVgRDV----------TTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 158 -------ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGR--TLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-214 |
8.34e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 30 QEGEMVAIMGASGSGKSTLLNIL--------GLLDTFDKGEYLLN---GRSLRNLTEsqaaDVRSREIGFIF--QSFNLI 96
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFT----KLLEGDVKVIVkpQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 --AYKDAVENIalplfyqgVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD 174
Cdd:cd03236 100 pkAVKGKVGEL--------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 175 SQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHC 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-200 |
9.51e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTF--DKGEYLLNGRSLRNLTESQAADVRsreigfIFQSFNliaY 98
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDRAGEG------IFMAFQ---Y 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 99 KDAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGH------HLPSEL---------SGGQKQRIAIARALITEPKV 163
Cdd:PRK09580 87 PVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTH 200
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-217 |
1.23e-10 |
|
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: 59.48 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfdKGEYLLNGRSLRNLTESQ---AADVRSREIgFIFQS---F 93
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLNT--EGDIQIDGVSWNSVPLQKwrkAFGVIPQKV-FIFSGtfrK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKdavenialplfyqgvgrALRKEKALKLLRAVGLEEWGHHLPSEL-----------SGGQKQRIAIARALITEPK 162
Cdd:cd03289 96 NLDPYG-----------------KWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQVNKeGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-200 |
1.27e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.71 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNltesqaADvRSREIGFIFQSFNLIAYKD 100
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR------GD-RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 AVENIAlplFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:PRK13543 99 TLENLH---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 1154823909 181 VMELLKQVNKEGRTLIVVTH 200
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-201 |
1.52e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfDKGEyLLNGRSLRnltesqaadvrsreIGFIFQSFNLiayk 99
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRvVLGLVAP-DEGV-IKRNGKLR--------------IGYVPQKLYL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 daveNIALPLfyqGVGRALRKEKALK---LLRAVGLEEWGHHLPS---ELSGGQKQRIAIARALITEPKVILADEPTGAL 173
Cdd:PRK09544 79 ----DTTLPL---TVNRFLRLRPGTKkedILPALKRVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*....
gi 1154823909 174 DSQTTLEVMELLKQVNKE-GRTLIVVTHE 201
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-220 |
3.35e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 1 MALIELSGIEKTYpGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNgrslRNLTESQ-AA 79
Cdd:PRK11147 1 MSLISIHGAWLSF-SDAPL--LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARlQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 80 DVRSREIGFIF---------QSFNLIAYKDAVENIALPLFYQGVGRALRKEKAL-------------KLLRAVGLEewGH 137
Cdd:PRK11147 74 DPPRNVEGTVYdfvaegieeQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLdhhnlwqlenrinEVLAQLGLD--PD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 138 HLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTtlevMELLKQVNKEGR-TLIVVTHETS-VAEMCDRTIHIR 215
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQgSIIFISHDRSfIRNMATRIVDLD 227
|
....*
gi 1154823909 216 DGIIV 220
Cdd:PRK11147 228 RGKLV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-214 |
3.42e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 29 IQEGEMVAIMGASGSGKSTLLNILGlldtfdkGEYLLN-GRSLRNL-----------TESQA--ADVRSREIGfifqsfn 94
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------GELIPNlGDYEEEPswdevlkrfrgTELQNyfKKLYNGEIK------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 95 lIAYK-DAVEniALPLFYQG-VGRALRK----EKALKLLRAVGLEE-WGHHLpSELSGGQKQRIAIARALITEPKVILAD 167
Cdd:PRK13409 162 -VVHKpQYVD--LIPKVFKGkVRELLKKvderGKLDEVVERLGLENiLDRDI-SELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1154823909 168 EPTGALDSQTTLEVMELLKQVNkEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHI 283
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-201 |
4.18e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 17 QPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSL-RNLTESQaadvrsREIGFIFQSFNL 95
Cdd:PRK13540 14 QPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQ------KQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 IAYKDAVENIALPLFYQgvgralrkEKALKLLRAVGLEEWGHHLPSE---LSGGQKQRIAIARALITEPKVILADEPTGA 172
Cdd:PRK13540 86 NPYLTLRENCLYDIHFS--------PGAVGITELCRLFSLEHLIDYPcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 1154823909 173 LDSQTTLEVMELLKQVNKEGRTLIVVTHE 201
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-210 |
4.52e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 28 QIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFDkGEYLLNGRSL--RNLtesqaaDVRSReIGFIFQSFNLiaYKD-AV- 102
Cdd:NF033858 288 RIRRGEIFGFLGSNGCGKSTTMKMLtGLLPASE-GEAWLFGQPVdaGDI------ATRRR-VGYMSQAFSL--YGElTVr 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 103 ENIAL--PLFyqGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLE 180
Cdd:NF033858 358 QNLELhaRLF--HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190
....*....|....*....|....*....|.
