|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-192 |
2.33e-94 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 275.43 E-value: 2.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------NI 72
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489530649 153 DEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEA 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-192 |
8.41e-93 |
|
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: 270.11 E-value: 8.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------NIGYMFQ 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 78 KDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489530649 158 ALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEA 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-192 |
3.12e-63 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 194.66 E-value: 3.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 155 PFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEA 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-192 |
3.34e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 196.47 E-value: 3.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:COG3842 77 rNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEA 199
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-188 |
5.24e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 186.79 E-value: 5.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------ 70
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -----NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSV 145
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHD 188
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-188 |
1.20e-59 |
|
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: 185.77 E-value: 1.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------------- 70
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHD 188
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-192 |
3.43e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 180.83 E-value: 3.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNI--------GYMFQK 78
Cdd:COG4525 5 TVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSA 158
Cdd:COG4525 85 DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 159 LDYQTR-----LLVcddvySIIKNENKSTILVTHDIGEA 192
Cdd:COG4525 165 LDALTReqmqeLLL-----DVWQRTGKGVFLITHSVEEA 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-192 |
2.22e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 181.50 E-value: 2.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIG 73
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprerRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQkDNLLeWRN--IMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILL 151
Cdd:COG1118 79 FVFQ-HYAL-FPHmtVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 152 LDEPFSALDYQTR-----LLVcddvySIIKNENKSTILVTHDIGEA 192
Cdd:COG1118 157 LDEPFGALDAKVRkelrrWLR-----RLHDELGGTTVFVTHDQEEA 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-192 |
3.05e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIG 73
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 154 EPFSALDYQTRLLVCDDVYSiIKNENKSTILVTHDIGEA 192
Cdd:COG1131 157 EPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEA 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-193 |
2.95e-53 |
|
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: 170.16 E-value: 2.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ------NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSL-DRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTL 143
Cdd:COG1127 77 lyelrrRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIrELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 144 SVNPDILLLDEPFSALDYQTrllvCDDVYSIIKNENK----STILVTHDIGEAR 193
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPIT----SAVIDELIRELRDelglTSVVVTHDLDSAF 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-192 |
1.67e-52 |
|
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: 169.36 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 13 MNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------------NIGYM 75
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 FQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 489530649 156 FSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEA 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-193 |
1.15e-51 |
|
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: 165.40 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------------- 70
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 NIGYMFQKDNLLEWRNIMDNITIGL-EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 150 LLLDEPFSALDYQtrlLVcDDVYSIIKN---ENKSTILVTHDIGEAR 193
Cdd:cd03262 157 MLFDEPTSALDPE---LV-GEVLDVMKDlaeEGMTMVVVTHEMGFAR 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-193 |
2.33e-51 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 165.17 E-value: 2.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIGL-EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:COG1126 77 rKVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 149 ILLLDEPFSALDYQtrlLVcDDVYSIIK---NENKSTILVTHDIGEAR 193
Cdd:COG1126 157 VMLFDEPTSALDPE---LV-GEVLDVMRdlaKEGMTMVVVTHEMGFAR 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-195 |
8.23e-51 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 164.01 E-value: 8.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLEWRNIMDN 90
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGLEIQGKKDKKSLDRVESLLKTYGL--WDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVC 168
Cdd:cd03295 96 IALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180
....*....|....*....|....*..
gi 489530649 169 DDVYSIIKNENKSTILVTHDIGEARCI 195
Cdd:cd03295 176 EEFKRLQQELGKTIVFVTHDIDEAFRL 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-195 |
4.58e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.93 E-value: 4.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKE-GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------- 70
Cdd:COG1123 260 LLEVRNLSKRYPVRGkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQkdN----LLEWRNIMDNITIGLEIQGKKDKKSL-DRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIR 141
Cdd:COG1123 340 lrrRVQMVFQ--DpyssLNPRMTVGDIIAEPLRLHGLLSRAERrERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTR-----LLVcddvySIIKNENKSTILVTHDIGEARCI 195
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQaqilnLLR-----DLQRELGLTYLFISHDLAVVRYI 471
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-189 |
4.16e-49 |
|
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: 159.28 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 149 ILLLDEPFSALDYQTrllvCDDVYSIIKNENKS---TI-LVTHDI 189
Cdd:cd03258 161 VLLCDEATSALDPET----TQSILALLRDINRElglTIvLITHEM 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-192 |
8.69e-49 |
|
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: 158.26 E-value: 8.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:COG1122 1 IELENLS---FSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQK-DN-LLEwRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:COG1122 78 GLVFQNpDDqLFA-PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 151 LLDEPFSALDYQTRllvcDDVYSIIKN---ENKSTILVTHDIGEA 192
Cdd:COG1122 157 VLDEPTAGLDPRGR----RELLELLKRlnkEGKTVIIVTHDLDLV 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-192 |
1.31e-48 |
|
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: 158.27 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLD----RVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAeiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 151 LLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-190 |
2.85e-48 |
|
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: 157.66 E-value: 2.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQ------------KDNLLEwrnimdnitiGLEIQGKKDKKslDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVAL 139
Cdd:COG1124 82 QMVFQdpyaslhprhtvDRILAE----------PLRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIG 190
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLA 200
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-193 |
2.88e-48 |
|
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: 156.90 E-value: 2.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGYMFQKDNLLE 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 84 WRNI--------------MdniTIG------LEIQGKKDKKSLDRVESLLKTYGLW---DFRSMYPKELSGGMRQRVALI 140
Cdd:cd03257 81 RKEIqmvfqdpmsslnprM---TIGeqiaepLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489530649 141 RTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVA 210
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-192 |
1.72e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 159.50 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGYM----------------FQKDNLLEWRNI 87
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGeDITKLskkelrelrrkkmsmvFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD------Y 161
Cdd:COG4175 123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDplirreM 202
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 162 QTRLLvcddvySIIKNENKSTILVTHDIGEA 192
Cdd:COG4175 203 QDELL------ELQAKLKKTIVFITHDLDEA 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-188 |
2.12e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.83 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:COG2884 1 MIRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:COG2884 78 rrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 149 ILLLDEPFSALDYQTRLlvcdDVYSIIK--NENKSTILV-THD 188
Cdd:COG2884 158 LLLADEPTGNLDPETSW----EIMELLEeiNRRGTTVLIaTHD 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-193 |
3.46e-47 |
|
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: 152.73 E-value: 3.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------------- 70
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 NIGYMFQKDNLLEWRNIMDNITIGleiqgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDIL 150
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 151 LLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAA 165
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-193 |
5.00e-47 |
|
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: 153.39 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIG 73
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQ--KDNLLEwRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILL 151
Cdd:cd03225 79 LVFQnpDDQFFG-PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 152 LDEPFSALDYQTRllvcDDVYSIIK---NENKSTILVTHDIGEAR 193
Cdd:cd03225 158 LDEPTAGLDPAGR----RELLELLKklkAEGKTIIIVTHDLDLLL 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-192 |
6.21e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 154.47 E-value: 6.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNI--------GYMFQKDNLLEWRNIMDNITIGL 95
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSII 175
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170
....*....|....*..
gi 489530649 176 KNENKSTILVTHDIGEA 192
Cdd:PRK11248 176 QETGKQVLLITHDIEEA 192
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-192 |
7.33e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.16 E-value: 7.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQK----DNLlewrNIMDNITIGLEIQgKKDKKSLD-RVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:COG3839 80 VFQSyalyPHM----TVYENIAFPLKLR-KVPKAEIDrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-192 |
2.22e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 152.70 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGY 74
Cdd:COG4555 3 EVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 155 PFSALDYQTRLLVCDDVYSiIKNENKSTILVTHDIGEA 192
Cdd:COG4555 159 PTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEV 195
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-188 |
2.72e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.24 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILtNLL-KPTSGDIKITG------------- 70
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLeRPTSGSVLVDGvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNP 147
Cdd:COG1135 80 arrKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489530649 148 DILLLDEPFSALDYQT-----RLLvcDDVysiikneNKS---TI-LVTHD 188
Cdd:COG1135 160 KVLLCDEATSALDPETtrsilDLL--KDI-------NRElglTIvLITHE 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-157 |
1.09e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.79 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLEWRNIMDNI 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIGLEIQGKKDKKSLDRVESLLKTYGLWDFR----SMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-195 |
1.36e-45 |
|
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: 150.34 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------------- 70
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSL-DRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:cd03261 77 rRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIrEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEARCI 195
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAI 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-192 |
4.44e-45 |
|
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: 148.87 E-value: 4.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILtNLL------KPTSGDIKITG--------- 70
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLndlipgAPDEGEVLLDGkdiydldvd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ------NIGYMFQKDNLLeWRNIMDNITIGLEIQGKKDKKSLD-RVESLLKTYGLWDF--RSMYPKELSGGMRQRVALIR 141
Cdd:cd03260 76 vlelrrRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLlvcdDVYSIIKNENKST--ILVTHDIGEA 192
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTA----KIEELIAELKKEYtiVIVTHNMQQA 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
1.16e-44 |
|
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: 147.97 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -------NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKslDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTL 143
Cdd:COG4181 84 rarlrarHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489530649 144 SVNPDILLLDEPFSALDYQTRLLVCDDVYSiIKNENKST-ILVTHDIGEA-RC 194
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFE-LNRERGTTlVLVTHDPALAaRC 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-192 |
2.09e-44 |
|
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: 147.38 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 155 PFSALDYQTRllvcDDVYSIIKNENKST----ILVTHDIGEA 192
Cdd:cd03300 157 PLGALDLKLR----KDMQLELKRLQKELgitfVFVTHDQEEA 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-193 |
2.70e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 2.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------NI 72
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLlEWR---NIMDNITIGL-------EIQGKKDKkslDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT 142
Cdd:COG1121 78 GYVPQRAEV-DWDfpiTVRDVVLMGRygrrglfRRPSRADR---EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 143 LSVNPDILLLDEPFSALDYQTRllvcDDVYSIIK---NENKSTILVTHDIGEAR 193
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATE----EALYELLRelrREGKTILVVTHDLGAVR 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-199 |
7.03e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.31 E-value: 7.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMnFYtkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILtNLLK-PTSGDIKITG-------------- 70
Cdd:COG4161 3 IQLKNINC-FY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLEtPDSGQLNIAGhqfdfsqkpsekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -----NIGYMFQKDNLLEWRNIMDNITIG-LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLS 144
Cdd:COG4161 78 rllrqKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 145 VNPDILLLDEPFSALDYQtrllVCDDVYSIIKNENKSTI---LVTHDIGEARCIKVQL 199
Cdd:COG4161 158 MEPQVLLFDEPTAALDPE----ITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQV 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-190 |
1.51e-43 |
|
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: 144.60 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------IGYMFQK 78
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLlEWR---NIMDNITIGL-------EIQGKKDKKsldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:cd03235 77 RSI-DRDfpiSVRDVVLMGLyghkglfRRLSKADKA---KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 149 ILLLDEPFSALDYQTRllvcDDVYSIIKN---ENKSTILVTHDIG 190
Cdd:cd03235 153 LLLLDEPFAGVDPKTQ----EDIYELLRElrrEGMTILVVTHDLG 193
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-193 |
2.28e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 147.12 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP---TSGDI--------------- 66
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEIlfdgedllklsekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 -KITGN-IGYMFQkdnllewrNIMD--N--ITIG------LEIQGKKDKKSL-DRVESLLKTYGL---WDFRSMYPKELS 130
Cdd:COG0444 81 rKIRGReIQMIFQ--------DPMTslNpvMTVGdqiaepLRIHGGLSKAEArERAIELLERVGLpdpERRLDRYPHELS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVA 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-192 |
6.23e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 143.01 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP---TSGDIKITG-----------NIGYMFQKDNLLEWRNIMDN 90
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGL-EIQGKKDKKslDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCD 169
Cdd:COG4136 97 LAFALpPTIGRAQRR--ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|...
gi 489530649 170 DVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG4136 175 FVFEQIRQRGIPALLVTHDEEDA 197
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-199 |
1.49e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 142.11 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGqslsklssnerakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNP 147
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489530649 148 DILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEARCIKVQL 199
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVL 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-192 |
2.74e-42 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 139.84 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIG 73
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNItigleiqgkkdkksldrvesllktyglwdfrsmypkELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:cd03230 77 YLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 154 EPFSALDYQTRllvcDDVYSII---KNENKSTILVTHDIGEA 192
Cdd:cd03230 121 EPTSGLDPESR----REFWELLrelKKEGKTILLSSHILEEA 158
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-192 |
3.68e-42 |
|
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: 148.13 E-value: 3.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYtkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPT---SGDIKITG--------- 70
Cdd:COG1123 2 TPLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ----NIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSV 145
Cdd:COG1123 80 lrgrRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-192 |
4.08e-42 |
|
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: 141.10 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIG 73
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 154 EPFSALDYQTRllvcDDVYSIIKNE--NKSTILVTHDIGEA 192
Cdd:cd03263 159 EPTSGLDPASR----RAIWDLILEVrkGRSIILTTHSMDEA 195
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-193 |
5.67e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.34 E-value: 5.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 14 NFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------IGYMFQ--- 77
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQepa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 78 ------KDNLLEWRNImdnitigleiqgKKDKKSLDRVESLLKTYGL------WDFRsmypkELSGGMRQRVALIRTLSV 145
Cdd:COG4619 85 lwggtvRDNLPFPFQL------------RERKFDRERALELLERLGLppdildKPVE-----RLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIE 195
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-192 |
7.32e-42 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 140.58 E-value: 7.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIG 73
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQK----DNLLEWrnimDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:cd03265 77 IVFQDlsvdDELTGW----ENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEA 195
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-192 |
9.02e-42 |
|
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: 140.08 E-value: 9.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQgKKDKKSLD-RVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLR-KVPKDEIDeRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 154 EPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEA 194
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-163 |
1.85e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.32 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNiLTNLL-KPTSGDIKITG-------------- 70
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLLeRPTSGRVLVDGqdltalsekelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK11153 81 rrQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170
....*....|....*
gi 489530649 149 ILLLDEPFSALDYQT 163
Cdd:PRK11153 161 VLLCDEATSALDPAT 175
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-188 |
2.13e-40 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 145.36 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDF-RSMyPK-----------ELSGGMRQRVALI 140
Cdd:COG2274 552 GVVLQDVFLFS-GTIRENITLG------DPDATDEEIIEAARLAGLHDFiEAL-PMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 141 RTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHD 188
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR 669
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-193 |
8.01e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.99 E-value: 8.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvderlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIG-LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK09493 77 qEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 149 ILLLDEPFSALDYQTR---LLVCDDvysiIKNENKSTILVTHDIGEAR 193
Cdd:PRK09493 157 LMLFDEPTSALDPELRhevLKVMQD----LAEEGMTMVIVTHEIGFAE 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-192 |
1.12e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 138.29 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLD----RVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAaikaKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 151 LLDEPFSALDYQTRllvcDDVYSIIKN---ENKST-ILVTHDIGEA 192
Cdd:PRK10851 159 LLDEPFGALDAQVR----KELRRWLRQlheELKFTsVFVTHDQEEA 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-192 |
1.63e-39 |
|
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: 134.34 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLK-----EGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------------NIGYMFQKDNLLEWRN 86
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIGLeiQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:cd03297 92 VRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180
....*....|....*....|....*.
gi 489530649 167 VCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEA 195
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-189 |
3.03e-39 |
|
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: 134.79 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLEWRN 86
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIG----LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQ 162
Cdd:COG1120 92 VRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180
....*....|....*....|....*..
gi 489530649 163 TRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDL 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-189 |
3.08e-39 |
|
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: 132.12 E-value: 3.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNItigleiqgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLL 152
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 489530649 153 DEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHDI 189
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRL 155
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-193 |
3.90e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.99 E-value: 3.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMnFYtkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILtNLLK-PTSGDIKITGN------------- 71
Cdd:PRK11124 3 IQLNGINC-FY---GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmPRSGTLNIAGNhfdfsktpsdkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ------IGYMFQKDNLLEWRNIMDN-ITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLS 144
Cdd:PRK11124 78 relrrnVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489530649 145 VNPDILLLDEPFSALDYQtrllVCDDVYSIIKNENKSTI---LVTHDIGEAR 193
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPE----ITAQIVSIIRELAETGItqvIVTHEVEVAR 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-192 |
6.22e-39 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 133.36 E-value: 6.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------NIGYMFQKDNLLEWRNIMDNITIGLE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 97 IQGKKDKKSLDR--VESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSI 174
Cdd:TIGR01184 81 RVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170
....*....|....*...
