|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-239 |
1.14e-123 |
|
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: 350.44 E-value: 1.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLGAFdrYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAY--ARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLGL 239
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-229 |
1.28e-108 |
|
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: 312.06 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAFDRYRRGLRDqdqTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKA---RLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-238 |
6.41e-73 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 222.06 E-value: 6.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLMLGAFDRYRRGLRdqdQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPR 159
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQ---ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 160 LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLG 238
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-229 |
3.51e-68 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 209.69 E-value: 3.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPvKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAFDRYRRGlrdqDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS----RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLREM-GVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-243 |
2.09e-65 |
|
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: 203.35 E-value: 2.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGM-- 81
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrPTSGRILFDGRDITGLPPHRIARLGIar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 ---NLvpekrELFAEMTVEDNLMLGAFDRYRRGL-----------RDQDQTLAEVFEL--FPRLQERRAQLAGTLSGGER 145
Cdd:COG0411 84 tfqNP-----RLFPELTVLENVLVAAHARLGRGLlaallrlprarREEREARERAEELleRVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|....*....
gi 2495741221 225 KVAQDPRVVEVYLGLGHGA 243
Cdd:COG0411 239 EVRADPRVIEAYLGEEAAA 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-232 |
1.30e-61 |
|
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: 193.04 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGA---------FDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALM 155
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartgsgllLARARREEREARERAEELLERV-GLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRV 232
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-238 |
7.42e-53 |
|
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: 170.80 E-value: 7.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMlgAFDRYRRGLRDQDQTLAE-VFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:cd03218 81 PQEASIFRKLTVEENIL--AVLEIRGLSKKEREEKLEeLLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLG 238
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-238 |
9.23e-52 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 167.90 E-value: 9.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlVKPDSGRIFLDGEDITHLPMHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLgAFDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:COG1137 84 PQEASIFRKLTVEDNILA-VLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLG 238
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-224 |
4.29e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.70 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK--AQEHAEIEEMVAAgmn 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVLGEdvARDPAEVRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 lVPEKRELFAEMTVEDNL-MLGAFdrYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:COG1131 78 -VPQEPALYPDLTVRENLrFFARL--YGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-238 |
1.04e-49 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 162.83 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGlVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLG 238
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-238 |
2.47e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 151.81 E-value: 2.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGG----KAQEHaeieE 75
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGkTRPDSGSVLFGGtdltGLDEH----E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 MVAAGMNLVPEKRELFAEMTVEDNLML------GAFD--RYRRGLRDQDQtLAEVFELFpRLQERRAQLAGTLSGGERQM 147
Cdd:COG4674 82 IARLGIGRKFQKPTVFEELTVFENLELalkgdrGVFAslFARLTAEERDR-IEEVLETI-GLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 148 LAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVA 227
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAG-KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
250
....*....|.
gi 2495741221 228 QDPRVVEVYLG 238
Cdd:COG4674 239 ADPRVIEVYLG 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
7.27e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.93 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAeiEEMVAa 79
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFGKPPRRA--RRRIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmnLVPEKRELFAE--MTVEDNLMLG------AFDRYRRGLRDQ-DQTLAEVfelfpRLQERRAQLAGTLSGGERQ--ML 148
Cdd:COG1121 79 ---YVPQRAEVDWDfpITVRDVVLMGrygrrgLFRRPSRADREAvDEALERV-----GLEDLADRPIGELSGGQQQrvLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 149 AvgRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLEtGTVTLEGPAAKVAQ 228
Cdd:COG1121 151 A--RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLT 227
|
....*...
gi 2495741221 229 DPRVVEVY 236
Cdd:COG1121 228 PENLSRAY 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-238 |
2.96e-43 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 146.67 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLML------------GAFD--RYRRGLRDQDQTLAEVFElFPRLQERRAQLAGTLSGGER 145
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKtpAFRRAESEALDRAATWLE-RVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
250
....*....|....
gi 2495741221 225 KVAQDPRVVEVYLG 238
Cdd:PRK11300 240 EIRNNPDVIKAYLG 253
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-236 |
4.20e-42 |
|
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: 143.65 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEM----VAA 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkPSSGEVLLDGR-----DLASLsrreLAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLMLG--AFDRYRRGLRDQDQTLA-EVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGryPHLGLFGRPSAEDREAVeEALERT-GLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEV 235
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEV 234
|
.
gi 2495741221 236 Y 236
Cdd:COG1120 235 Y 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-217 |
2.20e-41 |
|
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: 139.46 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK--AQEHAEIEEMVAagmn 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKdiKKEPEEVKRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEMTVEDNLMlgafdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03230 77 YLPEEPSLYENLTVRENLK--------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-234 |
5.54e-41 |
|
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: 140.16 E-value: 5.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIEEMVAag 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDGKditKKNLRELRRKVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 mnLV---PEkRELFAEmTVEDNLMLGAfdrYRRGLRDQ------DQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVG 151
Cdd:COG1122 79 --LVfqnPD-DQLFAP-TVEEDVAFGP---ENLGLPREeirervEEALELV-----GLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
...
gi 2495741221 232 VVE 234
Cdd:COG1122 227 LLE 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-228 |
5.88e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 140.38 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMnl 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkPDSGSILIDGEDVRKEPREARRQIGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNL-MLGAFdrYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:COG4555 79 LPDERGLYDRLTVRENIrYFAEL--YGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQ 228
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-216 |
7.85e-39 |
|
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: 134.13 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmVAAGMNL 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 V---PEkRELFAEmTVEDNLmlgAFDRYRRGL--RDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:cd03225 80 VfqnPD-DQFFGP-TVEEEV---AFGLENLGLpeEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 159 RLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGT 216
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-229 |
1.05e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYqPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLGAFDRyRRGLRDQDQTLAEVFELFPRLQERR--AQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPR-RGGLIDWRAMRRRARELLARLGLDIdpDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLI-----EqnaraALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIshrldE-----VFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-212 |
3.54e-37 |
|
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: 129.96 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEhaEIEEMVAagmnLVP 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKPLE--KERKRIG----YVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 86 EKRELFAEM--TVEDNLMLG------AFDRYRRGLRDQ-DQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGlyghkgLFRRLSKADKAKvDEALERV-----GLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVL 212
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-221 |
2.01e-36 |
|
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: 127.72 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITF-GGKAQEHAEIEEMVAAgmnL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFdGKSYQKNIEALRRIGA---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VpEKRELFAEMTVEDNLMLGAfDRYRRGLRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:cd03268 78 I-EAPGFYPNLTARENLRLLA-RLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-240 |
6.73e-36 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 127.32 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGnIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMlgAFDRYRRGL-RDQDQTLA-EVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLM--AVLQIRDDLsAEQREDRAnELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLGLG 240
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGED 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-194 |
5.07e-35 |
|
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: 124.13 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEemVAAGMNL 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLmlgAFDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:COG4133 80 LGHADGLKPELTVRENL---RFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|.
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILL 194
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-220 |
5.89e-35 |
|
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: 122.54 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNLV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEkrelfaemtvednlmlgafdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:cd03216 81 YQ-----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLE 220
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
7.10e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 7.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEE---MVAagm 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPLSAMPPPEwrrQVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nLVPEKRELFAEmTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQERRAQlagTLSGGERQMLAVGRALMAKPRLL 161
Cdd:COG4619 78 -YVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVE---RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-217 |
8.83e-35 |
|
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: 123.77 E-value: 8.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaqeHAEIEEMVAAGMN 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYING----YSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 L--VPEKRELFAEMTVEDNLMLgaFDR----YRRGLRDQDQTLAEVFELFPrLQERRaqlAGTLSGGERQMLAVGRALMA 156
Cdd:cd03263 77 LgyCPQFDALFDELTVREHLRF--YARlkglPKSEIKEEVELLLRVLGLTD-KANKR---ARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-216 |
6.62e-34 |
|
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: 119.66 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaeieemvaagmnlvp 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 86 ekrelfaemtvednlmlgafdryrrglrdqdqtlaEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:cd00267 62 -----------------------------------DIAKLPLEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 166 PSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGT 216
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-221 |
1.08e-33 |
|
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: 119.85 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGK---AQEHAEIEEMVAagmn 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeILLDGKdlaSLSPKELARKIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPekrelfaemtvednlmlgafdryrrglrdqdQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03214 77 YVP-------------------------------QALELL-----GLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-229 |
1.46e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAydkvEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGeIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPE--KRE-LFAEMTVEDNLMLGAFDRY-RRGLRDQDQTLAEVFELFPRLQER---RAQLAGTLSGGERQMLAVGRALMA 156
Cdd:COG1129 332 VPEdrKGEgLVLDLSIRENITLASLDRLsRGGLLDRRRERALAEEYIKRLRIKtpsPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 157 KPRLLMLDEPSLGlapriV-----REVFRIVARLREMGVSILLI-----EqnaraALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:COG1129 412 DPKVLILDEPTRG-----IdvgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRIVGELDREEA 481
|
...
gi 2495741221 227 AQD 229
Cdd:COG1129 482 TEE 484
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
1.54e-33 |
|
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: 126.56 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAY-----DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIE 74
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAAG--MNLV---PEkRELFAEMTVEDNLM--LGAFDRYRRGLRDQD-QTLAEVFELFPRLQERRaqlAGTLSGGERQ 146
Cdd:COG1123 336 SLRELRrrVQMVfqdPY-SSLNPRMTVGDIIAepLRLHGLLSRAERRERvAELLERVGLPPDLADRY---PHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 147 MLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAK 225
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....*.
gi 2495741221 226 VAQDPR 231
Cdd:COG1123 492 VFANPQ 497
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-245 |
1.58e-33 |
|
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: 126.56 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAkLLQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS----QGGITFGGK------AQ 68
Cdd:COG1123 1 MTP-LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggriSGEVLLDGRdllelsEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 69 EHAEIEEMVA--AGMNLVPekrelfaeMTVEDNLMLGAfdryRRGLRDQDQTLAEVFELFPR--LQERRAQLAGTLSGGE 144
Cdd:COG1123 80 LRGRRIGMVFqdPMTQLNP--------VTVGDQIAEAL----ENLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 145 RQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPA 223
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
250 260
....*....|....*....|..
gi 2495741221 224 AKVAQDPRVVEVYLGLGHGAPA 245
Cdd:COG1123 228 EEILAAPQALAAVPRLGAARGR 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-166 |
3.78e-33 |
|
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: 117.36 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAqEHAEIEEMVAAGMNLVPEKRELFAEMTVEDN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQD-LTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 100 LMLGA--FDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:pfam00005 80 LRLGLllKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-207 |
4.29e-33 |
|
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: 119.17 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKA--QEHAEIEEMVA-AGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeEPDSGTIIIDGLKltDDKKNINELRQkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nlVPEKRELFAEMTVEDNLMLGAfdRYRRGlRDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKPR 159
Cdd:cd03262 81 --VFQQFNLFPHLTVLENITLAP--IKVKG-MSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2495741221 160 LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVAD 207
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVAD 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-231 |
2.87e-32 |
|
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: 117.98 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY----DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMvAA 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAF-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLV---PEkRELFAEMTVEDNLMLGAfdrYRRGLRDQDQTLAEVFE---LFPRLQERRAQlagTLSGGERQMLAVGRA 153
Cdd:COG1124 80 RVQMVfqdPY-ASLHPRHTVDRILAEPL---RIHGLPDREERIAELLEqvgLPPSFLDRYPH---QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-240 |
4.16e-32 |
|
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: 117.44 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNLV 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFEL--FPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlkLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVYLGLG 240
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-217 |
1.88e-31 |
|
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: 114.92 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmvaAGMNLV 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLmlgAFDRYRRGLRDQDQT-----LAEVFELFPRLQERraqlAGTLSGGERQMLAVGRALMAKPR 159
Cdd:cd03259 78 FQDYALFPHLTVAENI---AFGLKLRGVPKAEIRarvreLLELVGLEGLLNRY----PHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 160 LLMLDEPSLGLAPRIvREVFR--IVARLREMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03259 151 LLLLDEPLSALDAKL-REELReeLKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
2.05e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.14 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAkLLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEE 75
Cdd:COG1136 1 MSP-LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVLIDGQ-----DISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 MVAAGM---------------NLVPEkrelfaeMTVEDNLMLGAfdRYRRGLRDQDQTLA-EVFELFpRLQERRAQLAGT 139
Cdd:COG1136 75 LSERELarlrrrhigfvfqffNLLPE-------LTALENVALPL--LLAGVSRKERRERArELLERV-GLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAAlQVADYAYVLETGTVT 218
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
3.30e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.51 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHaeieemvaa 79
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDSGRILLDGRDVTG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmnLVPEKRE---------LFAEMTVEDNLmlgAFdryrrGLR-------DQDQTLAEVFELFpRLQERRAQLAGTLSGG 143
Cdd:COG3842 72 ---LPPEKRNvgmvfqdyaLFPHLTVAENV---AF-----GLRmrgvpkaEIRARVAELLELV-GLEGLADRYPHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 144 ERQMLAVGRALMAKPRLLMLDEPsLG-----LAPRIVREVFRIvarLREMGVSILLI-----EqnaraALQVADYAYVLE 213
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEP-LSaldakLREEMREELRRL---QRELGITFIYVthdqeE-----ALALADRIAVMN 210
|
250
....*....|....*...