gi 1154823909 181 VMELLKQVNKE-GRTLIVVTHETSVAEMCDR 210
Cdd:NF033858 436 FWRLLIELSREdGVTIFISTHFMNEAERCDR 466
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-217 |
7.18e-10 |
|
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: 57.91 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 29 IQEGEMVAIMGASGSGKSTLLN-ILGLLDTFDKGEYLLNGRSL--RNLTESQAADV------RSREigfifqsfNLIAYK 99
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVdiRNPAQAIRAGIamvpedRKRH--------GIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLF--YQGVGRaLRKEKALKLLRA----VGLEEWGHHLP-SELSGGQKQRIAIARALITEPKVILADEPTGA 172
Cdd:TIGR02633 355 GVGKNITLSVLksFCFKMR-IDAAAELQIIGSaiqrLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1154823909 173 LDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDG 217
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEG 479
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-186 |
8.32e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLL-NILGLLDTFDK---GEYLLNGRSLRNLTESQAADV---RSREIGF----I 89
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIgveGVITYDGITPEEIKKHYRGDVvynAETDVHFphltV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 90 FQSFNLIAYKDAVENialplFYQGVGRALRKEKALKL-LRAVGLE-----EWGHHLPSELSGGQKQRIAIARALITEPKV 163
Cdd:TIGR00956 156 GETLDFAARCKTPQN-----RPDGVSREEYAKHIADVyMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180
....*....|....*....|...
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLK 186
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALK 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-187 |
1.00e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLN-ILGLLDTfdKGEYLLNGRSLRNLTESQ---AADVRSREIgFIFQ-SF-- 93
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLST--EGEIQIDGVSWNSVTLQTwrkAFGVIPQKV-FIFSgTFrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 94 NLIAYKDAVEnialplfyqgvgralrkEKALKLLRAVGLEEWGHHLPSEL-----------SGGQKQRIAIARALITEPK 162
Cdd:TIGR01271 1311 NLDPYEQWSD-----------------EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAK 1373
|
170 180
....*....|....*....|....*
gi 1154823909 163 VILADEPTGALDSQTTLEVMELLKQ 187
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-200 |
1.65e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAQpLHVLKGinaQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTfDKGEYLlngrslrnltesqaADV 81
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLaGVLKP-DEGEVD--------------PEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 RsreigfifqsfnlIAYK-----------------DAVENIALPLFYQGVGRALRKEKALKllRAVgleewghhlpSELS 144
Cdd:PRK13409 401 K-------------ISYKpqyikpdydgtvedllrSITDDLGSSYYKSEIIKPLQLERLLD--KNV----------KDLS 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 145 GGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKE-GRTLIVVTH 200
Cdd:PRK13409 456 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDH 512
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-217 |
1.68e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILglldTFD-----KGEYLLNGRSlRNLTESqAADVRsREIGFIFQSFNL 95
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDhpqgySNDLTLFGRR-RGSGET-IWDIK-KHIGYVSSSLHL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 iAYK--DAVENIALPLF------YQGVGRALRKeKALKLLRAVGLEEWGHHLP-SELSGGQkQRIA-IARALITEPKVIL 165
Cdd:PRK10938 348 -DYRvsTSVRNVILSGFfdsigiYQAVSDRQQK-LAQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPTLLI 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 166 ADEPTGALDSQTTLEVMELLKQVNKEGRT-LIVVTHETSVAEMC--DRTIHIRDG 217
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPACitHRLEFVPDG 479
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-212 |
4.34e-09 |
|
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: 54.93 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-IL---------------GLLDTFDKGEYL---------LNGRSLRN-- 72
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLypalarrlhlkkeqpGNHDRIEGLEHIdkvividqsPIGRTPRSnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 73 LTESQAADvrsrEIGFIF------QSFNL----IAYKDAveNIALPL---------FYQGVGRALRKekaLKLLRAVGLE 133
Cdd:cd03271 89 ATYTGVFD----EIRELFcevckgKRYNRetleVRYKGK--SIADVLdmtveealeFFENIPKIARK---LQTLCDVGLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 134 --EWGHHLPSeLSGGQKQRIAIARALI---TEPKVILADEPTGAL---DSQTTLEVMELLkqVNKeGRTLIVVTHETSVA 205
Cdd:cd03271 160 yiKLGQPATT-LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRL--VDK-GNTVVVIEHNLDVI 235
|
....*..