gi 489530649 175 IKNENKSTILVTHDIGEA 192
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEA 178
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-192 |
1.03e-38 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 134.82 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNI 87
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvreprkvrrSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180
....*....|....*....|....*
gi 489530649 168 CDDVYSiIKNENKSTILVTHDIGEA 192
Cdd:TIGR01188 164 WDYIRA-LKEEGVTILLTTHYMEEA 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-193 |
1.07e-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: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEvLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:cd03299 1 LKVENLSKDW----KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 155 PFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAW 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-192 |
1.61e-38 |
|
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: 133.32 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------------N 71
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeenlweirkK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 151 LLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-195 |
4.14e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.03 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGY----------MFQKDNLLEWRNIMDNITIGLEI 97
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTAlppaerpvsmLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 QGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR----LLVCDdvys 173
Cdd:COG3840 99 GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRqemlDLVDE---- 174
|
170 180
....*....|....*....|...
gi 489530649 174 iIKNENKSTIL-VTHDIGEARCI 195
Cdd:COG3840 175 -LCRERGLTVLmVTHDPEDAARI 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-192 |
7.09e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.69 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:PRK11432 2 TQKNFVVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK11432 78 rDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-193 |
7.18e-38 |
|
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: 128.13 E-value: 7.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIgymFQKDNLLEWRN 86
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD---IAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 imdniTIGLEIQgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:cd00267 74 -----RIGYVPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180
....*....|....*....|....*....
gi 489530649 167 VcddVYSI--IKNENKSTILVTHDIGEAR 193
Cdd:cd00267 119 L---LELLreLAEEGRTVIIVTHDPELAE 144
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-192 |
9.21e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 9.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:PRK13635 1 MKEEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVN 146
Cdd:PRK13635 79 vrrQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 147 PDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-193 |
1.77e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.16 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMnFYtkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNIL--TNLLKP---TSGDIKITG------- 70
Cdd:COG1117 9 EPKIEVRNLNV-YY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGediydpd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --------NIGYMFQKDNLLEWrNIMDNITIGLEIQGKKDKKSLD-RVESLLKTYGLWDfrsmypkE-----------LS 130
Cdd:COG1117 85 vdvvelrrRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDeIVEESLRKAALWD-------EvkdrlkksalgLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCD------DVYSIiknenkstILVTHDIGEAR 193
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEElilelkKDYTI--------VIVTHNMQQAA 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-188 |
3.09e-37 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 128.52 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------- 71
Cdd:TIGR02673 1 MIEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlrgrqlpll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ---IGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:TIGR02673 78 rrrIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDdvysIIKNENKS--TILV-THD 188
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILD----LLKRLNKRgtTVIVaTHD 196
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-192 |
5.72e-37 |
|
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: 126.78 E-value: 5.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGnigymfqkDNLLEWRN 86
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------KDLASLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIGLeiqgkkdkksldrVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:cd03214 69 KELARKIAY-------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180
....*....|....*....|....*.
gi 489530649 167 VCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLA 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-193 |
1.26e-36 |
|
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: 127.68 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------- 71
Cdd:cd03256 2 EVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQKDNLLEWRNIMDNITIG-----------LEIQGKKDKKsldRVESLLKTYGLWDFRSMYPKELSGGMRQRVAL 139
Cdd:cd03256 79 qIGMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQ---RALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAR 209
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-188 |
1.84e-36 |
|
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: 126.19 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 8 VKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN---------------- 71
Cdd:TIGR03608 1 LKNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpplnskkaskfrre 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:TIGR03608 77 kLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 151 LLDEPFSALDYQTRLLVCdDVYSIIKNENKSTILVTHD 188
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVL-DLLLELNDEGKTIIIVTHD 193
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-193 |
2.01e-36 |
|
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: 127.03 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIGL-----EIQG------KKDKKsldRVESLLKTYGLWDFRSMYPKELSGGMRQRV 137
Cdd:TIGR02315 78 rrRIGMIFQHYNLIERLTVLENVLHGRlgykpTWRSllgrfsEEDKE---RALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 138 ALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAK 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-193 |
6.30e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.94 E-value: 6.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQKDNLLEWRNIMDNITIG-----------LEIQGKKDKkslDRVESLLKTYGLWDFRSMYPKELSGGMRQRV 137
Cdd:COG3638 79 rrRIGMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDR---ERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 138 ALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLAR 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-192 |
1.27e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 128.14 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK09452 86 rHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489530649 150 LLLDEPFSALDYQTRLlvcddvysIIKNENKST--------ILVTHDIGEA 192
Cdd:PRK09452 166 LLLDESLSALDYKLRK--------QMQNELKALqrklgitfVFVTHDQEEA 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-192 |
1.61e-35 |
|
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: 126.84 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 40 LLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDR 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 109 VESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHD 188
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
....
gi 489530649 189 IGEA 192
Cdd:TIGR01187 161 QEEA 164
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-192 |
2.06e-35 |
|
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: 125.26 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG----------------NIGYMFQ--KDNLL 82
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditakkkkklkdlrkKVGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 83 EwRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL----WDfRSmyPKELSGGMRQRVALIRTLSVNPDILLLDEPFSA 158
Cdd:TIGR04521 97 E-ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdeeyLE-RS--PFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 159 LDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDV 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-193 |
2.26e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKItGNI------------- 72
Cdd:PRK11264 4 IEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDItidtarslsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 ---------GYMFQKDNLLEWRNIMDNITIG-LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT 142
Cdd:PRK11264 79 lirqlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 143 LSVNPDILLLDEPFSALDYQtrlLVcDDVYSIIK---NENKSTILVTHDIGEAR 193
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE---LV-GEVLNTIRqlaQEKRTMVIVTHEMSFAR 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-192 |
2.98e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.40 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIkITGN---------IGYMFQKDNLLEWRNIMDN 90
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaplaearedTRLMFQDARLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGLeiQGKKDKKSLDRVESLlktyGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDD 170
Cdd:PRK11247 102 VGLGL--KGQWRDAALQALAAV----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180
....*....|....*....|..
gi 489530649 171 VYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11247 176 IESLWQQHGFTVLLVTHDVSEA 197
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-192 |
3.27e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkEGELEVlKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------IG 73
Cdd:PRK11607 19 LLEIRNLTKSF---DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNITIGLEiQGKKDKKSL-DRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLK-QDKLPKAEIaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489530649 153 DEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-194 |
4.60e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 123.35 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------ 70
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeara 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -----NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSV 145
Cdd:PRK10584 84 klrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIG-EARC 194
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQlAARC 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-191 |
5.11e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.46 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------- 71
Cdd:PRK13650 2 SNIIEVKNLTFK-YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 --IGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK13650 81 hkIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGE 191
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-190 |
6.07e-35 |
|
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: 122.93 E-value: 6.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIK-----ITG---------NI 72
Cdd:cd03219 2 EVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGlppheiarlGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEWRNIMDNITIGLEIQG----------KKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT 142
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489530649 143 LSVNPDILLLDEPFSALD----YQTRLLVCDdvysiIKNENKSTILVTHDIG 190
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNpeetEELAELIRE-----LRERGITVLLVEHDMD 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-192 |
8.19e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 126.69 E-value: 8.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------------NIGYMFQKDNLLEWRNI 87
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180
....*....|....*....|....*
gi 489530649 168 CDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEA 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-195 |
3.16e-34 |
|
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: 120.28 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNI 87
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGKKDkkSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:COG4133 93 RENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 168 CDdvysII---KNENKSTILVTHD---IGEARCI 195
Cdd:COG4133 171 AE----LIaahLARGGAVLLTTHQpleLAAARVL 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-187 |
4.33e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.82 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLEwR 85
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFS-G 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDF-RSMyPK-----------ELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:COG1132 429 TIRENIRYG------RPDATDEEVEEAAKAAQAHEFiEAL-PDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 154 EPFSALDYQTRLLvcddvysIIKN-----ENKSTILVTH 187
Cdd:COG1132 502 EATSALDTETEAL-------IQEAlerlmKGRTTIVIAH 533
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-187 |
1.01e-33 |
|
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: 119.31 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN---------IGYMF 76
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 77 QKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 157 SALDYQTRLLVcDDVYSIIKNENKSTILVTH 187
Cdd:cd03269 157 SGLDPVNVELL-KDVIRELARAGKTVILSTH 186
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-190 |
1.14e-33 |
|
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: 120.14 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI-----KITG------ 70
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrDITGlpphri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQKDNLLEWRNIMDNITIGLEIQG---------------KKDKKSLDRVESLLKTYGLWDFRSMYPKELSGG 132
Cdd:COG0411 77 arlGIARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 133 MRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIG 190
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-192 |
1.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVN 146
Cdd:PRK13632 81 irkKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489530649 147 PDILLLDEPFSALDYQTRllvcDDVYSII----KNENKSTILVTHDIGEA 192
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGK----REIKKIMvdlrKTRKKTLISITHDMDEA 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-198 |
1.73e-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: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------IGYMFQKDNLLEWRNIMDNITIGLEI 97
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 QGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKN 177
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180
....*....|....*....|.
gi 489530649 178 ENKSTILVTHDIGEARCIKVQ 198
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQ 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-188 |
2.03e-33 |
|
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: 118.66 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG----------------NIGYMFQKDNLLEWRNIM 88
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVC 168
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180
....*....|....*....|.
gi 489530649 169 DDVYSIikNENKSTILV-THD 188
Cdd:cd03292 177 NLLKKI--NKAGTTVVVaTHA 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-195 |
3.05e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.53 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------IGYMFQKDNLLEWRNIMDNITIGLEI 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 QGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR-----LL--VCDd 170
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqemltLVsqVCQ- 177
|
170 180
....*....|....*....|....*.
gi 489530649 171 vysiiknENKSTIL-VTHDIGEARCI 195
Cdd:PRK10771 178 -------ERQLTLLmVSHSLEDAARI 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-199 |
3.19e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 18 KEGEL--EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------------IGYMFQK 78
Cdd:PRK11629 16 QEGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaelrnqkLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLwDFRSMY-PKELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHrPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 158 ALDYQTrllvCDDVYSIIKNENKST----ILVTHDIGEARCIKVQL 199
Cdd:PRK11629 175 NLDARN----ADSIFQLLGELNRLQgtafLVVTHDLQLAKRMSRQL 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-160 |
3.32e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGEL----EVLK---DVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NI 72
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDnLLEWR--------------N----IMDNITIGLEIQGKKDKKSL-DRVESLLKTYGLW-DFRSMYPKELSGG 132
Cdd:COG4608 83 TGLSGRE-LRPLRrrmqmvfqdpyaslNprmtVGDIIAEPLRIHGLASKAERrERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180
....*....|....*....|....*...
gi 489530649 133 MRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-189 |
3.75e-33 |
|
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: 117.74 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG----------NIGYMF 76
Cdd:cd03226 1 RIENIS---FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 77 QK-DNLLEWRNIMDNITIGLEIQGKKdkksLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:cd03226 78 QDvDYQLFTDSVREELLLGLKELDAG----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 156 FSALDYQTRLLVCdDVYSIIKNENKSTILVTHDI 189
Cdd:cd03226 154 TSGLDYKNMERVG-ELIRELAAQGKAVIVITHDY 186
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-192 |
7.15e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.90 E-value: 7.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGY 74
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaerGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 155 PFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-189 |
6.10e-32 |
|
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: 120.63 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:COG4988 337 IELEDVS---FSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEWrNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-------E----LSGGMRQRVALIR 141
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALAR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHDI 189
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL 532
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-195 |
1.07e-31 |
|
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: 114.13 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFnlKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------IGYMFQKDNLLEWRNI 87
Cdd:cd03298 10 YGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:cd03298 88 EQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180
....*....|....*....|....*...
gi 489530649 168 CDDVYSIIKNENKSTILVTHDIGEARCI 195
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRL 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-191 |
1.82e-31 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.74 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 27 DVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------------NIGYMFQKDNLLEWRNIMD 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 NITIGLE-IQGKKDKKSLDRVESLLktyGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR--LL 166
Cdd:COG4148 97 NLLYGRKrAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKaeIL 173
|
170 180 190
....*....|....*....|....*....|
gi 489530649 167 -----VCDDVySIiknenkSTILVTHDIGE 191
Cdd:COG4148 174 pylerLRDEL-DI------PILYVSHSLDE 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-160 |
4.27e-31 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 113.02 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQKDNLLEWRNIMD 89
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489530649 90 NITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
24-188 |
8.36e-31 |
|
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: 117.56 E-value: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLewrN--IM 88
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLF---DttLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-------E----LSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:COG4987 427 ENLRLA------RPDATDEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 158 ALDYQTRLLVCDDVYSIIKneNKSTILVTHD 188
Cdd:COG4987 501 GLDAATEQALLADLLEALA--GRTVLLITHR 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-192 |
8.70e-31 |
|
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: 112.08 E-value: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NI 72
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 153 DEPFSALD-YQTRLLVcdDVYSIIKNENKSTILVTHDIGEA 192
Cdd:cd03266 161 DEPTTGLDvMATRALR--EFIRQLRALGKCILFSTHIMQEV 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-193 |
1.50e-30 |
|
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: 109.44 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIgymfqkdnlLEWR 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE---------VSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGLEI--QgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT 163
Cdd:cd03216 68 SPRDARRAGIAMvyQ------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190
....*....|....*....|....*....|...
gi 489530649 164 RllvcDDVYSIIKN---ENKSTILVTHDIGEAR 193
Cdd:cd03216 118 V----ERLFKVIRRlraQGVAVIFISHRLDEVF 146
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-192 |
1.99e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.79 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMnFYTKEgelEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILT--------------------NLLK 60
Cdd:PRK14239 1 MTEPILQVSDLSV-YYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlnpevtitgsivynghNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 61 PTSGDIKITGNIGYMFQKDNLLEWrNIMDNITIGLEIQGKKDKKSLDR-VESLLKTYGLWDFRSMYPKE----LSGGMRQ 135
Cdd:PRK14239 77 PRTDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIWDEVKDRLHDsalgLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489530649 136 RVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIikNENKSTILVTHDIGEA 192
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQA 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-189 |
2.10e-30 |
|
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: 111.02 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNL- 81
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 -----------LEWRNIMDNITIGLEiqgkkdKKSLDRVESLLKTYGLWDFRSMYPKE-----------LSGGMRQRVAL 139
Cdd:cd03248 88 skvslvgqepvLFARSLQDNIAYGLQ------SCSFECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSiiKNENKSTILVTHDI 189
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRL 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-188 |
4.02e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.98 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------- 70
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNP 147
Cdd:PRK10535 84 rreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489530649 148 DILLLDEPFSALDYQTRllvcDDVYSIIK---NENKSTILVTHD 188
Cdd:PRK10535 164 QVILADEPTGALDSHSG----EEVMAILHqlrDRGHTVIIVTHD 203
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
23-160 |
4.97e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.50 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYM------FQKdnLl 82
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLpqeasiFRK--L- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 83 ewrNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:COG1137 94 ---TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-160 |
7.89e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 111.35 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------NIGYM 75
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpedrrRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 fqkdnlLEWRNIMDNITIG------LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:COG4152 77 ------PEERGLYPKMKVGeqlvylARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170
....*....|.