gi 2495741221 214 TGTVTLEGPAAKVAQDPR 231
Cdd:COG3842 211 DGRIEQVGTPEEIYERPA 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-223 |
6.30e-31 |
|
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: 113.01 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV---LPSQGGITFGGKAQEHAEIEEMVAAGMN 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEMTVEDnlmlgaFDRYrrglrdqdqtlaeVFELFprlqerraqlagtlSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03217 81 LAFQYPPEIPGVKNAD------FLRY-------------VNEGF--------------SGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQV-ADYAYVLETGTVTLEGPA 223
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
9.14e-31 |
|
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: 113.92 E-value: 9.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAA 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGEILVDGQ-----DITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVpeKRE---------LFAEMTVEDNLMLGAfdRYRRGLRDQDQT-----------LAEVFELFPrlqerrAQLagt 139
Cdd:COG1127 76 ELYEL--RRRigmlfqggaLFDSLTVFENVAFPL--REHTDLSEAEIRelvleklelvgLPGAADKMP------SEL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 lSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:COG1127 143 -SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*.
gi 2495741221 219 LEGPAAKVAQ--DPRV 232
Cdd:COG1127 222 AEGTPEELLAsdDPWV 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-226 |
1.31e-30 |
|
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: 113.04 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI------MGVLPSQGGITFGGK---AQEHAEIEEM 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlIPGAPDEGEVLLDGKdiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 77 VAAGMnlVPEKRELFAeMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFE---LFPRLQERraQLAGTLSGGERQMLAVGRA 153
Cdd:cd03260 81 RRVGM--VFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRkaaLWDEVKDR--LHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-221 |
1.70e-30 |
|
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: 112.98 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAA 79
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGK-----DLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVpeKREL---FAE--------MTVEDNLMLGAfdRYRRGLRDQDQ---TLAEVFELFPRLQERRAQLAGTLSGGER 145
Cdd:cd03257 76 LRKIR--RKEIqmvFQDpmsslnprMTIGEQIAEPL--RIHGKLSKKEArkeAVLLLLVGVGLPEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-217 |
2.42e-30 |
|
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: 112.20 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAAG 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVRVDGT-----DISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 M---------------NLVPekrelfaEMTVEDNLMLGAFDRYRRGlRDQDQTLAEVFELFpRLQERRAQLAGTLSGGER 145
Cdd:cd03255 76 LaafrrrhigfvfqsfNLLP-------DLTALENVELPLLLAGVPK-KERRERAEELLERV-GLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAAlQVADYAYVLETGTV 217
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-221 |
3.33e-30 |
|
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: 112.08 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG--ITFGGKA-QEHAEIEEMVAagmn 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGraTVAGHDVvREPREVRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEMTVEDNL-MLGAFDRYRRGLRdqDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:cd03265 77 IVFQDLSVDDELTGWENLyIHARLYGVPGAER--RERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
3.77e-30 |
|
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: 112.28 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEE-------- 75
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTDINKLKGKAlrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 -MVAAGMNLVPEkrelfaeMTVEDNLMLGAFDRYrrglrdqdQTLAEVFELFPRLQERRA--------------QLAGTL 140
Cdd:cd03256 81 gMIFQQFNLIER-------LSVLENVLSGRLGRR--------STWRSLFGLFPKEEKQRAlaalervglldkayQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 141 SGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTL 219
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
250
....*....|....*..
gi 2495741221 220 EGPAAKVaQDPRVVEVY 236
Cdd:cd03256 226 DGPPAEL-TDEVLDEIY 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-232 |
6.54e-30 |
|
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: 111.44 E-value: 6.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAAG---- 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIDGE-----DISGLSEAElyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 ---MNLVPEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAK 157
Cdd:cd03261 76 rrrMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAV-GLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 158 PRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV--AQDPRV 232
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSDDPLV 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-231 |
8.43e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 111.24 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGK--AQEHAEIEEMVA-AG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLlEEPDSGTITVDGEdlTDSKKDINKLRRkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MnlVPEKRELFAEMTVEDNLMLGAfdRYRRGlRDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:COG1126 81 M--VFQQFNLFPHLTVLENVTLAP--IKVKK-MSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 159 RLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-216 |
1.36e-29 |
|
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: 109.20 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaqehaeieEMVAAGMNLV 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDG---------EDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRE----------LFAEMTVEDNLMLGafdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRAL 154
Cdd:cd03229 72 PPLRRrigmvfqdfaLFPHLTVLENIALG------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 155 MAKPRLLMLDEPSLGLAPRIVREVFRIVARLREM-GVSILLIEQNARAALQVADYAYVLETGT 216
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-217 |
2.58e-29 |
|
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: 108.29 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYdkveAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRE---LFAEMTVEDNLMLGAFdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRL 160
Cdd:cd03215 80 VPEDRKregLVLDLSVAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 161 LMLDEPSLGLAPRIVREVFRIVARLREMGVSILLI-----EqnaraALQVADYAYVLETGTV 217
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLIsseldE-----LLGLCDRILVMYEGRI 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-218 |
5.90e-29 |
|
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: 108.11 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 15 YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNLVpeKRELFAE 93
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKERRKSIGYVMQDV--DYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 mTVEDNLMLGAfDRYRRGLRDQDQTLAEvFELFpRLQERRAQlagTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPR 173
Cdd:cd03226 88 -SVREELLLGL-KELDAGNEQAETVLKD-LDLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2495741221 174 IVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-229 |
7.03e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.61 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLGaFDRYRRGLRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG-LPKRQASMQKMKQLLAAL-----GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-226 |
1.97e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLMLGAfDRYRRGLRDQDQTLAEV--------FELFPRlqerraQLAGTLSGGERQMLAVG 151
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGL-EPTKGGRLDRKAARARIrelserygLDVDPD------AKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-230 |
2.08e-28 |
|
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: 110.19 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAeieemvAAGMNLVPEKR---------ELFAE 93
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLErPDSGRIRLGGEVLQDS------ARGIFLPPHRRrigyvfqeaRLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 MTVEDNLMLGafdrYRRGLRDQDQ-TLAEVFELF--PRLQERRAQlagTLSGGERQMLAVGRALMAKPRLLMLDEP--SL 168
Cdd:COG4148 92 LSVRGNLLYG----RKRAPRAERRiSFDEVVELLgiGHLLDRRPA---TLSGGERQRVAIGRALLSSPRLLLMDEPlaAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 169 GLAPRivREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:COG4148 165 DLARK--AEILPYLERLRdELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-194 |
2.15e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAAGMNLV 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEVLWDGE-----PLDPEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLM-LGAfdryRRGLRDQD--QTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:COG4152 77 PEERGLYPKMKVGEQLVyLAR----LKGLSKAEakRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190
....*....|....*....|....*....|...
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILL 194
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF 184
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-221 |
3.42e-28 |
|
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: 106.68 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEemVAA 79
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDGFDVVKEPAE--ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLmlgafdRYRRGLR--DQDQTLAEVFELFPRLQ-----ERRAqlaGTLSGGERQMLAVGR 152
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENL------EYFAGLYglKGDELTARLEELADRLGmeellDRRV---GGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 153 ALMAKPRLLMLDEPSLGL---APRIVREVFRivaRLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLdvmATRALREFIR---QLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-215 |
4.54e-28 |
|
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: 104.77 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD--KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAgMN 82
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAeMTVEDNLmlgafdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03228 80 YVPQDPFLFS-GTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNaRAALQVADYAYVLETG 215
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-236 |
4.64e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSaklLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAqehaeieemvaA 79
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRIVLNGRD-----------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRE---------LFAEMTVEDNLmlgAFdryrrGLRDQDQTLAE----VFELFprlqeRRAQLAG-------T 139
Cdd:COG1118 67 FTNLPPRERRvgfvfqhyaLFPHMTVAENI---AF-----GLRVRPPSKAEirarVEELL-----ELVQLEGladrypsQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPsLG-----LAPRIVREVFRIvarLREMGVSILLIEQNARAALQVADYAYVLET 214
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEP-FGaldakVRKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQ 209
|
250 260
....*....|....*....|..
gi 2495741221 215 GTVTLEGPAAKVAQDPRVVEVY 236
Cdd:COG1118 210 GRIEQVGTPDEVYDRPATPFVA 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-212 |
8.31e-28 |
|
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: 105.63 E-value: 8.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEmVAAG 80
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTSGEVLVDGE-----PVTG-PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEKRELFAEMTVEDNLMLGaFDRYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRL 160
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 161 LMLDEP--SL--GLAPRIVREVFRIvarLREMGVSILLIEQNARAALQVADYAYVL 212
Cdd:cd03293 153 LLLDEPfsALdaLTREQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-166 |
5.14e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.40 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAeiee 75
Cdd:COG1116 3 AAAPALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVDGKPVTGP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 mvAAGMNLVPEKRELFAEMTVEDNLMLGAfdRYRRGLRDQDQTLA-EVFELFpRLQERRAQLAGTLSGGERQMLAVGRAL 154
Cdd:COG1116 79 --GPDRGVVFQEPALLPWLTVLDNVALGL--ELRGVPKAERRERArELLELV-GLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170
....*....|..
gi 2495741221 155 MAKPRLLMLDEP 166
Cdd:COG1116 154 ANDPEVLLMDEP 165
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-195 |
5.77e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.07 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVAAG 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEKRELFAEMTVEDNLMLGAFDRyRRGLRDQDQTLAEVFELFPRLQER---RAQLaGTLSGGERQMLAVGRALMAK 157
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPH-KGGIVNRRLLNYEAREQLEHLGVDidpDTPL-KYLSIGQRQMVEIAKALARN 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2495741221 158 PRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLI 195
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYV 196
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-236 |
1.22e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.66 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMvaAGMNL 83
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELtPSSGEVRLNGRPLAAWSPWEL--ARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 V-PEKREL-FAeMTVEDNLMLGAfDRYRRGLRDQDQTLAEVFELF--PRLQERRAQlagTLSGGERQ--MLAvgRAL--- 154
Cdd:COG4559 79 VlPQHSSLaFP-FTVEEVVALGR-APHGSSAAQDRQIVREALALVglAHLAGRSYQ---TLSGGEQQrvQLA--RVLaql 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 155 ----MAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:COG4559 152 wepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
....*.
gi 2495741221 231 RVVEVY 236
Cdd:COG4559 232 LLERVY 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-221 |
1.44e-26 |
|
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: 101.97 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmvaagMNLV 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLM-LGAFdryrRGLRDQDqTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:cd03269 76 PEERGLYPKMKVIDQLVyLAQL----KGLKKEE-ARRRIDEWLERleLSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-205 |
1.45e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.17 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS----QGGITFGGKAQEHaeieemvaagm 81
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsaSGEVLLNGRRLTA----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nLVPEKRE---------LFAEMTVEDNLMLGAFDRYRRGLRDQ--DQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAV 150
Cdd:COG4136 71 -LPAEQRRigilfqddlLFPHLSVGENLAFALPPTIGRAQRRArvEQALEEA-----GLAGFADRDPATLSGGQRARVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIvREVFR--IVARLREMGVSILLI---EQNARAALQV 205
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAAL-RAQFRefVFEQIRQRGIPALLVthdEEDAPAAGRV 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-230 |
2.49e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 15 YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITF-------GGKAQEHAEIEEmvaAGMnlVPEK 87
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvnDPKVDERLIRQE---AGM--VFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 88 RELFAEMTVEDNLMLGAFdRYRRGLRDQDQTLAEvfELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:PRK09493 86 FYLFPHLTALENVMFGPL-RVRGASKEEAEKQAR--ELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 166 PSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-236 |
7.90e-26 |
|
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: 101.31 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQG------GITFGGkaqehAEIEE-- 75
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGndvrlfGERRGG-----EDVWElr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 ----MVAAGMnlvpeKRELFAEMTVEDNLMLGAFD---RYRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQML 148
Cdd:COG1119 78 krigLVSPAL-----QLRFPRDETVLDVVLSGFFDsigLYREPTDEQRERARELLELL-GLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 149 AVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVA 227
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
....*....