gi 1154823909 206 EMCDRTI 212
Cdd:cd03271 236 KCADWII 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-210 |
4.88e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTesqAADVRSReIGFIFQS-------- 92
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKV-LGIIPQApvlfsgtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 -FNLIAY---KDAVenialplFYQGVGRALRKEKALKllRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADE 168
Cdd:PLN03130 1330 rFNLDPFnehNDAD-------LWESLERAHLKDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1154823909 169 PTGALDSQTTLEVMellKQVNKEGR--TLIVVTHETSVAEMCDR 210
Cdd:PLN03130 1401 ATAAVDVRTDALIQ---KTIREEFKscTMLIIAHRLNTIIDCDR 1441
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-177 |
1.41e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRslrNLTESQAADVRSReIGFIFQSfnliaykd 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL---NIAKIGLHDLRFK-ITIIPQD-------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 101 avenialPLFYQGVGR-------ALRKEKALKLLRAVGLEEWGHHLPSEL-----------SGGQKQRIAIARALITEPK 162
Cdd:TIGR00957 1369 -------PVLFSGSLRmnldpfsQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTK 1441
|
170
....*....|....*
gi 1154823909 163 VILADEPTGALDSQT 177
Cdd:TIGR00957 1442 ILVLDEATAAVDLET 1456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-221 |
2.18e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAAD------VRSREIGFIFQSFNl 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINhgfalvTEERRSTGIYAYLD- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 IAYKDAVENIALplfYQGVGRALRKEKALK----LLRAVGLEEWGHHLP-SELSGGQKQRIAIARALITEPKVILADEPT 170
Cdd:PRK10982 343 IGFNSLISNIRN---YKNKVGLLDNSRMKSdtqwVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 171 GALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDGIIVG 221
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAG 471
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-216 |
2.49e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 114 VGRAL---RKE---KALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQ 187
Cdd:NF000106 110 IGR*LdlsRKDaraRADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
90 100
....*....|....*....|....*....
gi 1154823909 188 VNKEGRTLIVVTHETSVAEMCDRTIHIRD 216
Cdd:NF000106 190 MVRDGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-200 |
2.55e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 6 LSGIEKTYPGAQPlhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGE----------YL-----LN-GRS 69
Cdd:PRK11819 9 MNRVSKVVPPKKQ--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgikvgYLpqepqLDpEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 70 LRNLTESQAADVRSreigfIFQSFNLIAykdavENIALPLFYQgvgRALRKEKAlKL---LRAVGLEEWGHHL------- 139
Cdd:PRK11819 87 VRENVEEGVAEVKA-----ALDRFNEIY-----AAYAEPDADF---DALAAEQG-ELqeiIDAADAWDLDSQLeiamdal 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1154823909 140 --P------SELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVnkEGrTLIVVTH 200
Cdd:PRK11819 153 rcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PG-TVVAVTH 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
143-221 |
2.56e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKG 485
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-220 |
3.42e-08 |
|
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: 52.22 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTL-LNILGLLDTFDkGEYLLNGRSLRNLTesqAADVRSReIGFIFQS------- 92
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKLP---LHTLRSR-LSIILQDpilfsgs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 --FNLIAYKDAVENIalplfyqgVGRALRKEKALKLLRAV--GLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADE 168
Cdd:cd03288 111 irFNLDPECKCTDDR--------LWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1154823909 169 PTGALDSQTTlEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:cd03288 183 ATASIDMATE-NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-215 |
3.50e-08 |
|
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: 51.21 E-value: 3.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 143 LSGGQKQRIAIARAL----ITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIR 215
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-214 |