gi 489530649 150 LLLDEPFSALD 160
Cdd:COG4152 151 LILDEPFSGLD 161
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-192 |
1.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGD---IKITG------- 70
Cdd:PRK13640 1 MKDNIVEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGitltakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ------NIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTL 143
Cdd:PRK13640 79 vwdireKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489530649 144 SVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-187 |
1.82e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 107.30 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIG 73
Cdd:cd03246 2 EVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEwRNIMDNItigleiqgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:cd03246 80 YLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 154 EPFSALDYQTRLLVCDDVYSiIKNENKSTILVTH 187
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAA-LKAAGATRIVIAH 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-191 |
4.54e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN---------- 71
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprda 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ----IGYMFQKDNLLEWRNIMDNITIGLEIQGK---KDKKSLDRVESLLKTYGLwDFRsmyP----KELSGGMRQRVALI 140
Cdd:COG1129 77 qaagIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGL-DID---PdtpvGDLSVAQQQLVEIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 141 RTLSVNPDILLLDEPFSAL-DYQTRLLvcddvYSII---KNENKSTILVTHDIGE 191
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREVERL-----FRIIrrlKAQGVAIIYISHRLDE 202
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-194 |
5.11e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 107.96 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------IGYMFQk 78
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrrqVGVVLQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEWRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNP 147
Cdd:cd03252 84 ENVLFNRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 148 DILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHDIGEARC 194
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN 202
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-185 |
6.44e-29 |
|
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: 107.13 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMnFYtkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIK-----ITG---------NI 72
Cdd:cd03224 2 EVENLNA-GY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrdITGlppheraraGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEWRNIMDNITIGLEIQGKKDKK-SLDRVESL---LKtyglwDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRRAKRKaRLERVYELfprLK-----ERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 149 ILLLDEPFSALdyqtRLLVCDDVYSIIKNENKS--TILV 185
Cdd:cd03224 153 LLLLDEPSEGL----APKIVEEIFEAIRELRDEgvTILL 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-193 |
7.20e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 7.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------- 71
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -----IGYMFQK----DNL--LEwrnimdNITIGLEI--QGKKDKKSL-DRVESLLKTYGL--------WDfrsmypkeL 129
Cdd:COG3845 77 aialgIGMVHQHfmlvPNLtvAE------NIVLGLEPtkGGRLDRKAArARIRELSERYGLdvdpdakvED--------L 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530649 130 SGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRllvcDDVYSIIKN---ENKSTILVTHDIGEAR 193
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTPQEA----DELFEILRRlaaEGKSIIFITHKLREVM 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-187 |
7.76e-29 |
|
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: 106.91 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQkDNLLEWRNIMDNITIGLEIQgkKDKksldRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:cd03245 81 GYVPQ-DVTLFYGTLRDNITLGAPLA--DDE----RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIknENKSTILVTH 187
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITH 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-187 |
1.10e-28 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 106.85 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEgELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:cd03249 1 IEFKNVSFRYPSRP-DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:cd03249 80 GLVSQEPVLFD-GTIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTH 187
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAH 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-192 |
1.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNfYTKEGELE---VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG-------DIKITGN 71
Cdd:PRK13633 1 MNEMIKCKNVSYK-YESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdglDTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 I-------GYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTL 143
Cdd:PRK13633 80 LwdirnkaGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489530649 144 SVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-193 |
2.58e-28 |
|
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: 110.45 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------I 72
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNITIgleiqGKKDKKSLDRVESLLKTyGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:TIGR02857 399 AWVPQHPFLFA-GTIAENIRL-----ARPDASDAEIREALERA-GLDEFVAALPQgldtpigeggaGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIknENKSTILVTHDIGEAR 193
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAA 521
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-187 |
2.75e-28 |
|
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: 105.78 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNfYTKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:cd03251 1 VEFKNVTFR-YPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQkDNLLEWRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:cd03251 79 GLVSQ-DVFLFNDTVAENIAYG------RPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTH 187
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH 195
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-193 |
3.26e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 105.31 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNI------GYMFQKDnlLEWRnim 88
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllglGGGFNPE--LTGR--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRlLVC 168
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ-EKC 181
|
170 180
....*....|....*....|....*
gi 489530649 169 DDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSSIK 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-189 |
5.38e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.97 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNinMNFYTKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------- 71
Cdd:PRK13647 2 DNIIEVED--LHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekwvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 --IGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK13647 79 skVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489530649 149 ILLLDEPFSALDYQTRllvcDDVYSII---KNENKSTILVTHDI 189
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQ----ETLMEILdrlHNQGKTVIVATHDV 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-187 |
8.12e-28 |
|
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: 104.61 E-value: 8.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINmnFYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------I 72
Cdd:cd03254 3 IEFENVN--FSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNITIGLEIQGKkdkkslDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:cd03254 80 GVVLQDTFLFS-GTIMENIRLGRPNATD------EEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIikNENKSTILVTH 187
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAH 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-191 |
1.36e-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: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG-DIKItgnIGYMFQKDNL 81
Cdd:COG1119 1 DPLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRL---FGERRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 LEWR------------NIMDNIT------------IGL-----EIQgkkdkksLDRVESLLKTYGLWDFRSMYPKELSGG 132
Cdd:COG1119 74 WELRkriglvspalqlRFPRDETvldvvlsgffdsIGLyreptDEQ-------RERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 133 MRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGE 191
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-160 |
2.35e-27 |
|
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: 102.68 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------IGY 74
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyqkniealrrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKDNLLEWRNIMDNITIGLEIQGKKDKksldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
....*.
gi 489530649 155 PFSALD 160
Cdd:cd03268 153 PTNGLD 158
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-193 |
2.91e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--IGYMFQK---DNLLEWRnIMDNITIGL--- 95
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarVAYVPQRsevPDSLPLT-VRDLVAMGRwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 -EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRllvcDDVYSI 174
Cdd:NF040873 86 rGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR----ERIIAL 161
|
170 180
....*....|....*....|..
gi 489530649 175 IKNE--NKSTIL-VTHDIGEAR 193
Cdd:NF040873 162 LAEEhaRGATVVvVTHDLELVR 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-191 |
6.10e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMnfytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN---------- 71
Cdd:PRK10247 4 NSPLLQLQNVGY----LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ---IGYMFQKDNLLEwRNIMDNITIGLEIqgKKDKKSLDRVESLLKTYGLWDfrSMYPK---ELSGGMRQRVALIRTLSV 145
Cdd:PRK10247 80 rqqVSYCAQTPTLFG-DTVYDNLIFPWQI--RNQQPDPAIFLDDLERFALPD--TILTKniaELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGE 191
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-187 |
1.32e-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: 100.62 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGELE-VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKdnllEW 84
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQE----PW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 -RN--IMDNITIGLEIQGKKDKKSLdRVESLLKtyglwDFRSMyPK-------E----LSGGMRQRVALIRTLSVNPDIL 150
Cdd:cd03250 77 iQNgtIRENILFGKPFDEERYEKVI-KACALEP-----DLEIL-PDgdlteigEkginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 489530649 151 LLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTH 187
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTH 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-187 |
1.44e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.43 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEG---ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------------NIG 73
Cdd:PRK13637 7 NLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQ--KDNLLEwRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL--WDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK13637 87 LVFQypEYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 150 LLLDEPFSALDYQTRllvcDDVYSIIKN----ENKSTILVTH 187
Cdd:PRK13637 166 LILDEPTAGLDPKGR----DEILNKIKElhkeYNMTIILVSH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-192 |
1.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------ 70
Cdd:PRK13642 2 NKILEVENLVFK-YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 -NIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK13642 81 rKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-187 |
1.81e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.27 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNL--LKPTSGDI----------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 -----------------------------KITGNIGYMFQKD-NLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTY 116
Cdd:TIGR03269 77 kvgepcpvcggtlepeevdfwnlsdklrrRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489530649 117 GLwDFRSMY-PKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTH 187
Cdd:TIGR03269 157 QL-SHRITHiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-192 |
2.12e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.02 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKItGN------------------IGYMFQ--KDNLLEw 84
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GErvitagkknkklkplrkkVGIVFQfpEHQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT 163
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180
....*....|....*....|....*....
gi 489530649 164 RLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDA 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-187 |
2.19e-26 |
|
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: 100.77 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQkDNLLEWRNIMDNITIGLE-------IQGKKDKKSLDRVESLLKTY-------GLwdfrsmypkELSGGMRQRVA 138
Cdd:cd03253 78 GVVPQ-DTVLFNDTIGYNIRYGRPdatdeevIEAAKAAQIHDKIMRFPDGYdtivgerGL---------KLSGGEKQRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489530649 139 LIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTH 187
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAH 194
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-190 |
3.01e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.33 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------------IGYMFQKDNLLE 83
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflrrqIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 84 WRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQt 163
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA- 171
|
170 180 190
....*....|....*....|....*....|
gi 489530649 164 rllVCDDVYSIIKNENK---STILVTHDIG 190
Cdd:PRK10908 172 ---LSEGILRLFEEFNRvgvTVLMATHDIG 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-193 |
4.27e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.81 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------- 71
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -----------------IGYMFQKDNLLEWRNIMDNITIG-LEIQGKKDKKSLDRVESLLKTYGLWD-FRSMYPKELSGG 132
Cdd:PRK10619 77 gqlkvadknqlrllrtrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 133 MRQRVALIRTLSVNPDILLLDEPFSALDYQtrllVCDDVYSIIKN---ENKSTILVTHDIGEAR 193
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPE----LVGEVLRIMQQlaeEGKTMVVVTHEMGFAR 216
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
12-193 |
5.54e-26 |
|
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: 104.44 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQk 78
Cdd:TIGR01846 460 NIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGVVLQ- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEWRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNP 147
Cdd:TIGR01846 539 ENVLFSRSIRDNIALC------NPGAPFEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNP 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 148 DILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHDIGEAR 193
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVR 656
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-192 |
5.83e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINmnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI-------------K 67
Cdd:PRK13648 3 DKNSIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 68 ITGNIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVN 146
Cdd:PRK13648 81 LRKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 147 PDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-188 |
6.52e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 8 VKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--IGYMFQKDNLLEWR 85
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGL----EIQGKKDK------------KSLDRVESLLKTYGLWDF-------------------RSMypKELS 130
Cdd:COG0488 77 TVLDTVLDGDaelrALEAELEEleaklaepdedlERLAELQEEFEALGGWEAearaeeilsglgfpeedldRPV--SELS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPfsaldyqTRLLvcdDVYSI------IKNENKSTILVTHD 188
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEP-------TNHL---DLESIewleefLKNYPGTVLVVSHD 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-189 |
8.61e-26 |
|
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: 98.80 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGeILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------IG 73
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQkDNllewrNIMDNITIgLE-------IQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVN 146
Cdd:cd03264 76 YLPQ-EF-----GVYPNFTV-REfldyiawLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 147 PDILLLDEPFSALDYQTRLlvcdDVYSIIKN--ENKSTILVTHDI 189
Cdd:cd03264 149 PSILIVDEPTAGLDPEERI----RFRNLLSElgEDRIVILSTHIV 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-197 |
1.07e-25 |
|
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: 98.94 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLL 82
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkflrRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 83 EWR-NIMDNITIGLEIQGKKD---KKSLDRVESLLKtygLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSA 158
Cdd:cd03267 107 WWDlPVIDSFYLLAAIYDLPParfKKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 159 LDYQTRLlvcdDVYSIIKNENKST----ILVTHDIG--EARCIKV 197
Cdd:cd03267 184 LDVVAQE----NIRNFLKEYNRERgttvLLTSHYMKdiEALARRV 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-189 |
1.45e-25 |
|
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: 102.57 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKE-GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI--------------- 66
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 -----KITGNIGYMFQKDNLLEWRNIMDNIT--IGLEIqgkKDKKSLDRVESLLKTYGLWDFRSM-----YPKELSGGMR 134
Cdd:TIGR03269 357 pdgrgRAKRYIGILHQEYDLYPHRTVLDNLTeaIGLEL---PDELARMKAVITLKMVGFDEEKAEeildkYPDELSEGER 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 135 QRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-187 |
1.65e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.88 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------NIGYMFQK- 78
Cdd:TIGR00958 479 IEFQDVSFS-YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyDHHYLHRQv 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 -----DNLLEWRNIMDNITIGLeiqgkkDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRT 142
Cdd:TIGR00958 558 alvgqEPVLFSGSVRENIAYGL------TDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 143 LSVNPDILLLDEPFSALDYQTRLLvcddVYSIIKNENKSTILVTH 187
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAH 672
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-192 |
2.84e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 8 VKNINMNFYTkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLK-----PTSGDIKITG------------ 70
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGrniyspdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---NIGYMFQKDNLLEWRNIMDNITIGLEIQG-KKDKKSLD-RVESLLKTYGLWD----FRSMYPKELSGGMRQRVALIR 141
Cdd:PRK14267 83 vrrEVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDeRVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIikNENKSTILVTHDIGEA 192
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQA 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-191 |
1.08e-24 |
|
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: 98.65 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 11 INMNFYTKEGELEVlkDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------------IG 73
Cdd:TIGR02142 1 LSARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNITIGL-EIQGKKDKKSLDRVESLLktyGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNLRYGMkRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 153 DEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGE 191
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQE 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-160 |
1.37e-24 |
|
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: 99.76 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEG-------ELEVLKDVNFNLKEGEILTLLGPSGSGKSTI-LNILtNLLkPTSGDIKITG-NIGYM 75
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLI-PSEGEIRFDGqDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 FQKDnLLEWR------------------NIMDNITIGLEIQGKKDKKS--LDRVESLLKTYGL-WDFRSMYPKELSGGMR 134
Cdd:COG4172 353 SRRA-LRPLRrrmqvvfqdpfgslsprmTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLdPAARHRYPHEFSGGQR 431
|
170 180
....*....|....*....|....*.
gi 489530649 135 QRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD 457
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-192 |
1.38e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 96.07 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 30 FNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--------NIGYMFQKDNLlEW-------RNIMDNIT-- 92
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGaspgkgwrHIGYVPQRHEF-AWdfpisvaHTVMSGRTgh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 93 IGLEIQGKKDKKSldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCdDVY 172
Cdd:TIGR03771 80 IGWLRRPCVADFA--AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT-ELF 156
|
170 180
....*....|....*....|
gi 489530649 173 SIIKNENKSTILVTHDIGEA 192
Cdd:TIGR03771 157 IELAGAGTAILMTTHDLAQA 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-189 |
1.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------- 71
Cdd:PRK13639 1 ILETRDLK---YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 --IGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK13639 78 ktVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIikNENKSTILV-THDI 189
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDL--NKEGITIIIsTHDV 197
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-185 |
2.39e-24 |
|
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: 95.43 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMnFYtkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIK-----ITGN---------I 72
Cdd:COG0410 5 EVENLHA-GY---GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgedITGLpphriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMfqkdnlLEWRNI------MDNITIGLEIQGKKD--KKSLDRVESL---LKtyglwDFRSMYPKELSGGMRQRVALIR 141
Cdd:COG0410 81 GYV------PEGRRIfpsltvEENLLLGAYARRDRAevRADLERVYELfprLK-----ERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALdyQTrlLVCDDVYSIIK--NENKSTILV 185
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGL--AP--LIVEEIFEIIRrlNREGVTILL 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-189 |
2.87e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.57 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--IGYMFQKDNL 81
Cdd:PRK09544 3 SLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 lewrnimdNITIGLEIQ-------GKKDKK---SLDRVES--LLKtyglwdfrsmYP-KELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK09544 79 --------DTTLPLTVNrflrlrpGTKKEDilpALKRVQAghLID----------APmQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-194 |
5.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG-----DIKITGN------------IGYMFQ--KDNL 81
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGtvtvdDITITHKtkdkyirpvrkrIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 LEwrnimDNITIGLEIQGKKDKKSLDRVES----LLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PRK13646 99 FE-----DTVEREIIFGPKNFKMNLDEVKNyahrLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 157 SALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEARC 194
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVAR 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-166 |
5.34e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGnigymfqkDNLLEW--------RNIM------- 88
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG--------RPLAAWspwelarrRAVLpqhssla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 ------DNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRS-MYPkELSGGMRQRVALIRTL-----SVNPD--ILLLDE 154
Cdd:COG4559 88 fpftveEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLaqlwePVDGGprWLFLDE 166
|
170
....*....|....