gi 2495741221 228 QDPRVVEVY 236
Cdd:COG1119 232 TSENLSEAF 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-207 |
7.98e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.32 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-----DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEemvaa 79
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLpPDSGSILIDGK-----DVT----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmNLVPEKRELF-------------AEMTVEDNLMLgAFDR-YRRGL--------RDQDQTLAEVFELfpRLQERRAQLA 137
Cdd:COG1101 72 --KLPEYKRAKYigrvfqdpmmgtaPSMTIEENLAL-AYRRgKRRGLrrgltkkrRELFRELLATLGL--GLENRLDTKV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 138 GTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVAD 207
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGN 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-195 |
1.50e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVA-YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMN 82
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGsIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPE---KRELFAEMTVEDNLMLGAFDRY---RRGLRDQDQTLAEVFELFPRLQER---RAQLAGTLSGGERQMLAVGRA 153
Cdd:COG3845 337 YIPEdrlGRGLVPDMSVAENLILGRYRRPpfsRGGFLDRKAIRAFAEELIEEFDVRtpgPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLI 195
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-238 |
1.83e-25 |
|
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: 99.72 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEaVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIeemvaagMNLV 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDSGKILLNGK-----DI-------TNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRE---------LFAEMTVEDNLMLGafdrYRRGLRDQDQTLAEVFEL-----FPRLQERRAqlaGTLSGGERQMLAV 150
Cdd:cd03299 68 PEKRDisyvpqnyaLFPHMTVYKNIAYG----LKKRKVDKKEIERKVLEIaemlgIDHLLNRKP---ETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
250
....*....|.
gi 2495741221 230 PRVVEV--YLG 238
Cdd:cd03299 221 PKNEFVaeFLG 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-221 |
3.12e-25 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 99.26 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG---VLPSQGGITFGGKAQEHAEIEEMVAAGMN 82
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsYEVTSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEMTVEDnlMLGAFDRYRRGLRDQDQTlaEVFELFPRLQERRAQLA------------GtLSGGERQMLAV 150
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLE--FLRSALNARRSARGEEPL--DLLDFEKLLKEKLALLDmdeeflnrsvneG-FSGGEKKRNEI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVA-DYAYVLETGTVTLEG 221
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSG 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-217 |
3.82e-25 |
|
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: 98.85 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNLV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLmlgAFDRYRRGLR--DQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03300 78 FQNYALFPHLTVFENI---AFGLRLKKLPkaEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-221 |
5.33e-25 |
|
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: 97.95 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 25 SLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNLVPEKRELFAEMTVEDNLMLG 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFeTPQSGRVLINGVDVTAAPPADR---PVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 104 AFDRYRrgLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVA 183
Cdd:cd03298 95 LSPGLK--LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2495741221 184 RL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03298 173 DLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-166 |
6.74e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.53 E-value: 6.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaeieeMVAagmNLV 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEdPTSGEILIGGR---------DVT---DLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRE---------LFAEMTVEDNLmlgAFdryrrGLR-------DQDQTLAEVFELFpRLQERRAQLAGTLSGGERQML 148
Cdd:COG3839 72 PKDRNiamvfqsyaLYPHMTVYENI---AF-----PLKlrkvpkaEIDRRVREAAELL-GLEDLLDRKPKQLSGGQRQRV 142
|
170
....*....|....*...
gi 2495741221 149 AVGRALMAKPRLLMLDEP 166
Cdd:COG3839 143 ALGRALVREPKVFLLDEP 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-221 |
7.26e-25 |
|
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: 102.53 E-value: 7.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDK-VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaQEHAEI-EEMVAAGMN 82
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILING--VDLSDLdPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAeMTVEDNLMLGAFD----RYRRGLRDQDqtLAEVFELFP-----RLQERraqlAGTLSGGERQMLAVGRA 153
Cdd:COG4988 415 WVPQNPYLFA-GTIRENLRLGRPDasdeELEAALEAAG--LDEFVAALPdgldtPLGEG----GRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNArAALQVADYAYVLETGTVTLEG 221
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQG 553
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-193 |
1.07e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.43 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 16 DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaeieemvaagmNLVPEKRE----- 89
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErPTSGQVLVNGQ---------------DLSRLKRReipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 ------------LFAEMTVEDNLML-----GafdryrRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGR 152
Cdd:COG2884 78 rrrigvvfqdfrLLPDRTVYENVALplrvtG------KSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2495741221 153 ALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSIL 193
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVL 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-231 |
1.43e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGG-------------K 66
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGqtinlvrdkdgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 67 AQEHAEIEeMVAAGMNLVPEKRELFAEMTVEDNLMLGAFDRYrrGLRDQDQTLAEVFELFPRLQERRAQ--LAGTLSGGE 144
Cdd:PRK10619 81 VADKNQLR-LLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQgkYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 145 RQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
....*..
gi 2495741221 225 KVAQDPR 231
Cdd:PRK10619 238 QLFGNPQ 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-230 |
2.26e-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: 99.42 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEieemvaAGMNLVPEKRE---------LFAE 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTLFDSR------KGIFLPPEKRRigyvfqearLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 MTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQerraQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPR 173
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLG----RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 174 IVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:TIGR02142 166 RKYEILPYLERLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-231 |
3.93e-24 |
|
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: 98.20 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP----SQGGITFGGK---AQEHAEI 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDGEdllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 74 EEMVAAGMNLVpekrelFAE--------MTVEDNLMLGAfdRYRRGL--RDQDQTLAEVFEL--FPRLQERRAQLAGTLS 141
Cdd:COG0444 81 RKIRGREIQMI------FQDpmtslnpvMTVGDQIAEPL--RIHGGLskAEARERAIELLERvgLPDPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 142 GGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLE 220
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250
....*....|.
gi 2495741221 221 GPAAKVAQDPR 231
Cdd:COG0444 233 GPVEELFENPR 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
4.36e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS---QGGITFGGKAQEHAEIEEMV 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AAGMNLVPEKRELFAEMTVEDNLMLGAfDRYRRGLRDQDQTLAEVFELFPRLQ--ERRAQLAGTLSGGERQMLAVGRALM 155
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGN-EITPGGIMDYDAMYLRAQKLLAQLKldINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTED 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-228 |
4.62e-24 |
|
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: 100.29 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmVAAGMN 82
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPAS-LRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFaEMTVEDNLMLGafdryrrglrDQDQTLAEVFELfprlqerrAQLAG---------------------TLS 141
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG----------DPDATDEEIIEA--------ARLAGlhdfiealpmgydtvvgeggsNLS 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 142 GGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVRevfRIVARLREM--GVSILLIEQNArAALQVADYAYVLETGTVTL 219
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEA---IILENLRRLlkGRTVIIIAHRL-STIRLADRIIVLDKGRIVE 689
|
....*....
gi 2495741221 220 EGPAAKVAQ 228
Cdd:COG2274 690 DGTHEELLA 698
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-230 |
4.81e-24 |
|
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: 100.23 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD--KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEiEEMVAAGMN 82
Cdd:COG4987 334 LELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGSITLGGVDLRDLD-EDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAeMTVEDNLMLGafdryrrglRDQ--DQTLAEVFE---LFPRLQERRAQL-------AGTLSGGERQMLAV 150
Cdd:COG4987 413 VVPQRPHLFD-TTLRENLRLA---------RPDatDEELWAALErvgLGDWLAALPDGLdtwlgegGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIeQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLI-THRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-238 |
7.08e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.59 E-value: 7.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDkVEAVSgVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaQEHAEIEemvaagmnlv 84
Cdd:COG3840 2 LRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLpPDSGRILWNG--QDLTALP---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKR---------ELFAEMTVEDNLMLGafdrYRRGLR---DQDQTLAEVFElfpR--LQERRAQLAGTLSGGERQMLAV 150
Cdd:COG3840 68 PAERpvsmlfqenNLFPHLTVAQNIGLG----LRPGLKltaEQRAQVEQALE---RvgLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEP--SLGLAPRivREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV- 226
Cdd:COG3840 141 ARCLVRKRPILLLDEPfsALDPALR--QEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALl 218
|
250
....*....|...
gi 2495741221 227 -AQDPRVVEVYLG 238
Cdd:COG3840 219 dGEPPPALAAYLG 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-236 |
1.20e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.61 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMvAAGMNL 83
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELsPDSGEVRLNGRPLADWSPAEL-ARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLGAFDRYRRGLRDQ---DQTLAEVfELfprlqerrAQLAG----TLSGGERQMLAVGRALM- 155
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDalvAAALAQV-DL--------AHLAGrdypQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 156 -----AKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
....*..
gi 2495741221 230 PRVVEVY 236
Cdd:PRK13548 232 ETLRRVY 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
4.90e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKA-QEHAEIEEMva 78
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPvPSRARHARQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 aGMNLVPEKRELFAEMTVEDNLMLgaFDRY----RRGLRDQDQTLAEvfelFPRLQERRAQLAGTLSGGERQMLAVGRAL 154
Cdd:PRK13537 81 -RVGVVPQFDNLDPDFTVRENLLV--FGRYfglsAAAARALVPPLLE----FAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 155 MAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG-PAAKVAQDP--R 231
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGaPHALIESEIgcD 233
|
....*
gi 2495741221 232 VVEVY 236
Cdd:PRK13537 234 VIEIY 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-217 |
1.14e-22 |
|
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: 91.93 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNLV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLeEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAfdRYRRGLRDQ-DQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGL--KLRKVPKDEiDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-221 |
1.16e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqEHAEIEEMVAAGMN 82
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGV--PVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEmTVEDNLmlgafdryrrGLRdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL----------GRR--------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARaALQVADYAYVLETGTVTLEG 221
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-166 |
1.54e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK------AQEHAEIEEm 76
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDSGTVKLGETvkigyfDQHQEELDP- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 77 vaagmnlvpekrelfaEMTVEDNLMLGAFDRYRRGLRDqdqtLAEVFeLFPRlqERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:COG0488 393 ----------------DKTVLDELRDGAPGGTEQEVRG----YLGRF-LFSG--DDAFKPVGVLSGGEKARLALAKLLLS 449
|
170
....*....|
gi 2495741221 157 KPRLLMLDEP 166
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-217 |
1.99e-22 |
|
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: 91.20 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 30 EGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIeemvaaGMNLVPEKRE---------LFAEMTVEDN 99
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLFDSRK------KINLPPQQRKiglvfqqyaLFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 LMLGAFDRYRRGLRDQDQTLAEVFELFPrLQERRAQlagTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLaPRIVREVF 179
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDLLGLDH-LLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSAL-DRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2495741221 180 RIVAR--LREMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03297 171 LPELKqiKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-221 |
2.83e-22 |
|
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: 90.72 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGqIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaQEHAEIEEMVAAGMNLV 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTpPSSGTIRIDG--QDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLMLGAFdryRRGL--RDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAW---LKGIpsKEVKARVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 163 LDEPSLGLAPRiVREVFR-IVARLREMGVSIL---LIEQNARAALQVAdyayVLETGTVTLEG 221
Cdd:cd03264 154 VDEPTAGLDPE-ERIRFRnLLSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-238 |
2.96e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkAQEHAEIEeMVAA 79
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKITVLG-VPVPARAR-LARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLMLgaFDRY-RRGLRDQDQTLAEVFElFPRLQERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLV--FGRYfGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 159 RLLMLDEPSLGLAPRiVREVfrIVARLREM---GVSILLIEQNARAALQVADYAYVLETGTVTLEG-PAAKVAQDP--RV 232
Cdd:PRK13536 192 QLLILDEPTTGLDPH-ARHL--IWERLRSLlarGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGrPHALIDEHIgcQV 268
|
....*.