3.79e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLlnilglldTFDkgeyLLNGRSLRNLTESQAADVRSreigFIFQSfnliaYK 99
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSL--------AFD----TIYAEGQRRYVESLSAYARQ----FLGQM-----DK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIA------------------------------LPLFYQGVGRALRkekaLKLLRAVGLEewghHL-----PSELS 144
Cdd:cd03270 68 PDVDSIEglspaiaidqkttsrnprstvgtvteiydyLRLLFARVGIRER----LGFLVDVGLG----YLtlsrsAPTLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 145 GGQKQRIAIARAL---ITEPKVILaDEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:cd03270 140 GGEAQRIRLATQIgsgLTGVLYVL-DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-219 |
5.02e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQPLhVLKGINAQIQEGEMVAIMGASGSGKST-LLNILGLLDTFDkGEYLLNGR-----SLRNLtesq 77
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTlLLTFMRMVEVCG-GEIRVNGReigayGLREL---- 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 78 aadvrSREIGFIFQSfnliaykdavenialPLFYQGVGR--------ALRKE--KALKLlraVGLEEwghHLPSELSG-- 145
Cdd:PTZ00243 1383 -----RRQFSMIPQD---------------PVLFDGTVRqnvdpfleASSAEvwAALEL---VGLRE---RVASESEGid 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 146 ------------GQKQRIAIARALITE-PKVILADEPTG----ALDSQTTLEVMELLkqvnkEGRTLIVVTHETSVAEMC 208
Cdd:PTZ00243 1437 srvleggsnysvGQRQLMCMARALLKKgSGFILMDEATAnidpALDRQIQATVMSAF-----SAYTVITIAHRLHTVAQY 1511
|
250
....*....|.
gi 1154823909 209 DRTIHIRDGII 219
Cdd:PTZ00243 1512 DKIIVMDHGAV 1522
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-221 |
6.19e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 LSGGQKQRIAIARALITEPKVI--LADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI--RDGI 218
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIgpGAGI 556
|
...
gi 1154823909 219 IVG 221
Cdd:PRK00635 557 FGG 559
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-217 |
6.49e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnltesqaadvrsreiGFIFQSFNLIAYK 99
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 100 DAVENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTL 179
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 180 EVMELLKQVNKEGRTLIVVTHETS-VAEMCDRTIHIRDG 217
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSqVKSFCTKALWLHYG 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-200 |
8.90e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 8.90e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 144 SGGQKQRIAIARALITEPKVILADEPTGALDSQTtleVMELLKQVNKEGRTLIVVTH 200
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-212 |
9.04e-08 |
|
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: 50.87 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 29 IQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSlrnltesqaadvrsreigfifqsfnlIAYKdavenialP 108
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------------------------VSYK--------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 109 LF----YQGVGRALRKEKA----------LKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALD 174
Cdd:cd03237 68 QYikadYEGTVRDLLSSITkdfythpyfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 175 SQTTLEVMELLKQ-VNKEGRTLIVVTHETSVAEM-CDRTI 212
Cdd:cd03237 148 VEQRLMASKVIRRfAENNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
143-221 |
1.30e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHE-TSVAEMCDRTIHIRDGIIVG 221
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIAG 476
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-217 |
1.71e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.49 E-value: 1.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1154823909 142 ELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEG-RTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
20-214 |
3.73e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN--ILGLLDTFDKGE---YL----------------LNGRSLRN--LTES 76
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQGfcsNLsiqwgaisrlvhitrdLPGRSQRSipLTYI 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 77 QAAD---------VRSREIGFI---FqSFNL-------------IAYKDAVENIALPL-------------FYQGVG--- 115