gi 489530649 155 PFSALD--YQTRLL 166
Cdd:COG4559 167 PTSALDlaHQHAVL 180
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-190 |
6.16e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 94.36 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 27 DVNFNLKEGEILTLLGPSGSGKST----ILNILTNLLKPTSGDIKITG-----------NIGYMFQ--KDNLLEWRNIMD 89
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGrpllplsirgrHIATIMQnpRTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 NITIGLEIQGKKDKKSLDRVESLLKTYGLWDFR---SMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180
....*....|....*....|....
gi 489530649 167 VCDDVYSIIKNENKSTILVTHDIG 190
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLG 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-193 |
7.12e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDnIVEVKNINMNF------------------YTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPT 62
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 63 SGDIKITGNIGYM------FQKDnlLEWRnimDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMyP-KELSGGMRQ 135
Cdd:COG1134 80 SGRVEVNGRVSALlelgagFHPE--LTGR---ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 136 RVALIRTLSVNPDILLLDEPFSALD--YQTRllvCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDaaFQKK---CLARIRELRESGRTVIFVSHSMGAVR 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-188 |
1.77e-23 |
|
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: 96.66 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------IGYMFQKDNLLEwR 85
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFD-T 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYP-----------KELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:TIGR02868 424 TVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 155 PFSALDYQTRLLVCDDVYSIikNENKSTILVTHD 188
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-192 |
2.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLK-----PTSGDIKITGN------- 71
Cdd:PRK14247 2 NKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQdifkmdv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ------IGYMFQKDNLLEWRNIMDNITIGLEIQG-KKDKKSL-DRVESLLKTYGLWDF---RSMYPK-ELSGGMRQRVAL 139
Cdd:PRK14247 78 ielrrrVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELqERVRWALEKAQLWDEvkdRLDAPAgKLSGGQQQRLCI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTRLLVcDDVYSIIKNEnKSTILVTHDIGEA 192
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD-MTIVLVTHFPQQA 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-187 |
2.26e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:PRK13657 335 VEFDDVSFSY---DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQkDNLLEWRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:PRK13657 412 AVVFQ-DAGLFNRSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTH 187
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-190 |
2.30e-23 |
|
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: 96.29 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKS-TILNILtNLLkPtSGDIKITGNIgyMFQKD 79
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLL-P-DPAAHPSGSI--LFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLL-----EWRNI------MdnI------------TIGLEI-------QGKKDKKSLDRVESLLKTYGLWDFRSM---YP 126
Cdd:COG4172 77 DLLglserELRRIrgnriaM--IfqepmtslnplhTIGKQIaevlrlhRGLSGAAARARALELLERVGIPDPERRldaYP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 127 KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR-----LLVcddvySIIKNENKSTILVTHDIG 190
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQaqildLLK-----DLQRELGMALLLITHDLG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-192 |
3.07e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------- 71
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarha 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ---IGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK13537 79 rqrVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKnENKSTILVTHDIGEA 192
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEA 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-189 |
4.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.37 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI-------------- 66
Cdd:PRK13636 1 MEDYILKVEELNYNY--SDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 -KITGNIGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLS 144
Cdd:PRK13636 78 mKLRESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 145 VNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-192 |
5.01e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------NIGYMFQKDNLLEWRNI 87
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepadrDIAMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITIGLEIQGkKDKKSLD-RVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:PRK11650 94 RENMAYGLKIRG-MPKAEIEeRVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ 172
|
170 180
....*....|....*....|....*.
gi 489530649 167 VCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11650 173 MRLEIQRLHRRLKTTSLYVTHDQVEA 198
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-169 |
6.89e-23 |
|
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: 91.34 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNdNIVEVKNINMNF--YTKEG-ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNIL--TNLlkPTSGDIKITgnigYM 75
Cdd:COG4778 1 MT-TLLEVENLSKTFtlHLQGGkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVR----HD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 FQKDNL--LEWRNIMD--NITIG--------------LEI-------QGKKDKKSLDRVESLLKTYG----LWDfrsMYP 126
Cdd:COG4778 74 GGWVDLaqASPREILAlrRRTIGyvsqflrviprvsaLDVvaeplleRGVDREEARARARELLARLNlperLWD---LPP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 127 KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCD 169
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-189 |
7.44e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.41 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILtNLLKPTSGDIKITGNIGY----------- 74
Cdd:PRK14258 8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFfnqniyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 ----------MFQKDNLLEwRNIMDNITIGLEIQGKKDKKSLDR-VESLLKTYGLWD-FRSMYPK---ELSGGMRQRVAL 139
Cdd:PRK14258 83 lnrlrrqvsmVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDiVESALKDADLWDeIKHKIHKsalDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-189 |
7.51e-23 |
|
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: 91.70 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 31 NLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-IGYMFQK---DNLLEWRNIMDNITIGLEIQgkkdkkSL 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYikaDYEGTVRDLLSSITKDFYTH------PY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 107 DRVESL--LKTYGLWDFRSmypKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTIL 184
Cdd:cd03237 95 FKTEIAkpLQIEQILDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFV 171
|
....*
gi 489530649 185 VTHDI 189
Cdd:cd03237 172 VEHDI 176
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-189 |
9.14e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMnFYTKEGELEV--LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--------TGN---- 71
Cdd:PRK13641 3 IKFENVDY-IYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpeTGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -----IGYMFQ-KDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLS 144
Cdd:PRK13641 82 klrkkVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 145 VNPDILLLDEPFSALDYQTRLlvcdDVYSIIKNENK---STILVTHDI 189
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRK----EMMQLFKDYQKaghTVILVTHNM 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-167 |
1.51e-22 |
|
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: 90.41 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLL---KPTSGDIKITG----------NIGYMFQKDNLLEWRNIMDN 90
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGLEIQG---KKDKKSLDRVE-SLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:cd03234 102 LTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
.
gi 489530649 167 V 167
Cdd:cd03234 182 L 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-164 |
2.03e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--TGNIGYMFQK-D 79
Cdd:COG0488 313 KKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHqE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNITigleiQGKKDKKSLDrVESLLKTYGLWDFRSMYP-KELSGGMRQRVALIRTLSVNPDILLLDEPFSA 158
Cdd:COG0488 389 ELDPDKTVLDELR-----DGAPGGTEQE-VRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
....*.
gi 489530649 159 LDYQTR 164
Cdd:COG0488 463 LDIETL 468
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-166 |
2.05e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 7 EVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKItgnigymFQKDnLLEW-- 84
Cdd:PRK13548 4 EARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL-------NGRP-LADWsp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 ------RNIM-------------DNITIGLEI--QGKKDKKSLdrVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTL 143
Cdd:PRK13548 72 aelarrRAVLpqhsslsfpftveEVVAMGRAPhgLSRAEDDAL--VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 144 ------SVNPDILLLDEPFSALD--YQTRLL 166
Cdd:PRK13548 150 aqlwepDGPPRWLLLDEPTSALDlaHQHHVL 180
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-192 |
2.07e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTIL---NILTNLLKPTSGDIKIT-------- 69
Cdd:PRK14243 4 LNGTETVLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTfhgknlya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 70 ---------GNIGYMFQKDNLLEwRNIMDNITIGLEIQGKKDkkSLDR-VESLLKTYGLWDFRSMYPKE----LSGGMRQ 135
Cdd:PRK14243 82 pdvdpvevrRRIGMVFQKPNPFP-KSIYDNIAYGARINGYKG--DMDElVERSLRQAALWDEVKDKLKQsglsLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489530649 136 RVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIikNENKSTILVTHDIGEA 192
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQA 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-160 |
2.65e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.55 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG----------NIGYMFQKD---------- 79
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRNamkpaltvae 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNitigleiqgkkdkkSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSAL 159
Cdd:PRK13539 93 NLEFWAAFLGG--------------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
.
gi 489530649 160 D 160
Cdd:PRK13539 159 D 159
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-192 |
8.30e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 8.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGelevLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLL---KPTSGDIKITGNI--------- 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTvqregrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 ---------GYMFQKDNLLEWRNIMDNITIGL---------------EIQGKKDKKSLDRVesllktyGLWDFRSMYPKE 128
Cdd:PRK09984 80 dirksrantGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfswftREQKQRALQALTRV-------GMVHFAHQRVST 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 129 LSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYA 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-189 |
8.63e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------ 71
Cdd:PRK13652 2 HLIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQK-DNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK13652 79 fVGLVFQNpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQL 198
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-189 |
2.07e-21 |
|
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: 88.32 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYM--------FQKDNLLEWRN 86
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrkqrraFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNI----TIGlEIQGK--------KDKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:TIGR02769 97 SPSAVnprmTVR-QIIGEplrhltslDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 489530649 154 EPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDL 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-190 |
2.10e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.40 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP---TSGDIKITGN------ 71
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGReilnlp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -----------IGYMFQK--DNLLEWRNIMDNITIGLEIQGKKDK--------KSLDRV---ESLLKTyglwdfrSMYPK 127
Cdd:PRK09473 88 ekelnklraeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKaeafeesvRMLDAVkmpEARKRM-------KMYPH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 128 ELSGGMRQRVALIRTLSVNPDILLLDEPFSALDY----QTRLLVCDdvysiIKNE-NKSTILVTHDIG 190
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNE-----LKREfNTAIIMITHDLG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-160 |
2.17e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.03 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQKDNLLEWRNIMD 89
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 90 NITIGLEIqgKKD---KKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PRK10895 98 NLMAVLQI--RDDlsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-188 |
2.85e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------------IGYMFQKDNLLEW 84
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqidaiklrkeVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNITIGLEIQGKKDKKSLDR-VESLLKTYGLW----DFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSAL 159
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180
....*....|....*....|....*....
gi 489530649 160 DYQTRLLVcDDVYSIIKNEnKSTILVTHD 188
Cdd:PRK14246 185 DIVNSQAI-EKLITELKNE-IAIVIVSHN 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-187 |
2.93e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.45 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKE----GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP--TSGDIKITGN-------- 71
Cdd:cd03213 2 VTLSFRNLTVTVKSspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 --IGYMFQKDNLLEWRNIMDNITIGLEIQGkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDI 149
Cdd:cd03213 82 kiIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSL 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 150 LLLDEPFSALDYQTRLlvcdDVYSIIK---NENKSTILVTH 187
Cdd:cd03213 133 LFLDEPTSGLDSSSAL----QVMSLLRrlaDTGRTIICSIH 169
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-195 |
3.33e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.90 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNinMNFytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGYM------ 75
Cdd:PRK11831 5 ANLVDMRG--VSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeNIPAMsrsrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 ---------FQKDNLLEWRNIMDNITIGLEIQGKKDKKSL-DRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSV 145
Cdd:PRK11831 81 tvrkrmsmlFQSGALFTDMNVFDNVAYPLREHTQLPAPLLhSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 146 NPDILLLDEPFSALDYQTR-LLVcddvySIIKNENKS----TILVTHDIGEARCI 195
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMgVLV-----KLISELNSAlgvtCVVVSHDVPEVLSI 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-187 |
4.63e-21 |
|
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: 85.44 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKdnllewrNIMDNI 91
Cdd:cd03247 5 NVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-------ALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIgleiqgkkdkksLDRVESLLKTyglwDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDV 171
Cdd:cd03247 78 SV------------LNQRPYLFDT----TLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170
....*....|....*.
gi 489530649 172 YSIIKneNKSTILVTH 187
Cdd:cd03247 142 FEVLK--DKTLIWITH 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-160 |
4.83e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGEL-------EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPTSGDIKITGNIGYMFQ 77
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 78 KDNLLEWR------------------NIMDNITIGLEIQGKK--DKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQR 136
Cdd:PRK15134 354 RRQLLPVRhriqvvfqdpnsslnprlNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQR 433
|
170 180
....*....|....*....|....
gi 489530649 137 VALIRTLSVNPDILLLDEPFSALD 160
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLD 457
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-187 |
4.91e-21 |
|
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: 89.78 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NI 72
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaslrrQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 73 GYMFQKDNLLEwRNIMDNITIGleiqgKKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIR 141
Cdd:TIGR02203 409 ALVSQDVVLFN-DTIANNIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIAR 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIknENKSTILVTH 187
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAH 526
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-188 |
5.78e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.42 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--TGNIGYMFQkdnlle 83
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 84 wrnimdnitigleiqgkkdkksldrvesllktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT 163
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180
....*....|....*....|....*
gi 489530649 164 RLLvcddVYSIIKNENKSTILVTHD 188
Cdd:cd03221 106 IEA----LEEALKEYPGTVILVSHD 126
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-192 |
6.43e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 10 NINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG-----DIKITGN------------- 71
Cdd:PRK14271 26 NLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRsifnyrdvlefrr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQKDNLLEwRNIMDNITIGLEIQGKKDKKSLDRV-ESLLKTYGLWDF----RSMYPKELSGGMRQRVALIRTLSV 145
Cdd:PRK14271 102 rVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVaQARLTEVGLWDAvkdrLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 146 NPDILLLDEPFSALDYQTRLLVCDDVYSIIknENKSTILVTHDIGEA 192
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQA 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-192 |
8.27e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNIMDNI 91
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDV 171
Cdd:PRK13536 136 LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL 215
|
170 180
....*....|....*....|.
gi 489530649 172 YSIIKnENKSTILVTHDIGEA 192
Cdd:PRK13536 216 RSLLA-RGKTILLTTHFMEEA 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-193 |
1.16e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEgELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKItgNIGYMFQKDNLLEWR 85
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 ---------------NIMDNITIGLE-------------------------------------------------IQGKK 101
Cdd:PTZ00265 460 skigvvsqdpllfsnSIKNNIKYSLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnelIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 102 DKKSLD--RVESLLKTYGLWDFRSMYP-----------KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVC 168
Cdd:PTZ00265 540 NYQTIKdsEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|....*
gi 489530649 169 DDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRLSTIR 644
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-160 |
1.88e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.24 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 11 INMNFYTKEGELEVlkDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-----------------NIG 73
Cdd:PRK11144 2 LELNFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgiclppekrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 74 YMFQKDNLLEWRNIMDNITIGLeiqGKKDKKSLDRVESLLktyGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGM---AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
....*..
gi 489530649 154 EPFSALD 160
Cdd:PRK11144 154 EPLASLD 160
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-192 |
2.05e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYT-KEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------ 71
Cdd:COG1101 1 MLELKNLSKTFNPgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQ------------KDNLL--EWRNIMDNITIGLeiqGKKDKKSL-DRVESL-------LKT-YGLwdfrsmypk 127
Cdd:COG1101 81 yIGRVFQdpmmgtapsmtiEENLAlaYRRGKRRGLRRGL---TKKRRELFrELLATLglglenrLDTkVGL--------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 128 eLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:COG1101 149 -LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-192 |
2.80e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMF------QKDNLL-------EWRN 86
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssrqlaRRLALLpqhhltpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIG----LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD-- 160
Cdd:PRK11231 93 VRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDin 172
|
170 180 190
....*....|....*....|....*....|..