gi 2495741221 233 VEVYLG 238
Cdd:PRK13536 269 IEIYGG 274
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-206 |
6.82e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNL 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDGVDLSHVPPYQR---PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLG-AFDRYRRGlrDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGlKQDKLPKA--EIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2495741221 163 LDEPsLG-----LAPRIVREVFRIVARLremGVSILLIEQNARAALQVA 206
Cdd:PRK11607 173 LDEP-MGaldkkLRDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMA 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-229 |
6.83e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.53 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 17 KVEAVSG-----VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRE- 89
Cdd:PRK10762 259 KVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPrTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 --LFAEMTVEDNLMLGAFDRYRRG---LRDQDQTLA--EVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:PRK10762 339 dgLVLGMSVKENMSLTALRYFSRAggsLKHADEQQAvsDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQE 485
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
7.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 3 AKLLQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQeHAEIEEMVAAG 80
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREV-NAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLV---PEKrELFAeMTVEDNLmlgAFDRYRRGLrDQDQTLAEVFELFP--RLQERRAQLAGTLSGGERQMLAVGRALM 155
Cdd:PRK13647 81 VGLVfqdPDD-QVFS-STVWDDV---AFGPVNMGL-DKDEVERRVEEALKavRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGpAAKVAQDPRVVE 234
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDIVE 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-223 |
8.86e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG---VLPSQGGITFGGKAQEHAEIEEMVAAGMN 82
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LV----PEkrelFAEMTVEDNLMLGAFDRYRRGLRDQD-----QTLAEVFELFPRLQERraQLAGTLSGGER------QM 147
Cdd:COG0396 81 LAfqypVE----IPGVSVSNFLRTALNARRGEELSAREflkllKEKMKELGLDEDFLDR--YVNEGFSGGEKkrneilQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 148 lavgraLMAKPRLLMLDEPSLGL---APRIVREVFRivaRLREMGVSILLIEQNARA-ALQVADYAYVLETGTVTLEGPA 223
Cdd:COG0396 155 ------LLLEPKLAILDETDSGLdidALRIVAEGVN---KLRSPDRGILIITHYQRIlDYIKPDFVHVLVDGRIVKSGGK 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-195 |
1.54e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLrVAYDKV----EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP--SQGGITFGGKAQEHAEIEEMVAA 79
Cdd:PRK13549 260 LEVRNL-TAWDPVnphiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRE---LFAEMTVEDNLMLGAFDRY-RRGLRDQDQTLAEVFELFPRLQERRAQLA---GTLSGGERQMLAVGR 152
Cdd:PRK13549 339 GIAMVPEDRKrdgIVPVMGVGKNITLAALDRFtGGSRIDDAAELKTILESIQRLKVKTASPElaiARLSGGNQQKAVLAK 418
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2495741221 153 ALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLI 195
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-231 |
2.02e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP------SQGGITFGGKAQEHAEIEEM-VA 78
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVDPIeVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNLVPEKRELFAEMTVEDNLMLGAfdRYRRGLRDQDQtLAEVFE-------LFPRLQERRAQLAGTLSGGERQMLAVG 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKE-LDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAAlQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAA-RVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-221 |
2.41e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.93 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 15 YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKA--QEHAEIEEMVAAGMNlvpEKRELF 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAGLVpwKRRKKFLRRIGVVFG---QKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 92 AEMTVEDNLMLGA------FDRYRRGLRDqdqtLAEVFELFPRLQerraQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:cd03267 108 WDLPVIDSFYLLAaiydlpPARFKKRLDE----LSELLDLEELLD----TPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 166 PSLGL---APRIVREVFRIVARLRemGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03267 180 PTIGLdvvAQENIRNFLKEYNRER--GTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-230 |
5.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD-KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVA-AGM 81
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkPTSGSVLIRGEPITKENIREVRKfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFAEmTVEDNLmlgAFDRYRRGLRDQ--DQTLAEVFELFPrLQERRAQLAGTLSGGERQMLAVGRALMAKPR 159
Cdd:PRK13652 83 VFQNPDDQIFSP-TVEQDI---AFGPINLGLDEEtvAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 160 LLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-228 |
6.17e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSaIMGVL--PSQGGITFGG-------KAQEHAEIEEM 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLetPDSGQLNIAGhqfdfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 77 VAAGMnlVPEKRELFAEMTVEDNLM------LGafdryrrglRDQDQTLAEVFELFPRLQ--ERRAQLAGTLSGGERQML 148
Cdd:COG4161 82 QKVGM--VFQQYNLWPHLTVMENLIeapckvLG---------LSKEQAREKAMKLLARLRltDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 149 AVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQ 228
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-202 |
6.69e-21 |
|
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: 87.41 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSaIMGVL--PSQGGITFGGK---AQEHAEIEE 75
Cdd:TIGR02211 1 LLKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLH-LLGGLdnPTSGEVLFNGQslsKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 MVAAGMNLVPEKRELFAEMTVEDNLM----LGAFDRyrRGLRDQDQTLAEVFELFPRLQERraqlAGTLSGGERQMLAVG 151
Cdd:TIGR02211 80 LRNKKLGFIYQFHHLLPDFTALENVAmpllIGKKSV--KEAKERAYEMLEKVGLEHRINHR----PSELSGGERQRVAIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAA 202
Cdd:TIGR02211 154 RALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELA 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-231 |
9.60e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.66 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLL------------SAIMGVLPSQGGITFGGKAQEHAEI 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlielypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 74 EEMVAAGMNLVPEkrelfaeMTVEDNLMLG-AFDRYRRGLRDQDQTLAEVFE---LFPRLQERRAQLAGTLSGGERQMLA 149
Cdd:PRK14247 84 VQMVFQIPNPIPN-------LSIFENVALGlKLNRLVKSKKELQERVRWALEkaqLWDEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 150 VGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
..
gi 2495741221 230 PR 231
Cdd:PRK14247 236 PR 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-231 |
9.82e-21 |
|
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: 87.25 E-value: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 17 KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKaqehaEIEEMvaAGMNLVPEKRE------ 89
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGT-----DLTLL--SGKELRKARRRigmifq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 ---LFAEMTVEDNLMLgafdryrrGLR----DQDQTLAEVFEL--FPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRL 160
Cdd:cd03258 90 hfnLLSSRTVFENVAL--------PLEiagvPKAEIEERVLELleLVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 161 LMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-226 |
1.34e-20 |
|
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: 90.19 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmvaAGMN 82
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWpPTAGSVRLDGADLSQWDREE---LGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 L--VPEKRELFAEmTVEDNL-MLGAFDRyrrglrdqdqtlAEVFELfprlqerrAQLAG--------------------- 138
Cdd:COG4618 408 IgyLPQDVELFDG-TIAENIaRFGDADP------------EKVVAA--------AKLAGvhemilrlpdgydtrigegga 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 139 TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADYAYVLETGTVT 218
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRDGRVQ 545
|
....*...
gi 2495741221 219 LEGPAAKV 226
Cdd:COG4618 546 AFGPRDEV 553
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-226 |
1.40e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.78 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 33 IVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEieemvaAGMNLVPEKRE---------LFAEMTVEDNLML 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGlTRPQKGRIVLNGRVLFDAE------KGICLPPEKRRigyvfqdarLFPHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 103 GafdrYRRGLRDQDQTLAEVFELFPRLqerrAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEP--SLGLaPRiVREVFR 180
Cdd:PRK11144 100 G----MAKSMVAQFDKIVALLGIEPLL----DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPlaSLDL-PR-KRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2495741221 181 IVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:PRK11144 170 YLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-229 |
1.48e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.88 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS---QGGITFGGKAQEHAEIEEMVAAGM 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQ---ERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 159 RLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-166 |
1.56e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVaag 80
Cdd:COG4525 4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLaPSSGEITLDGVPVTGPGADRGV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 mnlVPEKRELFAEMTVEDNLMLG-------AFDRYRRGlrdqDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRA 153
Cdd:COG4525 81 ---VFQKDALLPWLNVLDNVAFGlrlrgvpKAERRARA----EELLALV-----GLADFARRRIWQLSGGMRQRVGIARA 148
|
170
....*....|...
gi 2495741221 154 LMAKPRLLMLDEP 166
Cdd:COG4525 149 LAADPRFLLMDEP 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-238 |
2.17e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQERRA--QLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSsdKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDpRVVEVYLG 238
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED-SLIEMMVG 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-231 |
2.30e-20 |
|
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: 89.36 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY-----------DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKaqehaEI 73
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQ-----DL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 74 EEMVAAGMNlvPEKREL-------FA----EMTVEdnlmlgafdryrrglrdqdQTLAEVFEL-FPRL--QERRAQLAGT 139
Cdd:COG4172 350 DGLSRRALR--PLRRRMqvvfqdpFGslspRMTVG-------------------QIIAEGLRVhGPGLsaAERRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 L-----------------SGGERQMLAVGRALMAKPRLLMLDEPSLGLaPRIVRevFRIVARLR----EMGVSILLIEQN 198
Cdd:COG4172 409 LeevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSAL-DVSVQ--AQILDLLRdlqrEHGLAYLFISHD 485
|
250 260 270
....*....|....*....|....*....|...
gi 2495741221 199 ARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:COG4172 486 LAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-232 |
2.96e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 3 AKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHA---EIEEMVA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGDDVEALsarAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AgmnlVPEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQERR--AQLAGTLSGGERQMLAVGRALMA 156
Cdd:PRK09536 81 S----VPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQfaDRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRV 232
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-195 |
3.00e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 14 AYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGitfggkaqehaEIEEMVAAGMNLVPEKRELFAE 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-----------TVRRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 M--TVEDNLMLGAFDR---YRRGLRDQDQTLAEVFELFPRLQERRAQLaGTLSGGERQMLAVGRALMAKPRLLMLDEPSL 168
Cdd:NF040873 70 LplTVRDLVAMGRWARrglWRRLTRDDRAAVDDALERVGLADLAGRQL-GELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*..
gi 2495741221 169 GLAPRIVREVFRIVARLREMGVSILLI 195
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVV 175
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
3.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAE---IEE 75
Cdd:PRK13636 1 MEDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILkPSSGRILFDGKPIDYSRkglMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 MVAAGMNLVPEKRELFAEMTVED------NLMLGAFDRYRRGLRDQDQTLAEVFELFPrlqerraqlAGTLSGGERQMLA 149
Cdd:PRK13636 81 RESVGMVFQDPDNQLFSASVYQDvsfgavNLKLPEDEVRKRVDNALKRTGIEHLKDKP---------THCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 150 VGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQ 228
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
....*
gi 2495741221 229 DPRVV 233
Cdd:PRK13636 232 EKEML 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-228 |
3.45e-20 |
|
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: 85.60 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 23 GVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVaagmnlVPEKRELFAEMTVEDNLM 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 102 LgAFDRYRRGLR--DQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPsLGLAPRIVREVF 179
Cdd:TIGR01184 77 L-AVDRVLPDLSksERRAIVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP-FGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 180 --RIVARLREMGVSILLIEQNARAALQVADYAYVLETgtvtleGPAAKVAQ 228
Cdd:TIGR01184 154 qeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTN------GPAANIGQ 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-180 |
3.74e-20 |
|
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: 88.96 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkAQEHAEIEEMVAAGMNL 83
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQGEVTLDG-VPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEmTVEDNLMLGAFDRyrrglrdQDQTLAEVFE---LFPRLQERRAQL-------AGTLSGGERQMLAVGRA 153
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDA-------TDEELWAALErvgLADWLRALPDGLdtvlgegGARLSGGERQRLALARA 485
|
170 180
....*....|....*....|....*..