Cdd:PRK00635 689 KAFDdlrelfaeqPRSKRLGLTkshF-SFNTplgacaecqglgsITTTDNRTSIPCPSclgkrflpqvlevRYKGKNiad 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 116 ----RALRKEK----------ALKLLRAVGLEewghHLP-----SELSGGQKQRIAIARALIT---EPKVILADEPTGAL 173
Cdd:PRK00635 768 ilemTAYEAEKffldepsiheKIHALCSLGLD----YLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1154823909 174 DSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHI 214
Cdd:PRK00635 844 HTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-212 |
4.01e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-----------------------ILGLlDTFDKGEYL---LNGRSLRN- 72
Cdd:TIGR00630 622 NNLKNITVSIPLGLFTCITGVSGSGKSTLINdtlypalanrlngaktvpgrytsIEGL-EHLDKVIHIdqsPIGRTPRSn 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 73 -------LTESQ---AADVRSREIGFI---FqSFNL------------------------------------------IA 97
Cdd:TIGR00630 701 patytgvFDEIRelfAETPEAKVRGYTpgrF-SFNVkggrceacqgdgvikiemhflpdvyvpcevckgkrynretleVK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 98 YKDavENIALPL---------FYQGVGRALRKekaLKLLRAVGLE--EWGHHLPSeLSGGQKQRIAIARAL---ITEPKV 163
Cdd:TIGR00630 780 YKG--KNIADVLdmtveeayeFFEAVPSISRK---LQTLCDVGLGyiRLGQPATT-LSGGEAQRIKLAKELskrSTGRTL 853
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1154823909 164 ILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTI 212
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-203 |
6.53e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 25 INAQIQEGEMVAIMGASGSGKSTLLNILGLLdtfdkgeyllngRSLRNLTESQAADVRsreIGFIFQS--FNL------I 96
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGEL------------WPVYGGRLTKPAKGK---LFYVPQRpyMTLgtlrdqI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 97 AYKDAVENialpLFYQGVGRAlRKEKALKLL-------RAVGLE---EWghhlPSELSGGQKQRIAIARALITEPKVILA 166
Cdd:TIGR00954 536 IYPDSSED----MKRRGLSDK-DLEQILDNVqlthileREGGWSavqDW----MDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154823909 167 DEPTGALDSQTTLEVMELLKQVnkeGRTLIVVTHETS 203
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREF---GITLFSVSHRKS 640
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-170 |
6.94e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQplHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL--------GLLDTFdkgeyllnGRSLrnlte 75
Cdd:NF033858 2 ARLEGVSHRY-GKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiqqGRVEVL--------GGDM----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 sqaADVRSRE-----IGFIFQSF--NLiaYKD--AVENIAL--PLFyqGVGRALRKEKALKLLRAVGLEEWGHHLPSELS 144
Cdd:NF033858 66 ---ADARHRRavcprIAYMPQGLgkNL--YPTlsVFENLDFfgRLF--GQDAAERRRRIDELLRATGLAPFADRPAGKLS 138
|
170 180
....*....|....*....|....*.
gi 1154823909 145 GGQKQRIAIARALITEPKVILADEPT 170
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-220 |
9.97e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.98 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 32 GEMVAIMGASGSGKSTLLN-ILGLLDTFDKGEYLLNGRSLRNLTESQAadvrsreigfifqsfnliaykdavenialplf 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 111 yqgvgralrkekalkllravgLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMEL-----L 185
Cdd:smart00382 50 ---------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|....*
gi 1154823909 186 KQVNKEGRTLIVVTHETSVAEMCDRTIHIRDGIIV 220
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-220 |
1.53e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGaQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLnilglldtfdkgeyllngRSLRNLTESQAADVRS 83
Cdd:PRK15064 320 LEVENLTKGFDN-GPL--FKNLNLLLEAGERLAIIGENGVGKTTLL------------------RTLVGELEPDSGTVKW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 RE---IGFIFQsfnliaykDAVENIA--LPLF---YQgvgraLRKEKALKL-LRAVgleeWGHHLPSE---------LSG 145
Cdd:PRK15064 379 SEnanIGYYAQ--------DHAYDFEndLTLFdwmSQ-----WRQEGDDEQaVRGT----LGRLLFSQddikksvkvLSG 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 146 GQKQRIAIARALITEPKVILADEPTGALDsqttLEVMELLKQV--NKEGrTLIVVTHETS-VAEMCDRTIHIRDGIIV 220
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMD----MESIESLNMAleKYEG-TLIFVSHDREfVSSLATRIIEITPDGVV 514
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-214 |
1.72e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 21 VLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKG-------------------------EYLLNG-RSLRNLt 74