gi 489530649 161 YQTRLLvcdDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK11231 173 HQVELM---RLMRELNTQGKTVVTVLHDLNQA 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-194 |
3.79e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.75 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGnigymfqkDNLLEWR 85
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG--------LDVATTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 N--------IM--DN-ITIGLEI------------QGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT 142
Cdd:COG4604 70 SrelakrlaILrqENhINSRLTVrelvafgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 143 LSVNPDILLLDEPFSALDYQ-----TRLL--VCDDvysiiknENKSTILVTHDIGEARC 194
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKhsvqmMKLLrrLADE-------LGKTVVIVLHDINFASC 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-160 |
4.43e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNI 87
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489530649 88 MDNITIGLEIQGKKDKKsldrVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
26-193 |
5.57e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.50 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 26 KDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI---TGNIGYMFQ----KDNLL---EWRNIMDNITIGL 95
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQlseaERRRLmrtEWGFVHQNPRDGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 EIQGKKDKKSLDRVESL-LKTYGlwDFRSM-----------------YPKELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:TIGR02323 100 RMRVSAGANIGERLMAIgARHYG--NIRATaqdwleeveidptriddLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 158 ALD--YQTRLLvcDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:TIGR02323 178 GLDvsVQARLL--DLLRGLVRDLGLAVIIVTHDLGVAR 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-190 |
1.04e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.50 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIK-----ITGNIGYM 75
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 ---------FQK----------DNLL--EWRNIMDNITIGL---EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSG 131
Cdd:PRK11300 77 iarmgvvrtFQHvrlfremtviENLLvaQHQQLKTGLFSGLlktPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489530649 132 GMRQRVALIRTLSVNPDILLLDEPFSALDYQ-TRLLvcDDVYSIIKNE-NKSTILVTHDIG 190
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKEL--DELIAELRNEhNVTVLLIEHDMK 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-193 |
1.13e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.44 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMF--------QKDNLL--EW----R 85
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalseaERRRLLrtEWgfvhQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMD----------NITIGLEIQGKK------DKKS--LDRVEslLKTYGLWDFrsmyPKELSGGMRQRVALIRTLSVNP 147
Cdd:PRK11701 97 HPRDglrmqvsaggNIGERLMAVGARhygdirATAGdwLERVE--IDAARIDDL----PTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 148 DILLLDEPFSALD--YQTRLLvcDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:PRK11701 171 RLVFMDEPTGGLDvsVQARLL--DLLRGLVRELGLAVVIVTHDLAVAR 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-189 |
1.86e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGE---------LEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGY 74
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 75 MFQKdnllEWRNIMDNI---------------TIG------LEIQGKKDKKS--LDRVESLLKTYGLW-DFRSMYPKELS 130
Cdd:PRK15079 88 MKDD----EWRAVRSDIqmifqdplaslnprmTIGeiiaepLRTYHPKLSRQevKDRVKAMMLKVGLLpNLINRYPHEFS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-189 |
1.95e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLK--------DVNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPTSGDIKITG-------------NIGYMFQKD 79
Cdd:PRK11174 354 DLEILSpdgktlagPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldpeswrkHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEwRNIMDNITIGleiqgkKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK11174 433 QLPH-GTLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 149 ILLLDEPFSALDYQTRLLVCDDVYSIIKneNKSTILVTHDI 189
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQL 544
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-162 |
2.41e-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: 81.77 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNiGYMFQKDNLLE---WRNIMDNITIGL- 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARgllYLGHAPGIKTTLs 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 ---EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQ 162
Cdd:cd03231 90 vleNLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-199 |
2.60e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.92 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKEG-----ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKIT------GN 71
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGYMFQK--------DNLLEWR----NIMD-NITIGLEIQGKKDKKsldRVESLLKTYGLW-DFRSMYPKELSGGMRQRV 137
Cdd:PRK15112 82 YSYRSQRirmifqdpSTSLNPRqrisQILDfPLRLNTDLEPEQREK---QIIETLRQVGLLpDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489530649 138 ALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEARCIKVQL 199
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQV 220
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-197 |
2.91e-19 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 82.56 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 9 KNINMNFYTkegelevLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNLLEWRNIM 88
Cdd:PRK13546 31 KHKNKTFFA-------LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDyQTRLLVC 168
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-QTFAQKC 182
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 169 DDVYSIIKNENKSTILVTHDIGEAR--CIKV 197
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRqfCTKI 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-160 |
3.57e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------------IGYMFQK 78
Cdd:PRK11308 21 LFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkadpeaqkllrqkIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 --DNLLEWRNIMDNITIGLEIQ---GKKDKKslDRVESLLKTYGLW-DFRSMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:PRK11308 101 pyGSLNPRKKVGQILEEPLLINtslSAAERR--EKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 489530649 153 DEPFSALD 160
Cdd:PRK11308 179 DEPVSALD 186
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-195 |
3.57e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.32 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQK 78
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEWrnimdniTIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNP 147
Cdd:TIGR01842 401 VELFPG-------TVAENIARFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDP 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 148 DILLLDEPFSALDYQTRLLVCDDVYSiIKNENKSTILVTHDIGEARCI 195
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRPSLLGCV 520
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-187 |
4.45e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG-----DIKITGN------------IGYMFQ--KDNLLEwR 85
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTskqkeikpvrkkVGVVFQfpESQLFE-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGLEIQGKKDKKSLDRVESLLKTYGLW-DFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180
....*....|....*....|...
gi 489530649 165 LLVCdDVYSIIKNENKSTILVTH 187
Cdd:PRK13643 181 IEMM-QLFESIHQSGQTVVLVTH 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-189 |
4.68e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.83 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEG-ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIK----------------- 67
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 68 --------------------ITGNIGYMFQ--KDNLLEwRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSM 124
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 125 YPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTrllvCDDVYSIIKN---ENKSTILVTHDI 189
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG----VKEILEIFDNlnkQGKTIILVTHDL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-189 |
6.72e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEG-------ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------- 70
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtls 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ---------NIGYMFQKDNL-LEWR-----NIMDNITIGLEIQGKKDKKsldRVESLLKTYGL-----WdfrsMYPKELS 130
Cdd:PRK10261 393 pgklqalrrDIQFIFQDPYAsLDPRqtvgdSIMEPLRVHGLLPGKAAAA---RVAWLLERVGLlpehaW----RYPHEFS 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-190 |
9.86e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI--------------- 66
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 -----------KITG-NIGYMFQKdnllEWRNIMDNITIGLEI-------QGKKDKKSLDRVESLLKTYGLWDFRSM--- 124
Cdd:PRK10261 89 elseqsaaqmrHVRGaDMAMIFQE----PMTSLNPVFTVGEQIaesirlhQGASREEAMVEAKRMLDQVRIPEAQTIlsr 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 125 YPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIG 190
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-189 |
1.05e-18 |
|
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: 81.44 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQkdnlLEW---RNIMDNITIGLeiqgk 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ----FSWimpGTIKENIIFGV----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 101 kdkkSLD--RVESLLKTYGLWDFRSMYPKE-----------LSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:cd03291 123 ----SYDeyRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180
....*....|....*....|..
gi 489530649 168 CDDVYSIIKnENKSTILVTHDI 189
Cdd:cd03291 199 FESCVCKLM-ANKTRILVTSKM 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-186 |
1.45e-18 |
|
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: 83.04 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNLLEwRNIMDNITIGLeiqgkkdk 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMP-GTIKDNIIFGL-------- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 104 kSLD--RVESLLKTYGLWDFRSMYPKE-----------LSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDD 170
Cdd:TIGR01271 512 -SYDeyRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
170
....*....|....*.
gi 489530649 171 VYSIIKNeNKSTILVT 186
Cdd:TIGR01271 591 CLCKLMS-NKTRILVT 605
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-189 |
1.87e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.55 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQK---------DNLLewRNIMDNITigleiqgkkd 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYikpdydgtvEDLL--RSITDDLG---------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 103 kKSLDRVEsLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKST 182
Cdd:PRK13409 430 -SSYYKSE-IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATA 507
|
....*..
gi 489530649 183 ILVTHDI 189
Cdd:PRK13409 508 LVVDHDI 514
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-189 |
2.09e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 18 KEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI--------KITGNIGYMFQKDNLLEWRnimD 89
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQRKAFRRDIQMVFQ---D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 NI-------TIGlEIQGK--------KDKKSLDRVESLLKTYGLWD-FRSMYPKELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:PRK10419 98 SIsavnprkTVR-EIIREplrhllslDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 489530649 154 EPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
25-190 |
2.41e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------IGYMFQKDNLlEWRN---IMDNI 91
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEEV-DWSFpvlVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIG-------LEIQGKKDKKsldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:PRK15056 102 MMGryghmgwLRRAKKRDRQ---IVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180
....*....|....*....|....*.
gi 489530649 165 LLVCdDVYSIIKNENKSTILVTHDIG 190
Cdd:PRK15056 179 ARII-SLLRELRDEGKTMLVSTHNLG 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-163 |
3.32e-18 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.52 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--TGNIGYMFQ-KD 79
Cdd:TIGR03719 320 DKVIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQsRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNITIGLEIQ--GKKDKKSldrvesllKTY-GLWDFR----SMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:TIGR03719 396 ALDPNKTVWEEISGGLDIIklGKREIPS--------RAYvGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170
....*....|.
gi 489530649 153 DEPFSALDYQT 163
Cdd:TIGR03719 468 DEPTNDLDVET 478
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-188 |
4.00e-18 |
|
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: 81.33 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKDNLLEW---RNI 87
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGtiaENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 --MDNITIgleiqgkkdkkslDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:COG4618 427 arFGDADP-------------EKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 155 PFSALDYQ-----TRLLvcddvySIIKNENKSTILVTHD 188
Cdd:COG4618 494 PNSNLDDEgeaalAAAI------RALKARGATVVVITHR 526
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
12-187 |
4.36e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEG---ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG----------------DIK-ITGN 71
Cdd:PRK13649 7 NVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlitstsknkDIKqIRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGYMFQ-KDNLLEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK13649 87 VGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489530649 150 LLLDEPFSALDYQTRllvcDDVYSIIKNENKS--TI-LVTH 187
Cdd:PRK13649 167 LVLDEPTAGLDPKGR----KELMTLFKKLHQSgmTIvLVTH 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-189 |
4.37e-18 |
|
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: 81.37 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQkdnllewrnimdnitiglEIQGKKDkkslDRVES 111
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ------------------YISPDYD----GTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 112 LLKTYGLWDFRSMY-------P-----------KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYS 173
Cdd:COG1245 421 FLRSANTDDFGSSYykteiikPlgleklldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170
....*....|....*.
gi 489530649 174 IIKNENKSTILVTHDI 189
Cdd:COG1245 501 FAENRGKTAMVVDHDI 516
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-191 |
1.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQK-DNLLEWRNIMD 89
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 NITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCD 169
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180
....*....|....*....|..
gi 489530649 170 DVYSiIKNENKSTILVTHDIGE 191
Cdd:PRK13644 178 RIKK-LHEKGKTIVYITHNLEE 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-187 |
1.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFYTK-EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI-----------T 69
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 70 GNIGYMFQK--DNLLEWR-----------------NIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSMYPKEL 129
Cdd:PRK13631 98 ELITNPYSKkiKNFKELRrrvsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 130 SGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSiIKNENKSTILVTH 187
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITH 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-194 |
2.62e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.40 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 27 DVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSG------------DIKITGNIGYMFQKDNLLEWRNIMDNitig 94
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdagDIATRRRVGYMSQAFSLYGELTVRQN---- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 95 LEIQGK----KDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQR----VALIRtlsvNPDILLLDEPFSALDYQTRll 166
Cdd:NF033858 360 LELHARlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAVIH----KPELLILDEPTSGVDPVAR-- 433
|
170 180 190
....*....|....*....|....*....|...
gi 489530649 167 vcDDVYSIIKN---ENKSTILV-THDIGEA-RC 194
Cdd:NF033858 434 --DMFWRLLIElsrEDGVTIFIsTHFMNEAeRC 464
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-191 |
4.13e-17 |
|
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: 75.16 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMF-----QKDNLLEWRN 86
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpvtrrsprdaiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIGLeiqgkkdkksldrvesllktyglwdfrsmypkELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRll 166
Cdd:cd03215 95 VAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK-- 140
|
170 180
....*....|....*....|....*...
gi 489530649 167 vcDDVYSII---KNENKSTILVTHDIGE 191
Cdd:cd03215 141 --AEIYRLIrelADAGKAVLLISSELDE 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-160 |
4.90e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEGEleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGnigymfqkDNLLEWR 85
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--------HDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 --NIMDNI------------TIGLEIQ-GKKDKKSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVAL 139
Cdd:PRK11176 412 laSLRNQValvsqnvhlfndTIANNIAyARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAI 491
|
170 180
....*....|....*....|.
gi 489530649 140 IRTLSVNPDILLLDEPFSALD 160
Cdd:PRK11176 492 ARALLRDSPILILDEATSALD 512
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-189 |
6.50e-17 |
|
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: 78.06 E-value: 6.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYM-----FQKDNLLEwrn 86
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVpqqawIQNDSLRE--- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 imdNITIGLEIQGKKDKKSLDRVESL--LKTYGLWDFRSMYPK--ELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQ 162
Cdd:TIGR00957 718 ---NILFGKALNEKYYQQVLEACALLpdLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190
....*....|....*....|....*....|
gi 489530649 163 TRLLVCDDVY---SIIKneNKSTILVTHDI 189
Cdd:TIGR00957 795 VGKHIFEHVIgpeGVLK--NKTRILVTHGI 822
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-163 |
1.23e-16 |
|
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: 77.17 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQkDNLLEwr 85
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQ-DTVLF-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 nimdNITIGLEIQ-GKKDKkSLDRVESLLKTYGLWDFRSMYPK-----------ELSGGMRQRVALIRTLSVNPDILLLD 153
Cdd:COG5265 445 ----NDTIAYNIAyGRPDA-SEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFD 519
|
170
....*....|
gi 489530649 154 EPFSALDYQT 163
Cdd:COG5265 520 EATSALDSRT 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-192 |
1.48e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.36 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 28 VNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNIMDNITIGL 95
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 EIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDdvySII 175
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD---LLL 1105
|
170
....*....|....*...
gi 489530649 176 KNENKSTILV-THDIGEA 192
Cdd:TIGR01257 1106 KYRSGRTIIMsTHHMDEA 1123
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-187 |
1.86e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNigymfqkdNLLEW-----RN 86
Cdd:PRK11160 343 NVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ--------PIADYseaalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IM---------------DNITIGL-EIQGKKDKKSLDRV--ESLLKTY-GLwdfrSMYPKE----LSGGMRQRVALIRTL 143
Cdd:PRK11160 415 AIsvvsqrvhlfsatlrDNLLLAApNASDEALIEVLQQVglEKLLEDDkGL----NAWLGEggrqLSGGEQRRLGIARAL 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489530649 144 SVNPDILLLDEPFSALDYQT-----RLL--VCddvysiiknENKSTILVTH 187
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETerqilELLaeHA---------QNKTVLMITH 532
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-194 |
2.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.51 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMF-QKDNLleWRNI 87
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkefarRIGVVFgQRSQL--WWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 --MDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDyqtrL 165
Cdd:COG4586 112 paIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD----V 187
|
170 180 190
....*....|....*....|....*....|....*
gi 489530649 166 LVCDDVYSIIKNENKS---TILVT-HDIG--EARC 194
Cdd:COG4586 188 VSKEAIREFLKEYNRErgtTILLTsHDMDdiEALC 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-192 |
2.44e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLK--PTSGDIKItgnigymfQKDNLLEWRNIMDNITIgle 96
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV--------PDNQFGREASLIDAIGR--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 97 iqgKKDKKslDRVEsLLKTYGLWD----FRSmyPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVY 172
Cdd:COG2401 109 ---KGDFK--DAVE-LLNAVGLSDavlwLRR--FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180
....*....|....*....|..