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFR 180
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLE 512
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
4.04e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI--MGVLPSQ----GGITFGGK-------- 66
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitGSIVYNGHniysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 67 -AQEHAEIeEMVAAGMNLVPekrelfaeMTVEDNLMLGafdrYR-RGLRDQdQTLAEVFE-------LFPRLQERRAQLA 137
Cdd:PRK14239 81 tVDLRKEI-GMVFQQPNPFP--------MSIYENVVYG----LRlKGIKDK-QVLDEAVEkslkgasIWDEVKDRLHDSA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 138 GTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQVAD 207
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISD 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-221 |
4.51e-20 |
|
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: 85.33 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD--KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHAEIEemvaA 79
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLDGtdiRQLDPADLR----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEmTVEDNLMLGA-FDRYRRGLRdqDQTLAEVFELFPR--------LQERRAQlagtLSGGERQMLAV 150
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITLGApLADDERILR--AAELAGVTDFVNKhpngldlqIGERGRG----LSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVRevfRIVARLREMGVSILLIEQNAR-AALQVADYAYVLETGTVTLEG 221
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQLLGDKTLIIITHRpSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-238 |
5.60e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 15 YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGvLPSQ--GGITFGGK--AQEHAEiEEMVAagmnLVPEKREL 90
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQtsGHIRFHGTdvSRLHAR-DRKVG----FVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 91 FAEMTVEDNLMLG--AFDRYRR----GLRDQDQTLAEVFELfPRLQERR-AQlagtLSGGERQMLAVGRALMAKPRLLML 163
Cdd:PRK10851 86 FRHMTVFDNIAFGltVLPRRERpnaaAIKAKVTQLLEMVQL-AHLADRYpAQ----LSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP--RVVEVYLG 238
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPatRFVLEFMG 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-217 |
5.72e-20 |
|
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: 84.14 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS---QGGITFGGKAQEHAEIEEMVAagmnLVPEKRELFAEMTVE 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVLINGRPLDKRSFRKIIG----YVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 98 DNLMLGafdryrrglrdqdqtlaevfelfprlqerrAQLAGtLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVRE 177
Cdd:cd03213 101 ETLMFA------------------------------AKLRG-LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2495741221 178 VFRIVARLREMGVSILLIEQNARAAL-QVADYAYVLETGTV 217
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPSSEIfELFDKLLLLSQGRV 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-221 |
5.81e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 88.25 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 18 VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRELFAEMTV 96
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYqKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 97 EDNLMLGafdRY-RRGL-RDQDQTLAEVFELFPRLQ---ERRAQLAgTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLA 171
Cdd:PRK10982 91 MDNMWLG---RYpTKGMfVDQDKMYRDTKAIFDELDidiDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 172 PRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETG----TVTLEG 221
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGqwiaTQPLAG 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
6.25e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEMTVEDNLMLGAFDRYR---------RGLRDQDQTLAEVFELFPRLQErraqLAGTLSGGERQMLAV 150
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDE----KVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-228 |
1.02e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSaklLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSaIMGVL--PSQGGIT-------FGGKAQEHA 71
Cdd:PRK11124 1 MS---IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLemPRSGTLNiagnhfdFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 72 EIEEMVAAGMnlVPEKRELFAEMTVEDNLmLGAFDRYRrGLrDQDQTLAEVFELFPRLqeRRAQLAGT----LSGGERQM 147
Cdd:PRK11124 77 IRELRRNVGM--VFQQYNLWPHLTVQQNL-IEAPCRVL-GL-SKDQALARAEKLLERL--RLKPYADRfplhLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 148 LAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVA 227
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFT 229
|
.
gi 2495741221 228 Q 228
Cdd:PRK11124 230 Q 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
1.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAE---IEEMVAA 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRELFAEmTVEDNLmlgAFDRYRRGLrDQDQTLAEVFELFPRLQ----ERRAqlAGTLSGGERQMLAVGRALM 155
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDV---AFGPLNLGL-SKEEVEKRVKEALKAVGmegfENKP--PHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVE 234
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-208 |
1.30e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI--MGVLPSQ----GGITFGGKAQEHAEIE-EMVA 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEvrveGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNLVPEKRELFAeMTVEDNLMLGAFD---RYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALM 155
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADY 208
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDF 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-217 |
1.40e-19 |
|
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: 87.19 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLrVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQ--GGITFGGKAQEHAEIEEMVA 78
Cdd:TIGR02633 257 ILEARNL-TCWDvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfeGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNLVPEKRE---LFAEMTVEDNLMLGAFDRY-RRGLRDQDQTLAEVFELFPRLQERRAQ--LA-GTLSGGERQMLAVG 151
Cdd:TIGR02633 336 AGIAMVPEDRKrhgIVPILGVGKNITLSVLKSFcFKMRIDAAAELQIIGSAIQRLKVKTASpfLPiGRLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-225 |
2.36e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 25 SLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaQEHAeieemvaagmNLVPEKR---------ELFAEM 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLtPASGSLTLNG--QDHT----------TTPPSRRpvsmlfqenNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 95 TVEDNLMLGafdrYRRGLR---DQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLA 171
Cdd:PRK10771 87 TVAQNIGLG----LNPGLKlnaAQREKLHAIARQM-GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 172 PRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAK 225
Cdd:PRK10771 162 PALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-230 |
2.51e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.77 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGkaQEHAeieemvaagmNL 83
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDG--QDIT----------HV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRE---------LFAEMTVEDNLmlgAFdryrrGLRDQDQTLAEVfelFPRLQE--RRAQLAGT-------LSGGER 145
Cdd:PRK09452 82 PAENRHvntvfqsyaLFPHMTVFENV---AF-----GLRMQKTPAAEI---TPRVMEalRMVQLEEFaqrkphqLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
....*.
gi 2495741221 225 KVAQDP 230
Cdd:PRK09452 231 EIYEEP 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-166 |
3.28e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 8 VRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQG------GITFGGKAQEHAEIEEM---- 76
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELePDSGevsipkGLRIGYLPQEPPLDDDLtvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 77 -VAAG----MNLVPEKRELFAEMTVEDNLMlgafDRYrrglrdqdqtlAEVFELFPRLQ----ERRA------------- 134
Cdd:COG0488 81 tVLDGdaelRALEAELEELEAKLAEPDEDL----ERL-----------AELQEEFEALGgweaEARAeeilsglgfpeed 145
|
170 180 190
....*....|....*....|....*....|....
gi 2495741221 135 --QLAGTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:COG0488 146 ldRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
3.64e-19 |
|
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: 85.89 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKT-TLLSaIMGVLPS-----QGGITFGGkaqeh 70
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPDpaahpSGSILFDG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 71 aeiEEMVAAgmnlvPEK--REL--------FAE--------MTVEDNLM--LgafdRYRRGLRDQdQTLAEVFELF---- 126
Cdd:COG4172 76 ---QDLLGL-----SERelRRIrgnriamiFQEpmtslnplHTIGKQIAevL----RLHRGLSGA-AARARALELLervg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 127 -PRLQERRAQLAGTLSGGERQ--MLAVgrALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAA 202
Cdd:COG4172 143 iPDPERRLDAYPHQLSGGQRQrvMIAM--ALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*....
gi 2495741221 203 LQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:COG4172 221 RRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-236 |
7.37e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMvAAGMNLVP 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGeVLVDGLDVATTPSREL-AKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 86 EKRELFAEMTVEDnlmLGAFDRY-----RRGLRDQ---DQTLaEVFELFPrLQERRaqlAGTLSGGERQmlavgRALMA- 156
Cdd:COG4604 82 QENHINSRLTVRE---LVAFGRFpyskgRLTAEDReiiDEAI-AYLDLED-LADRY---LDELSGGQRQ-----RAFIAm 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 157 ----KPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLI--EQNARAALqvADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:COG4604 149 vlaqDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVlhDINFASCY--ADHIVAMKDGRVVAQGTPEEIITP 226
|
....*..
gi 2495741221 230 PRVVEVY 236
Cdd:COG4604 227 EVLSDIY 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-197 |
9.84e-19 |
|
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: 81.55 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 17 KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSqGGITFG-----GKAQEHAEIEEMVAagmnLVPEKRELF 91
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGqilfnGQPRKPDQFQKCVA----YVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 92 AEMTVEDNLMLGAFDRYRRGLRD-QDQTLAEVFELfPRLQERRA--QLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSL 168
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDaIRKKRVEDVLL-RDLALTRIggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|
gi 2495741221 169 GLAPRIVREVFRIVARLREMGVSILL-IEQ 197
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILtIHQ 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
1.03e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 82.76 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHA---EIE 74
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVLSEEtvwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVaaGM---NlvPEKRelFAEMTVEDNLmlgAFDRYRRGL-RDQ-----DQTLAEVfelfpRLQERRAQLAGTLSGGER 145
Cdd:PRK13635 81 RQV--GMvfqN--PDNQ--FVGATVQDDV---AFGLENIGVpREEmvervDQALRQV-----GMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 146 QMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQvADYAYVLETGTVTLEGPAA 224
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
250
....*....|....*.
gi 2495741221 225 KV-AQDPRVVEVYLGL 239
Cdd:PRK13635 226 EIfKSGHMLQEIGLDV 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-236 |
1.33e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRELFAeMTVEDNLMLG 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 104 AFDRYRrgLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQ-------MLAVGRALMAKPRLLMLDEPSLGLapRIVR 176
Cdd:PRK03695 94 QPDKTR--TEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSL--DVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 177 EV--FRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVY 236
Cdd:PRK03695 169 QAalDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-231 |
1.38e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGvL--PSQGGITFGGKaqehaEI-----E 74
Cdd:COG1135 2 IELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LerPTSGSVLVDGV-----DLtalseR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAA----GM-----NLVPEKrelfaemTVEDNLMLgafdryrrGLR----DQDQTLAEVFELFPR--LQERRAQLAGT 139
Cdd:COG1135 76 ELRAArrkiGMifqhfNLLSSR-------TVAENVAL--------PLEiagvPKAEIRKRVAELLELvgLSDKADAYPSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250
....*....|...
gi 2495741221 219 LEGPAAKVAQDPR 231
Cdd:COG1135 221 EQGPVLDVFANPQ 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-242 |
1.48e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIEEmV 77
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIaPDHGEILFDGEnipAMSRSRLYT-V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AAGMNLVPEKRELFAEMTVEDNLmlgAFDryrrgLRDQDQTLAEVFELFPRLQERRAQLAGT-------LSGGERQMLAV 150
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNV---AYP-----LREHTQLPAPLLHSTVMMKLEAVGLRGAaklmpseLSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLRE-MGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVA-- 227
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQan 234
|
250
....*....|....*
gi 2495741221 228 QDPRVVEVYLGLGHG 242
Cdd:PRK11831 235 PDPRVRQFLDGIADG 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-239 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 8 VRDLRVAY---DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG--ITFGGKAQEHAEIEEmVAAGMN 82
Cdd:PRK13644 2 IRLENVSYsypDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvLVSGIDTGDFSKLQG-IRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKREL-FAEMTVEDNLMLGAFD------RYRRGLrdqDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALM 155
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENlclppiEIRKRV---DRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARaALQVADYAYVLETGTVTLEGPAAKVAQDPRVveV 235
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSL--Q 229
|
....
gi 2495741221 236 YLGL 239
Cdd:PRK13644 230 TLGL 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-229 |
1.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFG-------GKAQEHAEIEEMVAAGMNLvPEKrELF 91
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGdivvsstSKQKEIKPVRKKVGVVFQF-PES-QLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 92 AEMTVEDNlmlgAFDRYRRGL--RDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLG 169
Cdd:PRK13643 99 EETVLKDV----AFGPQNFGIpkEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 170 LAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-222 |
2.20e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.68 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDK-VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEE---MVAag 80
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRILIDGVDIRDLTLESlrrQIG-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 mnLVPEKRELFAeMTVEDNLMLGafdryrrglrDQDQTLAEVFE------------LFP-----RLQERraqlAGTLSGG 143
Cdd:COG1132 418 --VVPQDTFLFS-GTIRENIRYG----------RPDATDEEVEEaakaaqahefieALPdgydtVVGER----GVNLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 144 ERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQnaR-AALQVADYAYVLETGTVTLEGP 222
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH--RlSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-217 |
2.46e-18 |
|
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: 79.57 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEA--VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHAEIEEMVAA 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVRLDGadiSQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmnlVPEKRELFAEmTVEDNLmlgafdryrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPR 159
Cdd:cd03246 81 ----LPQDDELFSG-SIAENI---------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 160 LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADYAYVLETGTV 217
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-217 |
2.81e-18 |
|
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: 80.81 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqEHAEIEEM-VAAGMNLVPEKRELFAEMTVE 97
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePTSGEIFIDGE--DIREQDPVeLRRKIGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 98 DN----LMLGAFDRYRRGLRdQDQTLAEVfELFPrlQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPr 173
Cdd:cd03295 94 ENialvPKLLKWPKEKIRER-ADELLALV-GLDP--AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2495741221 174 IVR-----EVFRIvarLREMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03295 169 ITRdqlqeEFKRL---QQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-236 |
2.96e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAydkvEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAGMNLVP 85
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 86 EKRELFAeMTVEDNLMLGafdrYRRGLRDQ--DQTLAEVFELFpRLQERRAQLAGTLSGGERQ-------MLAVGRALMA 156
Cdd:COG4138 77 QQSPPFA-MPVFQYLALH----QPAGASSEavEQLLAQLAEAL-GLEDKLSRPLTQLSGGEWQrvrlaavLLQVWPTINP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVY 236
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-166 |
3.03e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.90 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMVaagmnl 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTVEDN----LMLGAFDRYRRGLRDQdQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPR 159
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNvafgLQLAGVEKMQRLEIAH-QMLKKV-----GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
....*..