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGsytfpgnwqlawvnqetpalpqpalEYVIDGdREYRQL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 75 ESQAADVRSREIGfifqsfNLIAYK----DAVENIALplfyqgvgralrKEKALKLLRAVGLEEWGHHLP-SELSGGQKQ 149
Cdd:PRK10636 95 EAQLHDANERNDG------HAIATIhgklDAIDAWTI------------RSRAASLLHGLGFSNEQLERPvSDFSGGWRM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154823909 150 RIAIARALITEPKVILADEPTGALDSQTTLEVMELLKqvNKEGrTLIVVTHETSVAE-MCDRTIHI 214
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK--SYQG-TLILISHDRDFLDpIVDKIIHI 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-188 |
3.74e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 19 LHVLKGINAQIQEGEMVAIMGASGSGKSTLLNIL-GLLDTFDK--GEYLLNGRSLRN-------------------LTES 76
Cdd:PLN03140 178 LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALaGKLDPSLKvsGEITYNGYRLNEfvprktsayisqndvhvgvMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 77 QAADVRSR--EIGFIFQSFNLIAYKDAVENIaLP-----LFY-----QGVGRALRKEKALKLLravGLEEW-----GHHL 139
Cdd:PLN03140 258 ETLDFSARcqGVGTRYDLLSELARREKDAGI-FPeaevdLFMkatamEGVKSSLITDYTLKIL---GLDICkdtivGDEM 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1154823909 140 PSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQV 188
Cdd:PLN03140 334 IRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI 382
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-221 |
4.57e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYPGAQP-LHV--LKG-----INAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTE 75
Cdd:PRK15439 253 LELPGNRRQQAAGAPvLTVedLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 76 SQAADVrsreiGFIF-----QSFNLiaYKDA--VENIAlPLFYQGVGRALRKEKALKLL----RAVGLEEWGHHLPSE-L 143
Cdd:PRK15439 333 AQRLAR-----GLVYlpedrQSSGL--YLDAplAWNVC-ALTHNRRGFWIKPARENAVLeryrRALNIKFNHAEQAARtL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 144 SGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVT---HEtsVAEMCDRTIHIRDGIIV 220
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISsdlEE--IEQMADRVLVMHQGEIS 482
|
.
gi 1154823909 221 G 221
Cdd:PRK15439 483 G 483
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-217 |
5.52e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGrslrnltesqaadvrsrEIGFIFQSFNLIAYKDA 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 102 VENIALPLFYQGVGRALRKEKALKLLRAVGLEEWGHHLPSELSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1154823909 182 MELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDG 217
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLgQVRQFCTKIAWIEGG 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-198 |
1.01e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 29 IQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLNGRSLRNLTESQAADVRSREigfiFQSFN---LIAYKDAVENI 105
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNtdmLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 106 ALPLFYQGVGRALRKEKALKLLravGLEewghHLPSE----LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEV 181
Cdd:PRK10938 102 TAEIIQDEVKDPARCEQLAQQF---GIT----ALLDRrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170
....*....|....*..
gi 1154823909 182 MELLKQVNKEGRTLIVV 198
Cdd:PRK10938 175 AELLASLHQSGITLVLV 191
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-215 |
1.23e-05 |
|
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: 44.52 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 36 AIMGASGSGKSTLLNIL-----GLLDTFDKGeyllnGRSLRNLTESQAadvRSREIGFIFQSFNLIAYK-----DAVENI 105
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyaltGELPPNSKG-----GAHDPKLIREGE---VRAQVKLAFENANGKKYTitrslAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 106 ALplfyqgvgraLRKEKALKLLravgLEEWGHhlpseLSGGQKQ------RIAIARALITEPKVILADEPTGALDS---- 175
Cdd:cd03240 98 IF----------CHQGESNWPL----LDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenie 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1154823909 176 QTTLEVMELLKQvnKEGRTLIVVTHETSVAEMCDRTIHIR 215
Cdd:cd03240 159 ESLAEIIEERKS--QKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-50 |
1.49e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 1.49e-05
10 20
....*....|....*....|....*....