gi 489530649 173 SIIKNENKSTILVTH--DIGEA 192
Cdd:COG2401 181 KLARRAGITLVVATHhyDVIDD 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-189 |
2.60e-16 |
|
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: 76.36 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIkitgnigymfqkDNLLEWRNIMD-----------------NITIG 94
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY------------DEEPSWDEVLKrfrgtelqdyfkklangEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 95 LEIQ----------GK--------KDKKSLDRVESLLKTYGLWDfRSMypKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:COG1245 164 HKPQyvdlipkvfkGTvrellekvDERGKLDELAEKLGLENILD-RDI--SELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 489530649 157 SALDYQTRLlvcdDVYSIIK---NENKSTILVTHDI 189
Cdd:COG1245 241 SYLDIYQRL----NVARLIRelaEEGKYVLVVEHDL 272
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-195 |
3.16e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------- 70
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ----NIGYMFQKDNLLEWRNIMDNITIGLEIQGK-------KDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVAL 139
Cdd:PRK09700 77 aaqlGIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489530649 140 IRTLSVNPDILLLDEPFSALDYQTrllvCDDVYSII---KNENKSTILVTHDIGEARCI 195
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKE----VDYLFLIMnqlRKEGTAIVYISHKLAEIRRI 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-188 |
3.66e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.74 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNI--GYMFQKDNLLEWRNIMDNITIGL-EIQG 99
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIkvGYLPQEPQLDPTKTVRENVEEGVaEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 100 KKDK-------------------KSLDRVESLLKTYGLWDFRSMY----------PKE-----LSGGMRQRVALIRTLSV 145
Cdd:TIGR03719 99 ALDRfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQLeiamdalrcpPWDadvtkLSGGERRRVALCRLLLS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489530649 146 NPDILLLDEPFSALDYQT-----RLLvcddvysiiKNENKSTILVTHD 188
Cdd:TIGR03719 179 KPDMLLLDEPTNHLDAESvawleRHL---------QEYPGTVVAVTHD 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-189 |
4.63e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKS-TILNIL------------------TNLLKPTSGD 65
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMglidypgrvmaeklefngQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 66 I-KITG-NIGYMFQkdnllewrNIMDNI----TIGLEI-------QGKKDKKSLDRVESLLKTYGLWDFRS---MYPKEL 129
Cdd:PRK11022 83 RrNLVGaEVAMIFQ--------DPMTSLnpcyTVGFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 130 SGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-189 |
7.23e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-IGYMFQKDNLLEW 84
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNITIGLEIQGKK--------------DKKSLDR--VESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPD 148
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQvvemgrtphrsrfdTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489530649 149 ILLLDEPFSALD--YQTRLLvcdDVYSIIKNENKSTILVTHDI 189
Cdd:PRK09536 160 VLLLDEPTASLDinHQVRTL---ELVRRLVDDGKTAVAAIHDL 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-187 |
7.82e-16 |
|
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: 72.53 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNfYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIgymfQKDNLLEW 84
Cdd:cd03244 3 IEFKNVSLR-YRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDI----SKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNI---------TI--GLEIQGKKDKKSLDRVeslLKTYGLWDFRSMYPKEL-----------SGGMRQRVALIRT 142
Cdd:cd03244 77 RSRISIIpqdpvlfsgTIrsNLDPFGEYSDEELWQA---LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 143 LSVNPDILLLDEPFSALDYQTRLLvcddVYSIIKNE--NKSTILVTH 187
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDAL----IQKTIREAfkDCTVLTIAH 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
10-187 |
8.83e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 10 NINmNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDnllEWR---- 85
Cdd:PRK10789 317 NIR-QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD---SWRsrla 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 -----------NIMDNITIGLEIQGKKDKKSLDRV----ESLLKtyglwdFRSMYPKE-------LSGGMRQRVALIRTL 143
Cdd:PRK10789 393 vvsqtpflfsdTVANNIALGRPDATQQEIEHVARLasvhDDILR------LPQGYDTEvgergvmLSGGQKQRISIARAL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489530649 144 SVNPDILLLDEPFSALDYQTRllvcddvYSIIKN-----ENKSTILVTH 187
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTE-------HQILHNlrqwgEGRTVIISAH 508
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-160 |
9.45e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP---TSGDIKITGNI----------GYMFQKDNL 81
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 LEWRNIMDNITIGLEIQGKKD---KKSLDRVESLLKTYGLWDFRSM------YPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLRMPRRvtkKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFC 190
|
....*...
gi 489530649 153 DEPFSALD 160
Cdd:TIGR00955 191 DEPTSGLD 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-188 |
1.16e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IV-EVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKItG---NIGYMFQ-KD 79
Cdd:PRK11147 318 IVfEMENVNYQIDGKQ----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GtklEVAYFDQhRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNITIG---LEIQGKkdkkslDR-VESLLKtyglwDF-----RSMYP-KELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK11147 393 ELDPEKTVMDNLAEGkqeVMVNGR------PRhVLGYLQ-----DFlfhpkRAMTPvKALSGGERNRLLLARLFLKPSNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489530649 150 LLLDEPFSALDYQT-RLLvcddvYSIIKNENKSTILVTHD 188
Cdd:PRK11147 462 LILDEPTNDLDVETlELL-----EELLDSYQGTVLLVSHD 496
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-187 |
1.46e-15 |
|
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: 71.40 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 14 NFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNL--LKPTSGDIkitgnigyMFQKDNLLEwRNIMDNI 91
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI--------LFKGEDITD-LPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIGL--------EIQGKKDKKSLDRVEsllktYGlwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT 163
Cdd:cd03217 76 RLGIflafqyppEIPGVKNADFLRYVN-----EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180
....*....|....*....|....
gi 489530649 164 RLLVCdDVYSIIKNENKSTILVTH 187
Cdd:cd03217 140 LRLVA-EVINKLREEGKSVLIITH 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-163 |
3.83e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.84 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--TGNIGYMFQ-KD 79
Cdd:PRK11819 322 DKVIEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQsRD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNITIGLEI--QGKKDKKSldrvesllKTY-GLWDFR----SMYPKELSGGMRQRVALIRTLSVNPDILLL 152
Cdd:PRK11819 398 ALDPNKTVWEEISGGLDIikVGNREIPS--------RAYvGRFNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLL 469
|
170
....*....|.
gi 489530649 153 DEPFSALDYQT 163
Cdd:PRK11819 470 DEPTNDLDVET 480
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-159 |
1.34e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------- 71
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahql 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYMFQKDNLLEWRNIMDNITIGLeiqgKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDIL 150
Cdd:PRK15439 87 gIYLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
....*....
gi 489530649 151 LLDEPFSAL 159
Cdd:PRK15439 163 ILDEPTASL 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-191 |
2.14e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNfytkegelEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN------------- 71
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdaira 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -IGYM---FQKDNLLEWRNIMDNITI---------GLeIQGKKDKKSLDR-VESL-LKTyglwdfRSMYPK--ELSGGMR 134
Cdd:COG1129 328 gIAYVpedRKGEGLVLDLSIRENITLasldrlsrgGL-LDRRRERALAEEyIKRLrIKT------PSPEQPvgNLSGGNQ 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 135 QRVALIRTLSVNPDILLLDEPFSALDYQTRllvcDDVYSIIK---NENKSTILVTHDIGE 191
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAK----AEIYRLIRelaAEGKAVIVISSELPE 456
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-189 |
2.14e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPtsgdikitgNIGymfQKDNLLEWRNIMD-----------------NITIG 94
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIP---------NLG---DYEEEPSWDEVLKrfrgtelqnyfkklyngEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 95 LEIQ----------GK--------KDKKSLDRVESLLKTYGLWDfRSMypKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PRK13409 164 HKPQyvdlipkvfkGKvrellkkvDERGKLDEVVERLGLENILD-RDI--SELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|....*
gi 489530649 157 SALDYQTRLLVCDdvysIIK--NENKSTILVTHDI 189
Cdd:PRK13409 241 SYLDIRQRLNVAR----LIRelAEGKYVLVVEHDL 271
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-168 |
2.29e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.04 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 9 KNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNllKPTSGdiKITGNIgymfqkdnLLEWRNIM 88
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAG--VITGEI--------LINGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DN--ITIGLEIQGKKDKKSLDRVESLLktyglwdFrSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:cd03232 75 KNfqRSTGYVEQQDVHSPNLTVREALR-------F-SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
..
gi 489530649 167 VC 168
Cdd:cd03232 147 IV 148
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-190 |
2.88e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKS----TILNILT---------------NLLKPTSG 64
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKdnwhvtadrfrwngiDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 65 D-IKITG-NIGYMFQkdnllEWRNIMD-NITIGLEI--------------QGKKDKKSldRVESLLKTYGLWDFRSM--- 124
Cdd:COG4170 82 ErRKIIGrEIAMIFQ-----EPSSCLDpSAKIGDQLieaipswtfkgkwwQRFKWRKK--RAIELLHRVGIKDHKDImns 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489530649 125 YPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT-----RLLvcddvYSIIKNENKSTILVTHDIG 190
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTqaqifRLL-----ARLNQLQGTSILLISHDLE 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-189 |
2.98e-14 |
|
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: 68.51 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 9 KNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTIL-----------------NILTNLLKPTSGDIKITGN 71
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemqtlegkvhwsNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGYMFQKDNLLEwRNIMDNITIGLEIQGKKDKKSLDRVeSLLKTYGLWDF--------RSMypkELSGGMRQRVALIRTL 143
Cdd:cd03290 81 VAYAAQKPWLLN-ATVEENITFGSPFNKQRYKAVTDAC-SLQPDIDLLPFgdqteigeRGI---NLSGGQRQRICVARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 144 SVNPDILLLDEPFSALD-YQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:cd03290 156 YQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-187 |
3.34e-14 |
|
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: 70.15 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNLLEWRN------------IMDN 90
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINylpqepyifsgsILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIG----LEIQGKKDKKSLDRVESLLKTY--GLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:TIGR01193 568 LLLGakenVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180
....*....|....*....|...
gi 489530649 165 LLVCDDVYSIiknENKSTILVTH 187
Cdd:TIGR01193 648 KKIVNNLLNL---QDKTIIFVAH 667
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-162 |
3.42e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 27 DVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN---------------IGYmfQ---KDNLLEWrnim 88
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdllyLGH--QpgiKTELTAL---- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 89 DNITIGLEIQGKKDKkslDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQ 162
Cdd:PRK13538 93 ENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-189 |
3.75e-14 |
|
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: 67.21 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIkitgnigymfqkdnllEWrnimDNITIGLEIQGKKdkksldrves 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------EW----DGITPVYKPQYID---------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 112 llktyglwdfrsmypkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:cd03222 72 -----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDL 132
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-160 |
4.12e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG--NIGYMFQKDNLLEWRNIMDNITIGL-EIQG 99
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgiKVGYLPQEPQLDPEKTVRENVEEGVaEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 100 KKDK----------------KSLD---RVESLLKTYGLWDFRSMY----------PKE-----LSGGMRQRVALIRTLSV 145
Cdd:PRK11819 101 ALDRfneiyaayaepdadfdALAAeqgELQEIIDAADAWDLDSQLeiamdalrcpPWDakvtkLSGGERRRVALCRLLLE 180
|
170
....*....|....*
gi 489530649 146 NPDILLLDEPFSALD 160
Cdd:PRK11819 181 KPDMLLLDEPTNHLD 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-155 |
4.21e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNLL--------EWRNIMDNI 91
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMreavaivpEGRRVFSRM 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489530649 92 TI-------GLEIQGKKDKKSLDRVESLLKTygLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:PRK11614 96 TVeenlamgGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-186 |
6.79e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMF--QKDNLlewrnimd 89
Cdd:COG4178 367 DLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFlpQRPYL-------- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 nitigleIQGK----------KDKKSLDRVESLLKTYGL------------WDfrsmypKELSGGMRQRVALIRTLSVNP 147
Cdd:COG4178 438 -------PLGTlreallypatAEAFSDAELREALEAVGLghlaerldeeadWD------QVLSLGEQQRLAFARLLLHKP 504
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 148 DILLLDEPFSALDYQTRllvcDDVYSIIKNENKSTILVT 186
Cdd:COG4178 505 DWLFLDEATSALDEENE----AALYQLLREELPGTTVIS 539
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-187 |
8.39e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.02 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMF--QKDNLlewrnimdniTIGleiqgkk 101
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFlpQRPYL----------PLG------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 102 dkkSLdRvESLLKTyglWDfrsmypKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRllvcDDVYSIIKNENKS 181
Cdd:cd03223 79 ---TL-R-EQLIYP---WD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE----DRLYQLLKELGIT 140
|
....*.
gi 489530649 182 TILVTH 187
Cdd:cd03223 141 VISVGH 146
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-160 |
1.12e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN----------IGYMFQKDNLLEWRNIMDNITI 93
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 94 GLEIQGKKDKKSldrVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT-LSVNPdILLLDEPFSALD 160
Cdd:PRK13543 106 LCGLHGRRAKQM---PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-192 |
1.50e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 35 GEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-------------IGYMFQKDNLLEWRNIMDNITIG------- 94
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGMTVRELVAIGrypwhga 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 95 LEIQGKKDKKsldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSI 174
Cdd:PRK10575 117 LGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170
....*....|....*...
gi 489530649 175 IKNENKSTILVTHDIGEA 192
Cdd:PRK10575 194 SQERGLTVIAVLHDINMA 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-189 |
1.90e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKEgELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPT-SGDIKITGNIGYMFQkdnlLEW 84
Cdd:PLN03232 615 ISIKNGYFSWDSKT-SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQ----VSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 ---RNIMDNITIGLEIQGKKDKKSLDrVESLLKTYGLWDFRSMYP-----KELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PLN03232 690 ifnATVRENILFGSDFESERYWRAID-VTALQHDLDLLPGRDLTEigergVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190
....*....|....*....|....*....|....*
gi 489530649 157 SALDYQTRLLVCDdvySIIKNE--NKSTILVTHDI 189
Cdd:PLN03232 769 SALDAHVAHQVFD---SCMKDElkGKTRVLVTNQL 800
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-191 |
2.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLL-----KPTSGDIKITGN-------------IGYMFQ-KDNL 81
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIPANlkkikevkrlrkeIGLVFQfPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 LEWRNIMDNITIGLEIQGKKDKKSLDRVESLLKTYGL-WDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 161 YQTRLLVCDDVYSIIKNENKSTILVTHDIGE 191
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQ 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-189 |
3.92e-13 |
|
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: 65.85 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 33 KEGEILTLLGPSGSGKSTILNILTNLLKPtsgdikitgNIGymfQKDNLLEWRNIMDNITiGLEIQ-------------- 98
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKP---------NLG---KFDDPPDWDEILDEFR-GSELQnyftkllegdvkvi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 99 --------------GK-----KDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSAL 159
Cdd:cd03236 91 vkpqyvdlipkavkGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 489530649 160 DYQTRLLVCDDVYSIIKnENKSTILVTHDI 189
Cdd:cd03236 171 DIKQRLNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-186 |
4.70e-13 |
|
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: 64.59 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 9 KNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLlkpTSGDIKITGNIGYmfqkdnllewrnim 88
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHY-------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 89 DNITIgLEIQGKKDKKSL-----DRVESLLKTYGLWDFR-----SMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSA 158
Cdd:cd03233 70 NGIPY-KEFAEKYPGEIIyvseeDVHFPTLTVRETLDFAlrckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 159 LDYQTRLlvcdDVYSIIK---NENKSTILVT 186
Cdd:cd03233 149 LDSSTAL----EILKCIRtmaDVLKTTTFVS 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-199 |
5.07e-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: 66.96 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 32 LKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKDNLLEWRNIMDNITIGLEIQG 99
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltnisdvhqNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 100 KKDKKsLDRVESL-LKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKnE 178
Cdd:TIGR01257 2042 VPAEE-IEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-E 2119
|
170 180
....*....|....*....|.
gi 489530649 179 NKSTILVTHDIGEARCIKVQL 199
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALCTRL 2140
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-160 |
6.90e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILN--------------ILTNLLKPTSGDIKITGnigYMFQKDNLLEWRN 86
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNalagriqgnnftgtILANNRKPTKQILKRTG---FVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNIT----IGLEIQGKKDKKSLdRVESLLKTYGLWDFRSM-----YPKELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:PLN03211 157 VRETLVfcslLRLPKSLTKQEKIL-VAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
...
gi 489530649 158 ALD 160
Cdd:PLN03211 236 GLD 238
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-188 |
8.35e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNigyMFQKDNLLEWRNIMDNI-------TIGLEI 97
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKLFSAVftdfhlfDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 QGKKDKKSLdrVESLLKTYG------LWDFRSMYPKeLSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDV 171
Cdd:PRK10522 416 EGKPANPAL--VEKWLERLKmahkleLEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVL 492
|
170
....*....|....*..