gi 2495741221 160 LLMLDEP 166
Cdd:PRK11248 149 LLLLDEP 155
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-220 |
4.96e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEE--MVAAGMNL 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtrLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRelfaemtVEDNLMLGAFDRYRRGLRdqdQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:PRK11247 93 LPWKK-------VIDNVGLGLKGQWRDAAL---QALAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 164 DEPsLGLAPRIVR-EVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLE 220
Cdd:PRK11247 158 DEP-LGALDALTRiEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-200 |
6.15e-18 |
|
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: 79.37 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 18 VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEM--VAAGMNLVPEKRELFAEM 94
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLRGRAIpyLRRKIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 95 TVEDNLMLgAFDRYRRGLRDQDQTLAEVFELFPrLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRI 174
Cdd:cd03292 94 NVYENVAF-ALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|....*.
gi 2495741221 175 VREVFRIVARLREMGVSILLIEQNAR 200
Cdd:cd03292 172 TWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-221 |
2.05e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.16 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAG--KTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMtvEDNLMLG-AFDRYRRGLRDQDQTLAEVFELfprlQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:NF000106 94 R*GRRESFSGR--ENLYMIGr*LDLSRKDARARADELLERFSL----TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-229 |
2.29e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS---QGGITFGGKAQEHAEIEEMVAAGM 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFAEMTVEDNLMLGAfDRYRRGLRDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKPR 159
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGN-ERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 160 LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTV--TLEGPAAKVAQD 229
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTieTLDCRADEVTED 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-208 |
3.43e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLL---SAIMGVLPS---QGGITFGGKAQEHAEIEEM-V 77
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrvEGKVTFHGKNLYAPDVDPVeV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AAGMNLVPEKRELFAEmTVEDNLMLGA-FDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGArINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREMgVSILLIEQNARAALQVADY 208
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDM 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-216 |
4.79e-17 |
|
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: 77.09 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 17 KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITF---GG-----KAQEHaEIEEM-------VAAG 80
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILVrhdGGwvdlaQASPR-EILALrrrtigyVSQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEK--RELFAEMTVEdnlmlgafdryrRGLrDQDQTLAEVFELFPRLQ--ERRAQLA-GTLSGGERQMLAVGRALM 155
Cdd:COG4778 102 LRVIPRVsaLDVVAEPLLE------------RGV-DREEARARARELLARLNlpERLWDLPpATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 156 AKPRLLMLDEP--SLGLAPRIVreVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGT 216
Cdd:COG4778 169 ADPPLLLLDEPtaSLDAANRAV--VVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-242 |
4.87e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAqeHAEIEemVAAG 80
Cdd:COG1134 23 SLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePTSGRVEVNGRV--SALLE--LGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNlvpekrelfAEMTVEDNLMLGA----FDRyrrglRDQDQTLAEVFElFPRLQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:COG1134 99 FH---------PELTGRENIYLNGrllgLSR-----KEIDEKFDEIVE-FAELGDFIDQPVKTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 157 KPRLLMLDEpslGLApriVR-EVFRI--VARLREM---GVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKvaqdp 230
Cdd:COG1134 164 DPDILLVDE---VLA---VGdAAFQKkcLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE----- 232
|
250
....*....|..
gi 2495741221 231 rVVEVYLGLGHG 242
Cdd:COG1134 233 -VIAAYEALLAG 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-216 |
6.37e-17 |
|
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: 76.35 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVE-----AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGK----AQEhAEIee 75
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGsVSVPGSiayvSQE-PWI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 mvaagMNlvpekrelfaeMTVEDNLMLGA-FD--RYRRGLR----DQDqtlaevFELFP-----RLQERraqlaG-TLSG 142
Cdd:cd03250 78 -----QN-----------GTIRENILFGKpFDeeRYEKVIKacalEPD------LEILPdgdltEIGEK-----GiNLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 143 GERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFR--IVARLREmGVSILLIEQNARAALQvADYAYVLETGT 216
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-231 |
6.84e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAklLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI-MGVLPSQGGITFGgkaQEHAEIEEMVAA 79
Cdd:PRK11264 1 MSA--IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIRVG---DITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKRE----------LFAEMTVEDNLMLGAFDRYRRglrDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQM 147
Cdd:PRK11264 76 QKGLIRQLRQhvgfvfqnfnLFPHRTVLENIIEGPVIVKGE---PKEEATARARELLAKvgLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 148 LAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVA 227
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
....
gi 2495741221 228 QDPR 231
Cdd:PRK11264 233 ADPQ 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-194 |
8.63e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 15 YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaqehaeieemvaagmnLVPEKRE---- 89
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvPTSGEVRVLG-----------------YVPFKRRkefa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 ------------LFAEMTVEDNL-MLGAF-----DRYRRGLRdqdqTLAEVFELFPRLQerraQLAGTLSGGERqM---L 148
Cdd:COG4586 95 rrigvvfgqrsqLWWDLPAIDSFrLLKAIyripdAEYKKRLD----ELVELLDLGELLD----TPVRQLSLGQR-MrceL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 149 AVgrALMAKPRLLMLDEPSLGL---APRIVREvFrivarLREM----GVSILL 194
Cdd:COG4586 166 AA--ALLHRPKILFLDEPTIGLdvvSKEAIRE-F-----LKEYnrerGTTILL 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-226 |
1.22e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAE-----IEEMVA 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLDYSKrgllaLRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNlVPEKRELFAEMTVE-----DNLMLGAFDRYRRglRDQDQTLAEVfelfprlQERRAQLAGTLSGGERQMLAVGRA 153
Cdd:PRK13638 81 TVFQ-DPEQQIFYTDIDSDiafslRNLGVPEAEITRR--VDEALTLVDA-------QHFRHQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-195 |
1.79e-16 |
|
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: 78.10 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEiEEMVAAGMNL 83
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTEGSIAVNGVPLADAD-ADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEmTVEDNLMLGAFDRYRRGLRD--QDQTLAEVFELFPRLQERRAQLAGT-LSGGERQMLAVGRALMAKPRL 160
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREalERAGLDEFVAALPQGLDTPIGEGGAgLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*
gi 2495741221 161 LMLDEPSLGLAPRIVREVFRIVARLREmGVSILLI 195
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV 513
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-194 |
2.07e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEhaeiEEMVAAGMNLV 84
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDID----DPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLmlgafdRYRRGLRDQDQTL----AEVFELfPRLQERRaqlAGTLSGGERQMLAVGRALMAKPRL 160
Cdd:PRK13539 79 GHRNAMKPALTVAENL------EFWAAFLGGEELDiaaaLEAVGL-APLAHLP---FGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....
gi 2495741221 161 LMLDEPSLGLAPRIVREVFRIVARLREMGVSILL 194
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-221 |
2.41e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.13 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIE---EMVAAGMNLVPEKRELFAEMT 95
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLpPTSGTVLVGGK-----DIEtnlDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLMLGAFDRYRRglRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIV 175
Cdd:TIGR01257 1020 VAEHILFYAQLKGRS--WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2495741221 176 REVFRIVARLREmGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:TIGR01257 1098 RSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-229 |
2.57e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKA----QEHAEIEEmVAAGMNLV---PEKrELF 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLitstSKNKDIKQ-IRKKVGLVfqfPES-QLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 92 AEMTVEDNlmlgAFDRYRRGLRDQD-QTLA-EVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLG 169
Cdd:PRK13649 100 EETVLKDV----AFGPQNFGVSQEEaEALArEKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 170 LAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-172 |
2.86e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.46 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI--MGVL-PSQ---GGITFGGkaqehaeiEEMVAA 79
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLiPGArveGEILLDG--------EDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPEKREL---------FAeMTVEDNLMLGAfdRYrRGLRDQDQtLAEVFE--LfprlqeRRAQL-----------A 137
Cdd:COG1117 84 DVDVVELRRRVgmvfqkpnpFP-KSIYDNVAYGL--RL-HGIKSKSE-LDEIVEesL------RKAALwdevkdrlkksA 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2495741221 138 GTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAP 172
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-221 |
6.77e-16 |
|
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: 74.11 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaeIEEMVAA 79
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYpPDSGTVTVRGR------VSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPekrelfaEMTVEDNL-MLGAFDRYRRglRDQDQTLAEVFElFPRLQERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:cd03220 92 GGGFNP-------ELTGRENIyLNGRLLGLSR--KEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 159 RLLMLDEpslGLA---PRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:cd03220 162 DILLIDE---VLAvgdAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-222 |
8.20e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 23 GVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS----QGGITFGGKAQEHAEIEEMVAagmnLVPEKRELFAEMTVED 98
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkgSGSVLLNGMPIDAKEMRAISA----YVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 99 NLMLGAFDRYRRGLrDQDQTLAEVFELFPRLQERRAQ--LAGT------LSGGERQMLAVGRALMAKPRLLMLDEPSLGL 170
Cdd:TIGR00955 119 HLMFQAHLRMPRRV-TKKEKRERVDEVLQALGLRKCAntRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 171 APRIVREVFRIVARLREMGVSILL-IEQNARAALQVADYAYVLETGTVTLEGP 222
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-222 |
8.32e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAY-DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMVA 78
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfVRLASGKISILGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 agmnLVPEKREL--FAEMTVEDNLMLGAFDRY---RRGLRDQDQTLAEVFELFPRLQERRAQLaGTLSGGERQMLAVGRA 153
Cdd:PRK15056 82 ----YVPQSEEVdwSFPVLVEDVVMMGRYGHMgwlRRAKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 154 LMAKPRLLMLDEPSLGLApriVREVFRIVARLREM---GVSILLIEQNARAALQVADYAyVLETGTVTLEGP 222
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVD---VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGP 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-194 |
9.01e-16 |
|
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: 73.16 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAqeHAEIEEMVAAGMNLV 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGTP--LAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNL-MLGAFDRYRRglRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:TIGR01189 79 GHLPGLKPELSALENLhFWAAIHGGAQ--RTIEDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|.