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLN 50
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-200 |
1.49e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTLLN-----------------------ILGlLDTFDKgeyLLN------GRS- 69
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNdilypalarklngakekpgphdsIEG-LEHIDK---VIDidqspiGRTp 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 70 -------------LRNL-TESQAADVR----SReigFifqSFNL------------------------------------ 95
Cdd:COG0178 695 rsnpatytgvfdpIRELfAQTPEAKARgykpGR---F---SFNVkggrceacqgdgvikiemhflpdvyvpcevckgkry 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 96 ------IAYKDAveNI----------ALPLFyQGVGRALRKekaLKLLRAVGLE--EWGHHLPSeLSGGQKQRIAIARAL 157
Cdd:COG0178 769 nretleVKYKGK--NIadvldmtveeALEFF-ENIPKIARK---LQTLQDVGLGyiKLGQPATT-LSGGEAQRVKLASEL 841
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1154823909 158 I---TEPKVILADEPTGAL---DSQTTLEVMELLkqVNKeGRTLIVVTH 200
Cdd:COG0178 842 SkrsTGKTLYILDEPTTGLhfhDIRKLLEVLHRL--VDK-GNTVVVIEH 887
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-214 |
2.09e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 124 LKLLRAVGLEEWGHHLPSE-LSGGQKQRIAIARAL---ITEPKVILaDEPTGALDSQTTLEVMELLKQVNKEGRTLIVVT 199
Cdd:TIGR00630 469 LGFLIDVGLDYLSLSRAAGtLSGGEAQRIRLATQIgsgLTGVLYVL-DEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVE 547
|
90
....*....|....*
gi 1154823909 200 HETSVAEMCDRTIHI 214
Cdd:TIGR00630 548 HDEDTIRAADYVIDI 562
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
143-221 |
2.58e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 143 LSGGQKQRIAIARALITEPKVILADEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHET-SVAEMCDRTIHIRDGIIVG 221
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELLGMCDRIYVMNEGRITG 484
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-200 |
6.30e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIeKTYPGAQPLHVLKGINAqiqegemvaIMGASGSGKSTLLNILGLL-------------DTFDKG--------E 62
Cdd:COG0419 5 LRLENF-RSYRDTETIDFDDGLNL---------IVGPNGAGKSTILEAIRYAlygkarsrsklrsDLINVGseeasvelE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 63 YLLNGRSLR---------NLTESQAADVRSreigFIFQSFNLIAYKDAVENiaLPLFYQGVGRALRKEKALKLLRAVGLE 133
Cdd:COG0419 75 FEHGGKRYRierrqgefaEFLEAKPSERKE----ALKRLLGLEIYEELKER--LKELEEALESALEELAELQKLKQEILA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1154823909 134 E-WGHHLPSELSGGQKQRIAIARALitepKVILaDepTGALDSQTTLEVMELLkqvnkegRTLIVVTH 200
Cdd:COG0419 149 QlSGLDPIETLSGGERLRLALADLL----SLIL-D--FGSLDEERLERLLDAL-------EELAIITH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-201 |
6.57e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 22 LKGINAQIQEGEMVAIMGASGSGKSTLLNI-LGLLDT---------------FDKGEYLLNGRS--LRNLTE-SQAADV- 81
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQAdsgrihcgtklevayFDQHRAELDPEKtvMDNLAEgKQEVMVn 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 82 -RSREIGFIFQSFnliaykdavenialpLFYQGvgRALRKEKALkllravgleewghhlpselSGGQKQRIAIARALITE 160
Cdd:PRK11147 415 gRPRHVLGYLQDF---------------LFHPK--RAMTPVKAL-------------------SGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1154823909 161 PKVILADEPTGALDsqttLEVMELLKQV--NKEGrTLIVVTHE 201
Cdd:PRK11147 459 SNLLILDEPTNDLD----VETLELLEELldSYQG-TVLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-177 |
1.09e-04 |
|
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: 42.61 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 4 IELSGIEKTYpGAQPLhvLKGINAQIQEGEMVAIMGASGSGKSTLLNILGLLDTFDKGEYLLnGRSLRnltesqaadvrs 83
Cdd:TIGR03719 323 IEAENLTKAF-GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 84 reIGFIFQSF-NLIAYKDAVENIALPLFYQGVGRALRKEKA-LKLLRAVGLEEwgHHLPSELSGGQKQRIAIARALITEP 161
Cdd:TIGR03719 387 --LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyVGRFNFKGSDQ--QKKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|....*.
gi 1154823909 162 KVILADEPTGALDSQT 177
Cdd:TIGR03719 463 NVLLLDEPTNDLDVET 478
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-187 |
1.53e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 3 LIELSGIEKTYPGAqPLhVLKGINAQIQEGEMVAIMGASGSGKSTLLNILGlldtfdkGEyllngrslrnLTESQAADVR 82
Cdd:PLN03073 508 IISFSDASFGYPGG-PL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GE----------LQPSSGTVFR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 83 SREIGF-IFQSFNLiaykDAVENIALPLFYQgvgralrkekaLKLLRAVGLEEWGHHLPS-------------ELSGGQK 148
Cdd:PLN03073 569 SAKVRMaVFSQHHV----DGLDLSSNPLLYM-----------MRCFPGVPEQKLRAHLGSfgvtgnlalqpmyTLSGGQK 633
|
170 180 190
....*....|....*....|....*....|....*....