gi 489530649 172 YSIIKNENKSTILVTHD 188
Cdd:PRK10522 493 LPLLQEMGKTIFAISHD 509
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-194 |
8.40e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNInmnfyTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKS----TILNILTNLLKPTSGDIKITG----------- 70
Cdd:PRK10418 5 IELRNI-----ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGkpvapcalrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 NIGYMFQKD----NLLewRNIMDNITIGLEIQGKKDkkSLDRVESLLKTYGLWDFR---SMYPKELSGGMRQRVALIRTL 143
Cdd:PRK10418 80 KIATIMQNPrsafNPL--HTMHTHARETCLALGKPA--DDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 144 SVNPDILLLDEPFSALDY--QTRLLvcDDVYSIIKNENKSTILVTHDIG-EARC 194
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVvaQARIL--DLLESIVQKRALGMLLVTHDMGvVARL 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-192 |
1.08e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-------------NIGYMFQKdnllewRN 86
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQN------AT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIG-LEIQGKKDKKSL---------DRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PRK10253 92 TPGDITVQeLVARGRYPHQPLftrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 157 SALD--YQTRLLvcdDVYSIIKNENKSTI-LVTHDIGEA 192
Cdd:PRK10253 172 TWLDisHQIDLL---ELLSELNREKGYTLaAVLHDLNQA 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-160 |
2.15e-12 |
|
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: 64.11 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNfYTKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKpTSGDIKITgniGYMFQKDNLLEWR 85
Cdd:cd03289 3 MTVKDLTAK-YTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID---GVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 86 NIMDNITIGLEIQGKKDKKSLD-----RVESLLKT---YGLWDFRSMYPKE-----------LSGGMRQRVALIRTLSVN 146
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRKNLDpygkwSDEEIWKVaeeVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSK 156
|
170
....*....|....
gi 489530649 147 PDILLLDEPFSALD 160
Cdd:cd03289 157 AKILLLDEPSAHLD 170
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-196 |
2.18e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.91 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 15 FYTKEGELE-VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKDNLLEWRNIMDNITI 93
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 94 GLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDyQTRLLVCDDVYS 173
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD-QTFTKKCLDKMN 187
|
170 180
....*....|....*....|....*
gi 489530649 174 IIKNENKSTILVTHDIGEAR--CIK 196
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKsfCTK 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-186 |
3.07e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFYTKeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTS-GDIKITGNIGYMFQkdnlLEW 84
Cdd:PLN03130 615 ISIKNGYFSWDSK-AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQ----VSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 ---RNIMDNITIGLEIQGKK-----DKKSLDRVESLLKTYGLWDF--RSMypkELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:PLN03130 690 ifnATVRDNILFGSPFDPERyeraiDVTALQHDLDLLPGGDLTEIgeRGV---NISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190
....*....|....*....|....*....|....
gi 489530649 155 PFSALDYQTRLLVCDdvySIIKNE--NKSTILVT 186
Cdd:PLN03130 767 PLSALDAHVGRQVFD---KCIKDElrGKTRVLVT 797
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-189 |
5.71e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKS-TILNILTNLLKP----TSGDIKITG----- 70
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGesllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ------------NIGYMFQKD--NLLEWRNIMDNITIGLEIQGKKDKKS--------LDRVESLLKTYGLWDfrsmYPKE 128
Cdd:PRK15134 81 aseqtlrgvrgnKIAMIFQEPmvSLNPLHTLEKQLYEVLSLHRGMRREAargeilncLDRVGIRQAAKRLTD----YPHQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 129 LSGGMRQRVALIRTLSVNPDILLLDEPFSALD--YQTRLLvcdDVYSIIKNE-NKSTILVTHDI 189
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvsVQAQIL---QLLRELQQElNMGLLFITHNL 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-189 |
5.84e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG---------------NIGYMFQK-DNLLEWRN 86
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskrgllalrqQVATVFQDpEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMDNITIGLEIQGKKDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLL 166
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180
....*....|....*....|...
gi 489530649 167 VCDDVYSIIKNENKsTILVTHDI 189
Cdd:PRK13638 175 MIAIIRRIVAQGNH-VIISSHDI 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-189 |
5.91e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPT---------SGDI--------- 66
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtadrmrFDDIdllrlspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 67 --KITG-NIGYMFQK-DNLLE-----WRNIMDNITiGLEIQGKKDKK---SLDRVESLLKTYGLWDFRSM---YPKELSG 131
Cdd:PRK15093 83 rrKLVGhNVSMIFQEpQSCLDpservGRQLMQNIP-GWTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDAmrsFPYELTE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 132 GMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDI 189
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDL 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-187 |
1.09e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 12 NMNFYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMFQKD 79
Cdd:PRK10790 345 NVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 NLLEWRNIMDNITIGLEIqgkkdkkSLDRVESLLKTYGLWDF-RSMyPK-----------ELSGGMRQRVALIRTLSVNP 147
Cdd:PRK10790 424 PVVLADTFLANVTLGRDI-------SEEQVWQALETVQLAELaRSL-PDglytplgeqgnNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 148 DILLLDEPFSALDY---------------QTRLLVCDDVYSIIKNENksTILVTH 187
Cdd:PRK10790 496 QILILDEATANIDSgteqaiqqalaavreHTTLVVIAHRLSTIVEAD--TILVLH 548
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-160 |
1.24e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--IGYM------ 75
Cdd:PRK15064 318 NALEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENanIGYYaqdhay 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 76 -FQKD-NLLEW----RNIMDNI-----TIGLEIQGKKD-KKSldrvesllktyglwdfrsmyPKELSGGMRQRVALIRTL 143
Cdd:PRK15064 394 dFENDlTLFDWmsqwRQEGDDEqavrgTLGRLLFSQDDiKKS--------------------VKVLSGGEKGRMLFGKLM 453
|
170
....*....|....*..
gi 489530649 144 SVNPDILLLDEPFSALD 160
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMD 470
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-185 |
1.86e-11 |
|
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: 60.50 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNfYTKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGymfqKDNLLEW 84
Cdd:cd03369 7 IEVENLSVR-YAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDIS----TIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNITigleiqgkKDKKSLD-RVESLLKTYGLWD----FRSMYPKE----LSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:cd03369 81 RSSLTIIP--------QDPTLFSgTIRSNLDPFDEYSdeeiYGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190
....*....|....*....|....*....|.
gi 489530649 156 FSALDYQTRLLvcddVYSIIKNE-NKSTILV 185
Cdd:cd03369 153 TASIDYATDAL----IQKTIREEfTNSTILT 179
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-193 |
2.31e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTIL-----NILTNLLKPTSGDIKITGNIGYMF 76
Cdd:PTZ00265 1222 NDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVfknsgKILLDGVDICDYNLKDLRNLFSIV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 77 QKDNLLEWRNIMDNITIGLEIQGKKDKKSLDR-------VESLLKTYGlwDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:PTZ00265 1302 SQEPMLFNMSIYENIKFGKEDATREDVKRACKfaaidefIESLPNKYD--TNVGPYGKSLSGGQKQRIAIARALLREPKI 1379
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489530649 150 LLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEAR 193
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-187 |
3.53e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQKDNLLEWRNIMDN 90
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGleiQ-----GKKDKKSL-DRVESLLKTYGLwDFRSMYP-KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT 163
Cdd:PRK11288 100 LYLG---QlphkgGIVNRRLLnYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180
....*....|....*....|....*..
gi 489530649 164 rllvCDDVYSII---KNENKSTILVTH 187
Cdd:PRK11288 176 ----IEQLFRVIrelRAEGRVILYVSH 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-160 |
4.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 11 INMNFYTKEGELevLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NI-----GYMFQKDNLLEW 84
Cdd:PRK13540 5 IELDFDYHDQPL--LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqSIkkdlcTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNIMDNITIG----LEIQGKKDKKSLDRVESLLKTYGLWDFRSMYpkeLSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PRK13540 83 SGINPYLTLRenclYDIHFSPGAVGITELCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-188 |
6.20e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILtnllkptSGDIKI-TGNIGYM-------FQKD---NllEWRNIMDNITI 93
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLdDGRIIYEqdlivarLQQDpprN--VEGTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 94 GLEIQGKKDK------------------KSLDRVESLLKTYGLWDFRS--------------MYPKELSGGMRQRVALIR 141
Cdd:PRK11147 90 GIEEQAEYLKryhdishlvetdpseknlNELAKLQEQLDHHNLWQLENrinevlaqlgldpdAALSSLSGGWLRKAALGR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489530649 142 TLSVNPDILLLDEPFSALDYQTrllvCDDVYSIIKNENKSTILVTHD 188
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-191 |
8.40e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGYMFQKDNL-------------------- 81
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkEINALSTAQRLarglvylpedrqssglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 82 -LEWR--NIMDNiTIGLEIQGKKDKKSLDRVEsllktyglwdfRSMYPK---------ELSGGMRQRVALIRTLSVNPDI 149
Cdd:PRK15439 357 pLAWNvcALTHN-RRGFWIKPARENAVLERYR-----------RALNIKfnhaeqaarTLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489530649 150 LLLDEPFSALDYQTRllvcDDVYSIIKN---ENKSTILVTHDIGE 191
Cdd:PRK15439 425 LIVDEPTRGVDVSAR----NDIYQLIRSiaaQNVAVLFISSDLEE 465
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-195 |
2.28e-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: 59.07 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLK--PTSGDIKITGN----------- 71
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSplkasnirdte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 ---IGYMFQKDNLLEWRNIMDNITIGLEIQGKKDKKSLD----RVESLLKTYGLWDFRSMYP-KELSGGMRQRVALIRTL 143
Cdd:TIGR02633 77 ragIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489530649 144 SVNPDILLLDEPFSALDYQ-TRLLVcdDVYSIIKNENKSTILVTHDIGEARCI 195
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKeTEILL--DIIRDLKAHGVACVYISHKLNEVKAV 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-195 |
2.42e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPT---SGDIKITGN------ 71
Cdd:PRK13549 1 MMEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqasn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 --------IGYMFQKDNLLEWRNIMDNITIGLEIQ--GKKD-KKSLDRVESLLKTYGLwdfrSMYP----KELSGGMRQR 136
Cdd:PRK13549 76 irdteragIAIIHQELALVKELSVLENIFLGNEITpgGIMDyDAMYLRAQKLLAQLKL----DINPatpvGNLGLGQQQL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 137 VALIRTLSVNPDILLLDEPFSAL-DYQTRLLVcdDVYSIIKNENKSTILVTHDIGEARCI 195
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAI 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-191 |
2.98e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQ---KDNLLEWRNI 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNITI---------GLEIQGKKDKKSLDRVESL--LKTYGlwdfRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PRK10762 348 KENMSLtalryfsraGGSLKHADEQQAVSDFIRLfnIKTPS----MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 157 SALDYQTRllvcDDVYSII---KNENKSTILVTHDIGE 191
Cdd:PRK10762 424 RGVDVGAK----KEIYQLInqfKAEGLSIILVSSEMPE 457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-189 |
3.26e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 23 EVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIGYMFQKdnllEWrnIM-----DNITIGLEI 97
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ----AW--IMnatvrGNILFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 QGKKDKKSLdRVESL-----LKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVY 172
Cdd:PTZ00243 748 DAARLADAV-RVSQLeadlaQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF 826
|
170
....*....|....*..
gi 489530649 173 sIIKNENKSTILVTHDI 189
Cdd:PTZ00243 827 -LGALAGKTRVLATHQV 842
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-160 |
3.61e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 16 YTKEGElEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKpTSGDIKITgniGYMFQKDNLLEWRNIMDNITIGL 95
Cdd:TIGR01271 1227 YTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID---GVSWNSVTLQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 96 EIQGKKDKKSLDRVES--------LLKTYGLWDFRSMYPKE-----------LSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:TIGR01271 1302 FIFSGTFRKNLDPYEQwsdeeiwkVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
....
gi 489530649 157 SALD 160
Cdd:TIGR01271 1382 AHLD 1385
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-193 |
4.15e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 35 GEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITgnigymfqkdnllewrnimdnitigleiqgkkdkkSLDRVESLLK 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-----------------------------------DGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 115 TYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDV-----YSIIKNENKSTILVTHDI 189
Cdd:smart00382 47 DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEKNLTVILTTNDE 126
|
....
gi 489530649 190 GEAR 193
Cdd:smart00382 127 KDLG 130
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-187 |
4.76e-10 |
|
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: 58.22 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMnfYTKEGELeVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI--TGNIGYMFQKD 79
Cdd:TIGR00954 448 QDNGIKFENIPL--VTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 80 nLLEWRNIMDNITIGLEIQGKKDK--------KSLDRV--ESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDI 149
Cdd:TIGR00954 525 -YMTLGTLRDQIIYPDSSEDMKRRglsdkdleQILDNVqlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*...
gi 489530649 150 LLLDEPFSALDYQtrllVCDDVYSIIKNENKSTILVTH 187
Cdd:TIGR00954 604 AILDECTSAVSVD----VEGYMYRLCREFGITLFSVSH 637
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-187 |
6.16e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 1 MNDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTN--LLKPTSGDIKitgnigymFQK 78
Cdd:CHL00131 3 KNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDIL--------FKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 79 DNLLEW-------RNIMDNITIGLEIQG-------------KKDKKSLDRVESL---------LKTYGLWD-FRSMYPKE 128
Cdd:CHL00131 71 ESILDLepeerahLGIFLAFQYPIEIPGvsnadflrlaynsKRKFQGLPELDPLefleiinekLKLVGMDPsFLSRNVNE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 129 -LSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTrLLVCDDVYSIIKNENKSTILVTH 187
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDA-LKIIAEGINKLMTSENSIILITH 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-199 |
1.35e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILnILTNLLKPTSGDI------------KITGN 71
Cdd:NF000106 12 NAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRpwrf*twcanrrALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGY----MFQKDNLLEWRNIMDNITIGLEIQgKKDKKSldRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNP 147
Cdd:NF000106 87 IG*hrpvR*GRRESFSGRENLYMIGR*LDLS-RKDARA--RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489530649 148 DILLLDEPFSALDYQTRLLVCDDVYSIIKnENKSTILVTHDIGEARCIKVQL 199
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHEL 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-155 |
2.84e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQ---KdNLL 82
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQglgK-NLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 83 EWRNIMDNITI-----GleiQGKKDKKSldRVESLLKTYGLWDFRSMYPKELSGGMRQRV----ALIRtlsvNPDILLLD 153
Cdd:NF033858 91 PTLSVFENLDFfgrlfG---QDAAERRR--RIDELLRATGLAPFADRPAGKLSGGMKQKLglccALIH----DPDLLILD 161
|
..
gi 489530649 154 EP 155
Cdd:NF033858 162 EP 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-195 |
3.39e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 2 NDNIVEVKNINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILT--------NLL-----KPTSG---- 64
Cdd:PRK10938 257 NEPRIVLNNGVVSY----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysNDLtlfgrRRGSGetiw 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 65 DIKitGNIGYMfqKDNL-LEWR---NIMDNI------TIGL-----EIQGKKDKKSLDRVeSLLKTYGLWDFRSmypkeL 129
Cdd:PRK10938 333 DIK--KHIGYV--SSSLhLDYRvstSVRNVIlsgffdSIGIyqavsDRQQKLAQQWLDIL-GIDKRTADAPFHS-----L 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 130 SGGmRQRVALI-RTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSIIKNENKSTILVTHDIGEA-RCI 195
Cdd:PRK10938 403 SWG-QQRLALIvRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDApACI 469
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-168 |
7.73e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 4 NIVEVKNINMNFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKP---TSGDIKITG---------N 71
Cdd:TIGR00956 758 DIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGrpldssfqrS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 IGYMFQKDNLLEWRNIMDNITIGLEI-QGKK--DKKSLDRVESLLKTYGLWDFRSMY---PKE-LSGGMRQRVALIRTLS 144
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSAYLrQPKSvsKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELV 917
|
170 180
....*....|....*....|....*
gi 489530649 145 VNPDILL-LDEPFSALDYQTRLLVC 168
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSIC 942
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-164 |
1.03e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITgnigymFQKDNLL-----------EW-RNIMDNITIGLE 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ------FSHITRLsfeqlqklvsdEWqRNNTDMLSPGED 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489530649 97 IQGK-------KDKKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:PRK10938 97 DTGRttaeiiqDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-191 |
1.23e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQKDNLLEWRNIMDN 90
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkssqeagIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 91 ITIGLEIQ---GKKD-KKSLDRVESLLKTYGLwDFRSMYP-KELSGGMRQRVALIRTLSVNPDILLLDEPFSAL-DYQTR 164
Cdd:PRK10762 100 IFLGREFVnrfGRIDwKKMYAEADKLLARLNL-RFSSDKLvGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE 178
|
170 180 190
....*....|....*....|....*....|
gi 489530649 165 LLvcddvYSII---KNENKSTILVTHDIGE 191
Cdd:PRK10762 179 SL-----FRVIrelKSQGRGIVYISHRLKE 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-160 |
1.79e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 28 VNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPTSGDIKITGNigymfqkdNLLEWRN------------------IMD 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQ--------PLEAWSAaelarhraylsqqqtppfAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 90 ---NITIGLEIQGKKD--KKSLDRVESLLKtygLWDFRSMYPKELSGGMRQRVALIRT-LSVNPDI------LLLDEPFS 157
Cdd:PRK03695 86 vfqYLTLHQPDKTRTEavASALNEVAEALG---LDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMN 162
|
...