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILL 194
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-244 |
9.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 19 EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG-----KAQEHAEIEEMVAagmnLV---PEkRE 89
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGvditdKKVKLSDIRKKVG----LVfqyPE-YQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 LFAEmTVEDNLmlgAFDRYRRGLRDqDQTLAEVFELFPRLQERRAQLAGT----LSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:PRK13637 96 LFEE-TIEKDI---AFGPINLGLSE-EEIENRVKRAMNIVGLDYEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 166 PSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDprvVEVYLGLGHGAP 244
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE---VETLESIGLAVP 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-230 |
1.11e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGgkaqehaeiEEMVAAGM---NLVPEKR------- 88
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTIG---------ERVITAGKknkKLKPLRKkvgivfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 89 ----ELFAEmTVEDNLmlgAFDRYRRGLRDQD--QTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:PRK13634 93 fpehQLFEE-TVEKDI---CFGPMNFGVSEEDakQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-217 |
1.60e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 9 RDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAqehaeieemvaagMNLV-PE 86
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKR-------------MNDVpPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 87 KRE---------LFAEMTVEDNLMLG-AFDRYRRGLRDQD-QTLAEVFELfPRLQERRAQlagTLSGGERQMLAVGRALM 155
Cdd:PRK11000 74 ERGvgmvfqsyaLYPHLSVAENMSFGlKLAGAKKEEINQRvNQVAEVLQL-AHLLDRKPK---ALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 156 AKPRLLMLDEP--SLGLAPRIvreVFRI-VARL-REMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:PRK11000 150 AEPSVFLLDEPlsNLDAALRV---QMRIeISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-229 |
1.63e-15 |
|
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: 75.22 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVE-----AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 G-------MNLVPEKRELFAEMTVEDNLmlgafdryrrglrdqdqTLAEVFELFPRLQERRA------------------ 134
Cdd:TIGR03269 359 GrgrakryIGILHQEYDLYPHRTVLDNL-----------------TEAIGLELPDELARMKAvitlkmvgfdeekaeeil 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 135 -QLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVL 212
Cdd:TIGR03269 422 dKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAReEMEQTFIIVSHDMDFVLDVCDRAALM 501
|
250
....*....|....*..
gi 2495741221 213 ETGTVTLEGPAAKVAQD 229
Cdd:TIGR03269 502 RDGKIVKIGDPEEIVEE 518
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-221 |
2.42e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-----PSQGGITFGGKAQEHAEIEEMVA- 78
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELLGRTVQREGRLARDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 --AGMNLVPEKRELFAEMTVEDNLMLGAFDR---YRRGLRdqdqtlaevfeLFPRLQERRA--------------QLAGT 139
Cdd:PRK09984 84 srANTGYIFQQFNLVNRLSVLENVLIGALGStpfWRTCFS-----------WFTREQKQRAlqaltrvgmvhfahQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAP---RIVREVFRIVArlREMGVSILLIEQNARAALQVADYAYVLETGT 216
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPesaRIVMDTLRDIN--QNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
....*
gi 2495741221 217 VTLEG 221
Cdd:PRK09984 231 VFYDG 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-245 |
3.15e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLrvaydKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK15439 268 VLTVEDL-----TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGrIMLNGKEINALSTAQRLARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRE---LFAEMTVEDNLMlgAFDRYRRGLRDQDQTLAEVFELFprlqeRRA---------QLAGTLSGGERQMLAVG 151
Cdd:PRK15439 343 LPEDRQssgLYLDAPLAWNVC--ALTHNRRGFWIKPARENAVLERY-----RRAlnikfnhaeQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDpR 231
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD-T 494
|
250
....*....|....
gi 2495741221 232 VVEVYLGLGHGAPA 245
Cdd:PRK15439 495 IMRLAFGEHQAQEA 508
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-195 |
3.37e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGgitfggkaqehaEIEEMVAAGMNL 83
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEG------------VIKRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEMTvednLMLGAFDRYRRGLRDQDqtlaevfeLFPRLQERRA-----QLAGTLSGGERQMLAVGRALMAKP 158
Cdd:PRK09544 72 VPQKLYLDTTLP----LTVNRFLRLRPGTKKED--------ILPALKRVQAghlidAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 2495741221 159 RLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLI 195
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRrELDCAVLMV 177
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-229 |
3.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDK-----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTL---LSAIMgvLPSQGGITF---GGKAQEHAEIE 74
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL--LPDTGTIEWifkDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAAGMNLVPEKR----------------------ELFaEMTVEDNLMLGAFDRyrrGLRDQD--QTLAEVFELFPRLQ 130
Cdd:PRK13651 81 EKVLEKLVIQKTRFkkikkikeirrrvgvvfqfaeyQLF-EQTIEKDIIFGPVSM---GVSKEEakKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 131 ERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAY 210
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*....
gi 2495741221 211 VLETGTVTLEGPAAKVAQD 229
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSD 255
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-231 |
3.55e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.65 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAA 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLaPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmnlvpEKRELF--------------------AEMTVEDNLMlGAFDRYRRGLRDQDQTLAEVFELFPrlqERRAQLAGT 139
Cdd:PRK11701 82 ------ERRRLLrtewgfvhqhprdglrmqvsAGGNIGERLM-AVGARHYGDIRATAGDWLERVEIDA---ARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250
....*....|...
gi 2495741221 219 LEGPAAKVAQDPR 231
Cdd:PRK11701 232 ESGLTDQVLDDPQ 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
5.15e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKV----EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS------QGGITFGGKAQEH 70
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 71 AEIEEMVAAGMNLVPEkreLFAEMTVEDNLM------LGAFDRYRRGLRdQDQTLAEVFELFPRLQERRA--QLAG---T 139
Cdd:PRK15134 81 ASEQTLRGVRGNKIAM---IFQEPMVSLNPLhtlekqLYEVLSLHRGMR-REAARGEILNCLDRVGIRQAakRLTDyphQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETG 215
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-166 |
8.04e-15 |
|
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: 71.31 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGkaQE-HAEIE 74
Cdd:COG4181 4 SSAPIIELRGLTKTVGtgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAG--QDlFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAA----GMNLVPEKRELFAEMTVEDNLML--------GAFDRYRRGLrdqdqtlAEVfelfpRLQERRAQLAGTLSG 142
Cdd:COG4181 82 DARARlrarHVGFVFQSFQLLPTLTALENVMLplelagrrDARARARALL-------ERV-----GLGHRLDHYPAQLSG 149
|
170 180
....*....|....*....|....
gi 2495741221 143 GERQMLAVGRALMAKPRLLMLDEP 166
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEP 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-230 |
8.48e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 8.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMvaaGMNLVPEKRELFAEMTVEDNLml 102
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKPTEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPHMSLGENV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 103 gafdRYrrGLRDQDQTLAEVFElfpRLQERRA--QLAG-------TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAP- 172
Cdd:PRK11432 100 ----GY--GLKMLGVPKEERKQ---RVKEALElvDLAGfedryvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDAn 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 173 --RIVREvfrivaRLREM----GVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK11432 171 lrRSMRE------KIRELqqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-217 |
8.78e-15 |
|
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: 71.52 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGK---AQEHAEIEEMVAAGMNLVPEKRELFAEMT 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPTSGKVLIDGQdiaAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLMLG-------AFDRYRRGlrdqdqtlAEVFELFPrLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSL 168
Cdd:cd03294 119 VLENVAFGlevqgvpRAEREERA--------AEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2495741221 169 GLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:cd03294 190 ALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-231 |
1.36e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 12 RVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVAA----GM----- 81
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLeRPTSGRVLVDGQDLTALSEKELRKArrqiGMifqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKrelfaemTVEDNLML-----GafdryrrglRDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRAL 154
Cdd:PRK11153 92 NLLSSR-------TVFDNVALplelaG---------TPKAEIKARVTELLELvgLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 155 MAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-165 |
1.40e-14 |
|
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: 70.33 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVE-AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHAEIEEMVAagm 81
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGidiRDISRKSLRSMIG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nLVPEKRELFAEmTVEDNLMLGafdryrrglrDQDQTLAEVFELFPRLQ-----------------ERraqlAGTLSGGE 144
Cdd:cd03254 81 -VVLQDTFLFSG-TIMENIRLG----------RPNATDEEVIEAAKEAGahdfimklpngydtvlgEN----GGNLSQGE 144
|
170 180
....*....|....*....|.
gi 2495741221 145 RQMLAVGRALMAKPRLLMLDE 165
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDE 165
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-165 |
1.80e-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: 72.46 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 19 EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAgMNLVPEKRELFAEmTVE 97
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDIDRHTLRQF-INYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 98 DNLMLGAfdryRRGLRDQD----QTLAEV---FELFPR-LQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:TIGR01193 566 ENLLLGA----KENVSQDEiwaaCEIAEIkddIENMPLgYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-170 |
1.85e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRV-AYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGkaQEHAEIEEMV-AAGMNL 83
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKING--IELRELDPESwRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEmTVEDNLMLGAFDryrrgLRDQ--DQTL--AEVFELFPRL--------QERraqlAGTLSGGERQMLAVG 151
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGNPD-----ASDEqlQQALenAWVSEFLPLLpqgldtpiGDQ----AAGLSVGQAQRLALA 497
|
170
....*....|....*....
gi 2495741221 152 RALMAKPRLLMLDEPSLGL 170
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASL 516
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-166 |
2.58e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.03 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD-KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIEE----MVAA 79
Cdd:PRK11650 4 LKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWIGGRVVNELEPADrdiaMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNLVPekrelfaEMTVEDNLMLGAfdRYRRGLRDQ-DQTLAEV---FELFPRLQERRAQlagtLSGGERQMLAVGRALM 155
Cdd:PRK11650 84 NYALYP-------HMSVRENMAYGL--KIRGMPKAEiEERVAEAariLELEPLLDRKPRE----LSGGQRQRVAMGRAIV 150
|
170
....*....|.
gi 2495741221 156 AKPRLLMLDEP 166
Cdd:PRK11650 151 REPAVFLFDEP 161
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-213 |
2.98e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.36 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAgMN 82
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDLRSS-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEmTVEDNLmlGAFDRYrrglrdqdqTLAEVFELFprlqeRRAQLAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--DPFDEY---------SDEEIYGAL-----RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 163 LDEP-------SLGLAPRIVREVFRivarlremGVSILLIEQNARAalqVADYAYVLE 213
Cdd:cd03369 149 LDEAtasidyaTDALIQKTIREEFT--------NSTILTIAHRLRT---IIDYDKILV 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-221 |
3.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 19 EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEM-----VAAGMNLV---PEkREL 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrLRKEIGLVfqfPE-YQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 91 FAEmTVEDNLmlgAFDRYRRGLRDQD--QTLAEVFEL--FPRLQERRAQLagTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:PRK13645 104 FQE-TIEKDI---AFGPVNLGENKQEayKKVPELLKLvqLPEDYVKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 167 SLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-166 |
3.28e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.53 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDK-----------VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQ 68
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVrgglfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 69 EHAEIEEMVA--AGMNLV---PekrelFA----EMTVEDnlMLG-AFDRYrrGLRDQDQTLAEVFELFPRLQERRAQL-- 136
Cdd:COG4608 83 TGLSGRELRPlrRRMQMVfqdP-----YAslnpRMTVGD--IIAePLRIH--GLASKAERRERVAELLELVGLRPEHAdr 153
|
170 180 190
....*....|....*....|....*....|.
gi 2495741221 137 -AGTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:COG4608 154 yPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-195 |
4.13e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD-------------KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKaqeh 70
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGK---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 71 aEIEEMVAAGMNlvpEKRE------------LFAEMTVEDNLM--LGAF--DRYRRGLRDQDQTLAEVFELFPRLQERRA 134
Cdd:PRK15079 84 -DLLGMKDDEWR---AVRSdiqmifqdplasLNPRMTIGEIIAepLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 135 QlagTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLI 195
Cdd:PRK15079 160 H---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFI 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-231 |
4.86e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-------PSQGGITFGGKaqEHAEIEEM-VAAGMNLVPEKRELFAEMT 95
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGK--DIFQIDAIkLRKEVGMVFQQPNPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLmlgAFDRYRRGLRDQDQTLAEVFE------LFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLG 169
Cdd:PRK14246 107 IYDNI---AYPLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 170 LAPRIVREVFRIVARLREMgVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-218 |
5.27e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAydKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREkSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRE---LFAEMTVEDNLMLGAFDRYRR--GLRDQDQTLAEVFELFPRLQER---RAQLAGTLSGGERQMLAVGRALM 155
Cdd:PRK10982 328 VTEERRstgIYAYLDIGFNSLISNIRNYKNkvGLLDNSRMKSDTQWVIDSMRVKtpgHRTQIGSLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 156 AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-237 |
5.89e-14 |
|
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: 70.60 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV---LPSQGGITFG-GKAQEHAEIEEMVAAGM 81
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIYHvALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 N-------LVPEKRE-------------------------LFAEMTVEDNLMLGAFDRYRRGlRDQDQTLAEVFELFpRL 129
Cdd:TIGR03269 81 PcpvcggtLEPEEVDfwnlsdklrrrirkriaimlqrtfaLYGDDTVLDNVLEALEEIGYEG-KEAVGRAVDLIEMV-QL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 130 QERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFR-IVARLREMGVSILLIEQNARAALQVADY 208
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270
....*....|....*....|....*....|
gi 2495741221 209 AYVLETGTVTLEGpaakvaqDP-RVVEVYL 237
Cdd:TIGR03269 239 AIWLENGEIKEEG-------TPdEVVAVFM 261
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-165 |
6.61e-14 |
|
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: 68.80 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHAEIEEMVAa 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGhdvRDYTLASLRRQIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 gmnLVPEKRELFAEmTVEDNLMLGAFDRYRRGLRDQDQtLAEVFELFPRLQERRAQLAG----TLSGGERQMLAVGRALM 155
Cdd:cd03251 80 ---LVSQDVFLFND-TVAENIAYGRPGATREEVEEAAR-AANAHEFIMELPEGYDTVIGergvKLSGGQRQRIAIARALL 154
|
170
....*....|
gi 2495741221 156 AKPRLLMLDE 165
Cdd:cd03251 155 KDPPILILDE 164
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-221 |
6.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.35 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHA-EIEEmvAAGMNLVPEKRELFAEM 94
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDGldtSDEENLwDIRN--KAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 95 TVEDNlmlgAFDRYRRGLrDQDQTLAEVFELFPR--LQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAP 172
Cdd:PRK13633 103 VEEDV----AFGPENLGI-PPEEIRERVDESLKKvgMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2495741221 173 RIVREVFRIVARL-REMGVSILLIEQNARAALQvADYAYVLETGTVTLEG 221
Cdd:PRK13633 178 SGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-234 |
2.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI------MGVLPSQGGITFGGKA--QEHAEI 73
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYSGDVLLGGRSifNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 74 EEMVAAGMNLvpeKRELFAEMTVEDNLMLGAFDRY---RRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAV 150
Cdd:PRK14271 98 EFRRRVGMLF---QRPNPFPMSIMDNVLAGVRAHKlvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMgVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
....