gi 1154823909 149 QRIAIARALITEPKVILADEPTGALDsqttLEVMELLKQ 187
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQ 668
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
28-215 |
7.16e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 28 QIQEGEMVAIMGASGSGKSTLlnilglldtFDKGEYLLNGRSLRNLTESQAADVRSR-----EIGFIFQ----------S 92
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTI---------LDAITYALYGKTPRYGRQENLRSVFAPgedtaEVSFTFQlggkkyrverS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 93 FNLiAYKDAVENIALPlfyQGVGRALrkekalkLLRAVgleewghhlpSELSGGQKQRIAIARALITEPKVILA------ 166
Cdd:cd03279 95 RGL-DYDQFTRIVLLP---QGEFDRF-------LARPV----------STLSGGETFLASLSLALALSEVLQNRggarle 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1154823909 167 ----DEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMCDRTIHIR 215
Cdd:cd03279 154 alfiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-48 |
2.28e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.28e-03
10 20
....*....|....*....|....*....
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTL 48
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
31-217 |
3.37e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 31 EGEMVAIMGASGSGKSTLLNILGLL------DTFDKGEYLLNGRS--------------LRNLTESQAADVRSREIGFIF 90
Cdd:COG3593 22 SDDLTVLVGENNSGKSSILEALRLLlgpsssRKFDEEDFYLGDDPdlpeieieltfgslLSRLLRLLLKEEDKEELEEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 91 QSFN------LIAYKDAVENIALPLF-YQGVGRALRKEKALKLLRAVGLE-EWGHHLP-SELSGGQKQRI------AIAR 155
Cdd:COG3593 102 EELNeelkeaLKALNELLSEYLKELLdGLDLELELSLDELEDLLKSLSLRiEDGKELPlDRLGSGFQRLIllallsALAE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1154823909 156 ALITEPKVILA-DEPTGALDSQTTLEVMELLKQVNKEGRTLIVVTHETSVAEMC--DRTIHIRDG 217
Cdd:COG3593 182 LKRAPANPILLiEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVplENIRRLRRD 246
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-217 |
3.70e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154823909 119 RKEKALKLLRAVGLeewgHHLP-----SELSGGQKQRIAIARALI---TEPKVILADEPTGALDSQTTLEVMELLKQVNK 190
Cdd:PRK00635 1675 KIQKPLQALIDNGL----GYLPlgqnlSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVS 1750
|
90 100
....*....|....*....|....*..
gi 1154823909 191 EGRTLIVVTHETSVAEMCDRTIHIRDG 217
Cdd:PRK00635 1751 LGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
142-177 |
4.51e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.41 E-value: 4.51e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1154823909 142 ELSGGQKQRIAIARALITEPKVILADEPTGALDSQT 177
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
16-52 |
5.03e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.22 E-value: 5.03e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1154823909 16 AQPLHVLKginAQIQEGEMVAIMGASGSGKSTLLNIL 52
Cdd:PRK01889 182 GEGLDVLA---AWLSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
32-86 |
6.11e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 37.28 E-value: 6.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1154823909 32 GEMVAIMGASGSGKSTLLNILGLLDTFDK------GEyllNGRSLRNLTESQAADVRSREI 86
Cdd:PRK06002 165 GQRIGIFAGSGVGKSTLLAMLARADAFDTvvialvGE---RGREVREFLEDTLADNLKKAV 222
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-48 |
6.46e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 6.46e-03
10 20
....*....|....*....|....*....
gi 1154823909 20 HVLKGINAQIQEGEMVAIMGASGSGKSTL 48
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
35-59 |
6.76e-03 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 36.53 E-value: 6.76e-03
10 20
....*....|....*....|....*.
gi 1154823909 35 VAIMGASGSGKSTLLN-ILGLLDTFD 59
Cdd:cd01851 10 VSVFGSQSSGKSFLLNhLFGTSDGFD 35
|
|
| |