gi 489530649 158 ALD 160
Cdd:PRK03695 163 SLD 165
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-188 |
2.54e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 10 NINMNFytkeGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--IGYMFQKDNLLEWRNI 87
Cdd:PRK15064 6 NITMQF----GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNerLGKLRQDQFAFEEFTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 88 MDNItigleIQGKKD----KKSLDRVESLLK--------------TYGLWD----------------------FRSMypK 127
Cdd:PRK15064 82 LDTV-----IMGHTElwevKQERDRIYALPEmseedgmkvadlevKFAEMDgytaearagelllgvgipeeqhYGLM--S 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489530649 128 ELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQT-RLLvcDDVYsiikNENKST-ILVTHD 188
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTiRWL--EDVL----NERNSTmIIISHD 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-70 |
3.00e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 3.00e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 3 DNIVEVKNINmnfYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG 70
Cdd:COG3845 255 EVVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-160 |
3.05e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDI----KITGNIGYMFQKDNLLEWRN---IMDNITIGLE 96
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsaKVRMAVFSQHHVDGLDLSSNpllYMMRCFPGVP 603
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489530649 97 IQgkkdkksldRVESLLKTYGL---WDFRSMYpkELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PLN03073 604 EQ---------KLRAHLGSFGVtgnLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-160 |
3.13e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.76 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPTSGDIkitgnigyMFQKDNLLEWR------------------N 86
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEI--------LLNGRPLSDWSaaelarhraylsqqqsppF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 87 IMD---NITIGLEiQGKKDKKSLDRVESLLKTYGLWDF--RSMypKELSGGMRQRVALIRTL-----SVNPD--ILLLDE 154
Cdd:COG4138 83 AMPvfqYLALHQP-AGASSEAVEQLLAQLAEALGLEDKlsRPL--TQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDE 159
|
....*.
gi 489530649 155 PFSALD 160
Cdd:COG4138 160 PMNSLD 165
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-155 |
9.17e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 28 VNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------NIGYMF-----QKDNLLEWRNIMDN 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirsprdaiRAGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 91 ITI---------GLEIQGKKDKKSLDR-VESL-LKTYGlwdfRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:PRK11288 352 INIsarrhhlraGCLINNRWEAENADRfIRSLnIKTPS----REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-164 |
9.23e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 20 GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNI--GYMFQKDnlLEWRnimdnitiglei 97
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIklGYFAQHQ--LEFL------------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 98 qgKKDKKSLDRV--------ESLLKTY-GLWDFR----SMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:PRK10636 389 --RADESPLQHLarlapqelEQKLRDYlGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-187 |
1.52e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNINMNFYTKEgeleVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNllkptSGDIKITGNiGYMFQKDNLLEW 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-----REDYEVTGG-TVEFKGKDLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 -------RNIMDNITIGLEIQGKKDKKSLDRVESLLKTY------GLWDFRSM---------YPKEL---------SGGM 133
Cdd:PRK09580 71 spedragEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYrgqeplDRFDFQDLmeekiallkMPEDLltrsvnvgfSGGE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489530649 134 RQRVALIRTLSVNPDILLLDEPFSALDYQTRLLVCDDVYSiIKNENKSTILVTH 187
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTH 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-167 |
2.89e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 21 ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKI----TGNI-----GYMFQKDNLLEWRNIMDNI 91
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkncnINNIakpycTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 92 TIGLEIQgkkdkKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRLLV 167
Cdd:PRK13541 92 KFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-167 |
4.02e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.56 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 6 VEVKNINMNFytKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG-NIGYMFQKDNLLEW 84
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 85 RNI-MDNITIGLEIQGKKD---KKSLDRVESLLKTYGLWDFRSMYP-----------KELSGGMRQRVALIRTLSVNPDI 149
Cdd:TIGR00957 1363 TIIpQDPVLFSGSLRMNLDpfsQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKI 1442
|
170
....*....|....*...
gi 489530649 150 LLLDEPFSALDYQTRLLV 167
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLI 1460
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-154 |
5.35e-07 |
|
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: 49.03 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 28 VNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-IGymfqKDNLLEWRNIMDNI---------TIGLEi 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQpVT----ADNREAYRQLFSAVfsdfhlfdrLLGLD- 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489530649 98 qgkkDKKSLDRVESLLKTYGLWDfrsmypK-----------ELSGGMRQRVALIRTLSVNPDILLLDE 154
Cdd:COG4615 426 ----GEADPARARELLERLELDH------KvsvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-159 |
9.75e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN--------------IGYMFQKDNLLEWRNIMDN 90
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489530649 91 ITIG-LEIQGK--KDKKSLDRVESLLKTYGLwdfrSMYPKE----LSGGMRQRVALIRTLSVNPDILLLDEPFSAL 159
Cdd:PRK10982 94 MWLGrYPTKGMfvDQDKMYRDTKAIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-188 |
1.33e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 35 GEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGN-----------------IGYMFQKDNllEWRNIMDNITIGLE- 96
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalpqpaLEYVIDGDR--EYRQLEAQLHDANEr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 97 --------IQGKKDkkSLD------RVESLLKTYGLWDFRSMYP-KELSGGMRQRVALIRTLSVNPDILLLDEPFSALDY 161
Cdd:PRK10636 105 ndghaiatIHGKLD--AIDawtirsRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180 190
....*....|....*....|....*....|
gi 489530649 162 qtrllvcDDVYSI---IKNENKSTILVTHD 188
Cdd:PRK10636 183 -------DAVIWLekwLKSYQGTLILISHD 205
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-160 |
1.97e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.97e-06
10 20 30
....*....|....*....|....*....|....
gi 489530649 127 KELSGGMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-160 |
2.30e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 19 EGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNllKPT----SGDIKITG---------NI-GYMFQKD----N 80
Cdd:PLN03140 890 EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGfpkkqetfaRIsGYCEQNDihspQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 81 LLEWRNIMDNITIGLEIQGKKDKKS--LDRVESLLKTYGLWDFRSMYP--KELSGGMRQRVALIRTLSVNPDILLLDEPF 156
Cdd:PLN03140 968 VTVRESLIYSAFLRLPKEVSKEEKMmfVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....
gi 489530649 157 SALD 160
Cdd:PLN03140 1048 SGLD 1051
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-191 |
5.80e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMNFYTKegelevLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITG------------ 70
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprspldav 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 --NIGYMFQ--KDN-LLEWRNIMDNITI-------------GLeIQGKKDKKSLDRVESLL--KTYGLwdfrSMYPKELS 130
Cdd:PRK09700 337 kkGMAYITEsrRDNgFFPNFSIAQNMAIsrslkdggykgamGL-FHEVDEQRTAENQRELLalKCHSV----NQNITELS 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 131 GGMRQRVALIRTLSVNPDILLLDEPFSALDYQTRllvcDDVYSIIK---NENKSTILVTHDIGE 191
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK----AEIYKVMRqlaDDGKVILMVSSELPE 471
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-159 |
7.17e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 5 IVEVKNInmnfyTKE-GELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLkPT---SGDIKITGN--------- 71
Cdd:NF040905 1 ILEMRGI-----TKTfPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkdird 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 72 -----IGYMFQKDNLLEWRNIMDNITIGLEiQGKKD----KKSLDRVESLLKTYGLWDFRSMYPKELSGGMRQRVALIRT 142
Cdd:NF040905 75 sealgIVIIHQELALIPYLSIAENIFLGNE-RAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170
....*....|....*..
gi 489530649 143 LSVNPDILLLDEPFSAL 159
Cdd:NF040905 154 LSKDVKLLILDEPTAAL 170
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-74 |
1.51e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 11 INMNFyTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTsgdIKITGNIGY 74
Cdd:PLN03140 168 LGINL-AKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPS---LKVSGEITY 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-185 |
2.57e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITgniGYMFQKDNLLEWRNIMDNI---------TIG 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILID---GCDISKFGLMDLRKVLGIIpqapvlfsgTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 95 LEIQGKKDKKSLDRVESL----LK------TYGLWDFRSMYPKELSGGMRQRVALIRTLSVNPDILLLDEPFSALDYQTR 164
Cdd:PLN03130 1331 FNLDPFNEHNDADLWESLerahLKdvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
170 180
....*....|....*....|..
gi 489530649 165 LLvcddVYSIIKNENKS-TILV 185
Cdd:PLN03130 1411 AL----IQKTIREEFKScTMLI 1428
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-191 |
2.62e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNIgyMFQKDNLLEWRN-------------IMDNI 91
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKK--INNHNANEAINHgfalvteerrstgIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 92 TIGLE-----IQGKKDKKSLDRvESLLKTYGLWDFRSMYPK---------ELSGGMRQRVALIRTLSVNPDILLLDEPFS 157
Cdd:PRK10982 342 DIGFNslisnIRNYKNKVGLLD-NSRMKSDTQWVIDSMRVKtpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190
....*....|....*....|....*....|....*..
gi 489530649 158 ALDYQTRLlvcdDVYSII---KNENKSTILVTHDIGE 191
Cdd:PRK10982 421 GIDVGAKF----EIYQLIaelAKKDKGIIIISSEMPE 453
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-160 |
2.78e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.05 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMnFYTKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLKPT-SGDIKITG---NIGYMFQ- 77
Cdd:TIGR02633 255 DVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpvDIRNPAQa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 78 -------------KDNLLEWRNIMDNITIGL--------EIQGKKDKKSLDRVESLLKTyglwdfRSMYP----KELSGG 132
Cdd:TIGR02633 334 iragiamvpedrkRHGIVPILGVGKNITLSVlksfcfkmRIDAAAELQIIGSAIQRLKV------KTASPflpiGRLSGG 407
|
170 180
....*....|....*....|....*...
gi 489530649 133 MRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-192 |
1.16e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 24 VLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLL--KPTSGDIKITGNIgymfqkdnllewrnimdniTIGLEIQGKK 101
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVTGDV-------------------TLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 102 DKKSLDRVESLLKTYGLWDFR---------SMYP---------------------------------KELSGGMRQRVAL 139
Cdd:PRK13547 77 DAPRLARLRAVLPQAAQPAFAfsareivllGRYPharragalthrdgeiawqalalagatalvgrdvTTLSGGELARVQF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489530649 140 IRTLS---------VNPDILLLDEPFSALD--YQTRLLvcDDVYSIIKNENKSTILVTHDIGEA 192
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDlaHQHRLL--DTVRRLARDWNLGVLAIVHDPNLA 218
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
26-63 |
3.09e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 3.09e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489530649 26 KDVNFNLKEGEILTllGPSGSGKSTILNILTNLLKPTS 63
Cdd:pfam13555 15 HTIPIDPRGNTLLT--GPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-188 |
3.29e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 27 DVNFNlkEGEILTLLGPSGSGKSTILniltnllkptsgdikitgnigymfqkdnllewrnimDNITIGLEIQGKKDKKSL 106
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTIL------------------------------------DAIGLALGGAQSATRRRS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 107 DRVESLLKTYGLWDFRSMYPKeLSGGMRQRVALIRTL---SVNPDIL-LLDEPFSALDYQTRLLVCDDVYSIIKNENKsT 182
Cdd:cd03227 57 GVKAGCIVAAVSAELIFTRLQ-LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQ-V 134
|
....*.
gi 489530649 183 ILVTHD 188
Cdd:cd03227 135 IVITHL 140
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-188 |
6.26e-04 |
|
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: 38.84 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 25 LKDVNFNLKEGEILTLLGPSGSGKSTILNiltnllkptsgdikitgNIGYMFQKDNLLEWR-NIMDNITIgleiqgkkdk 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLpKFSRNKLI---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 104 kSLDRVESLLKTyGLWDF---RSMypKELSGGMRQRVALIRTLSVNPD--ILLLDEPFSALDYQTRLLVCDDVYSIIkNE 178
Cdd:cd03238 64 -FIDQLQFLIDV-GLGYLtlgQKL--STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI-DL 138
|
170
....*....|
gi 489530649 179 NKSTILVTHD 188
Cdd:cd03238 139 GNTVILIEHN 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-186 |
1.16e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.32 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 17 TKEGELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILT----NLLKPTSG----------DIK--ITGNIGYMFQKDN 80
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGvitydgitpeEIKkhYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 81 LLEWRNIMDNITIGLEIQGKKDK-KSLDR-------VESLLKTYGLWDFRSM-----YPKELSGGMRQRVALIRTLSVNP 147
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKTPQNRpDGVSReeyakhiADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190
....*....|....*....|....*....|....*....
gi 489530649 148 DILLLDEPFSALDYQTRLLVCdDVYSIIKNENKSTILVT 186
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFI-RALKTSANILDTTPLVA 266
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
126-188 |
2.09e-03 |
|
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: 37.59 E-value: 2.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 126 PKELSGGMRQ------RVALIRTLSVNPDILLLDEPFSALDYQTR-LLVCDDVYSIIKNENKSTILVTHD 188
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-160 |
2.25e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.99 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 3 DNIVEVKNINMnfYTKEG-ELEVLKDVNFNLKEGEILTLLGPSGSGKSTILNILTNLLK-PTSGDIKITG---------- 70
Cdd:PRK13549 257 EVILEVRNLTA--WDPVNpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpvkirnpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 71 ----NIGYMFQ---KDNLLEWRNIMDNITI--------GLEIQGKKDKKSLDRVESLLKTyglwdfRSMYP----KELSG 131
Cdd:PRK13549 335 aiaqGIAMVPEdrkRDGIVPVMGVGKNITLaaldrftgGSRIDDAAELKTILESIQRLKV------KTASPelaiARLSG 408
|
170 180
....*....|....*....|....*....
gi 489530649 132 GMRQRVALIRTLSVNPDILLLDEPFSALD 160
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
16-66 |
2.32e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 2.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489530649 16 YTKEGeLEVLKDVnfnLKeGEILTLLGPSGSGKSTILNILTNLLKPTSGDI 66
Cdd:cd01854 71 KTGEG-LDELREL---LK-GKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
22-55 |
5.58e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 5.58e-03
10 20 30
....*....|....*....|....*....|....
gi 489530649 22 LEVLKDVnfnLKEGEILTLLGPSGSGKSTILNIL 55
Cdd:PRK01889 185 LDVLAAW---LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
129-155 |
5.80e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 36.69 E-value: 5.80e-03
10 20
....*....|....*....|....*..
gi 489530649 129 LSGGMRQRVALIRTLSVNPDILLLDEP 155
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-67 |
7.25e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.13 E-value: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489530649 25 LKDVNFNLKEGEILTLL-GPSGSGKSTILNILTNLLKPTSGDIK 67
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLD 57
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
29-115 |
8.74e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 36.43 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489530649 29 NFNLKEGEILTLLGPSGSGKSTILNILTNLLKPTSGDIKITGNiGYMFQ-KDNLleWRNIMDNITIGLEIQGKKDKKSLD 107
Cdd:COG4928 23 SSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVYFN-AWLYDgEEDL--LAALLSEIAAELEKKKKKDKKAAK 99
|
....*...
gi 489530649 108 RVESLLKT 115
Cdd:COG4928 100 KLKKYAKR 107
|
|
| |