gi 2495741221 231 RVVE 234
Cdd:PRK14271 254 KHAE 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-239 |
2.67e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.88 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 19 EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG-------KAQEHAEIEEMVaaGMNLVPEKREL 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVTVDDitithktKDKYIRPVRKRI--GMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 91 FaEMTVEDNLMLGAfdryRRGLRDQDQTLAEVFEL-----FPR--LQERRAQLagtlSGGERQMLAVGRALMAKPRLLML 163
Cdd:PRK13646 99 F-EDTVEREIIFGP----KNFKMNLDEVKNYAHRLlmdlgFSRdvMSQSPFQM----SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEG-PAAKVAQDPRVVEVYLGL 239
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPKELFKDKKKLADWHIGL 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-204 |
2.81e-13 |
|
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: 69.17 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAgMNL 83
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKA-FGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEmTVEDNLmlgafDRYRRGLRDQDQTLAE------VFELFP-RLQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNL-----DPYEQWSDEEIWKVAEevglksVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2495741221 157 KPRLLMLDEPSLGLAPrIVREVFRIVARLREMGVSILLIEQNARAALQ 204
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-217 |
3.49e-13 |
|
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: 67.19 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY-DKVEAV-SGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAgMNL 83
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKA-FGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFAEmTVEDNLmlgafDRYRRGLRDQDQTLAE------VFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMA 156
Cdd:cd03289 82 IPQKVFIFSG-TFRKNL-----DPYGKWSDEEIWKVAEevglksVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 157 KPRLLMLDEPSLGLAPrIVREVFRIVARLREMGVSILLIEQNARAALQVADYaYVLETGTV 217
Cdd:cd03289 156 KAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRF-LVIEENKV 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-222 |
5.63e-13 |
|
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: 67.82 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMvAAGM 81
Cdd:TIGR02203 330 DVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfYEPDSGQILLDGHDLADYTLASL-RRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFAEmTVEDNLMLGAFDRYRRG-LRD--QDQTLAEVFELFPR-LQERRAQLAGTLSGGERQMLAVGRALMAK 157
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRAeIERalAAAYAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 158 PRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNArAALQVADYAYVLETGTVTLEGP 222
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRL-STIEKADRIVVMDDGRIVERGT 550
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-220 |
5.68e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 17 KVEAVSG------VSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRE 89
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGaTRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 ---LFAEMTVEDNLMLGAFDRYRR-GLRDQDQTLAEVFELF-PRLQER---RAQLAGTLSGGERQMLAVGRALMAKPRLL 161
Cdd:PRK11288 339 aegIIPVHSVADNINISARRHHLRaGCLINNRWEAENADRFiRSLNIKtpsREQLIMNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 162 MLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLE 220
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-170 |
5.81e-13 |
|
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: 65.59 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQehAEIEEMVAAGMNLV 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPL--DFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDNLmlgafdRYRRGLRDQDQTLAEVFELFPRLQERRAqlAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:cd03231 79 GHAPGIKTTLSVLENL------RFWHADHSDEQVEEALARVGLNGFEDRP--VAQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*.
gi 2495741221 165 EPSLGL 170
Cdd:cd03231 151 EPTTAL 156
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-221 |
6.17e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMvAAGMNLV 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVFLGDKPISMLSSRQL-ARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 PEKRELFAEMTVEDnlmLGAFDR------YRRgLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKP 158
Cdd:PRK11231 82 PQHHLTPEGITVRE---LVAYGRspwlslWGR-LSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 159 RLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-221 |
7.98e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGgitFGGKA-QEHAEIEEMVAAGMNLVPEKRELFAEMTVEDN 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN---FTGTIlANNRKPTKQILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 LMLGAFDRYRRGLRDQDQTLAE---VFELfpRLQERRAQLAGT-----LSGGERQMLAVGRALMAKPRLLMLDEPSLGLA 171
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAesvISEL--GLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 172 PRIVREVFRIVARLREMGVSILL-IEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-222 |
1.44e-12 |
|
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: 64.94 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYD-KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaQEHAEIE-EMVAAGMN 82
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILIDG--QDIREVTlDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 LVPEKRELFAEmTVEDNLMLGafdryRRGLRDQDQTLA-------EVFELFP-----RLQERraqlaGT-LSGGERQMLA 149
Cdd:cd03253 79 VVPQDTVLFND-TIGYNIRYG-----RPDATDEEVIEAakaaqihDKIMRFPdgydtIVGER-----GLkLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 150 VGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREmGVSILLIEQNARAALQvADYAYVLETGTVTLEGP 222
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-239 |
2.30e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmVAAG 80
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKE-VARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEKRELFAEMTVEDNLMLG------AFDRYRRglRDQDQTLAEVFElfPRLQERRAQLAGTLSGGERQMLAVGRAL 154
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGryphqpLFTRWRK--EDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 155 MAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGpAAKVAQDPRVV 233
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-APKEIVTAELI 237
|
....*.
gi 2495741221 234 EVYLGL 239
Cdd:PRK10253 238 ERIYGL 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-167 |
2.54e-12 |
|
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: 62.47 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGgkaqehaeieemvaagmnlv 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 85 pekrelfaemtveDNLMLGAFDRyrrglrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:cd03221 61 -------------STVKIGYFEQ--------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
...
gi 2495741221 165 EPS 167
Cdd:cd03221 96 EPT 98
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-204 |
2.74e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAkLLQVRDLRVAY----DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSaIMGVL--PSQGGITFGGkaQEHAEIE 74
Cdd:PRK10535 1 MTA-LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdkPTSGTYRVAG--QDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAAGM-----NLVPEKRELFAEMTVEDNLMLGAFdrYRRGLRDQDQTLAEvfELFPRL--QERRAQLAGTLSGGERQM 147
Cdd:PRK10535 77 ADALAQLrrehfGFIFQRYHLLSHLTAAQNVEVPAV--YAGLERKQRLLRAQ--ELLQRLglEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 148 LAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQ 204
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-231 |
3.05e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.62 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIM-GVLPSQGGITFGGKAQeHAEIEEMVAAGM 81
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPI-ADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFAEmTVEDNLMLGAFDRyrrglrdQDQTLAEVFE---LFPRLQERRA------QLAGTLSGGERQMLAVGR 152
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNA-------SDEALIEVLQqvgLEKLLEDDKGlnawlgEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 153 ALMAKPRLLMLDEPSLGLAPRIVREVFRIvarLREM--GVSILLIEQNARaALQVADYAYVLETGTVTLEGPAAK-VAQD 229
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILEL---LAEHaqNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQElLAQQ 564
|
..
gi 2495741221 230 PR 231
Cdd:PRK11160 565 GR 566
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-187 |
3.43e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGIT-FGGKAQEHAEIEEMVA--AGMn 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArKIQQGRVEvLGGDMADARHRRAVCPriAYM- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 lvPE--KRELFAEMTVEDNLmlgafdryrrglrdqdqtlaevfELFPRL-----QERRAQL----------------AGT 139
Cdd:NF033858 82 --PQglGKNLYPTLSVFENL-----------------------DFFGRLfgqdaAERRRRIdellratglapfadrpAGK 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLRE 187
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRA 184
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-208 |
3.57e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKA--QEHAEIEEMVAagm 81
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFERQSikKDLCTYQKQLC--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nLVPEKRELFAEMTVEDNLMlgaFDRYRRGLRDQDQTLAEVFEL-----FPrlqerraqlAGTLSGGERQMLAVGRALMA 156
Cdd:PRK13540 78 -FVGHRSGINPYLTLRENCL---YDIHFSPGAVGITELCRLFSLehlidYP---------CGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 157 KPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADY 208
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ-DLPLNKADY 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-165 |
4.56e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.98 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD-KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGkaqehAEIEEMVAAGMN 82
Cdd:PRK13657 334 AVEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFdPQSGRILIDG-----TDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 ----LVPEKRELFAEmTVEDNLMLGAfdryrrglrdQDQTLAEVFELFPRLQ-----ERRAQLAGT--------LSGGER 145
Cdd:PRK13657 409 rniaVVFQDAGLFNR-SIEDNIRVGR----------PDATDEEMRAAAERAQahdfiERKPDGYDTvvgergrqLSGGER 477
|
170 180
....*....|....*....|
gi 2495741221 146 QMLAVGRALMAKPRLLMLDE 165
Cdd:PRK13657 478 QRLAIARALLKDPPILILDE 497
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
5.21e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.49 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD-----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG------ITFGGKAQEHAEI 73
Cdd:PRK13631 21 ILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 74 EEMVAAGMNLVPEKREL------FAEM-----TVEDNLMLG---------------AFDRYRRGLrdqDQTLAEV--FEL 125
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRvsmvfqFPEYqlfkdTIEKDIMFGpvalgvkkseakklaKFYLNKMGL---DDSYLERspFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 126 fprlqerraqlagtlSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQV 205
Cdd:PRK13631 178 ---------------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEV 242
|
250 260
....*....|....*....|....*....
gi 2495741221 206 ADYAYVLETGTVTLEGPAAKVAQDPRVVE 234
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-229 |
7.00e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPsqggitfggkaqeHAEIEEMVAAG-MNLVPEKRELFaEMTVEDN 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------HAETSSVVIRGsVAYVPQVSWIF-NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 LMLGAFDRYRRGLRDQDQT-LAEVFELFP-RLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVRE 177
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTaLQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 178 VFRIVARLREMGVSILLIeQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-165 |
8.51e-12 |
|
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: 62.87 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDK---VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGK---AQEHAEIEEMV 77
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqVLLDGKpisQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AagmnLVPEKRELFAEmTVEDNLMLG----AFDRYRRGlrdQDQTLAEVF--ELFPRLQERRAQLAGTLSGGERQMLAVG 151
Cdd:cd03248 91 S----LVGQEPVLFAR-SLQDNIAYGlqscSFECVKEA---AQKAHAHSFisELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170
....*....|....
gi 2495741221 152 RALMAKPRLLMLDE 165
Cdd:cd03248 163 RALIRNPQVLILDE 176
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-230 |
8.61e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.77 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITfggkaqehaeIEEMVAAG 80
Cdd:COG4170 3 LLDIRNLTIEIDtpqgRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVT----------ADRFRWNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNL----VPEKREL--------FAE--------MTVEDNLMLG-------------AFDRYRR--------GLRDQDQtl 119
Cdd:COG4170 73 IDLlklsPRERRKIigreiamiFQEpsscldpsAKIGDQLIEAipswtfkgkwwqrFKWRKKRaiellhrvGIKDHKD-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 120 aeVFELFPRlqerraqlagTLSGGERQ--MLAVgrALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREM-GVSILLIE 196
Cdd:COG4170 151 --IMNSYPH----------ELTEGECQkvMIAM--AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLIS 216
|
250 260 270
....*....|....*....|....*....|....
gi 2495741221 197 QNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:COG4170 217 HDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
9.14e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIE 74
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQaitDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAagmnLV---PEKRelFAEMTVEDNLMLGAFDR---YRRGLRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQML 148
Cdd:PRK13648 83 KHIG----IVfqnPDNQ--FVGSIVKYDVAFGLENHavpYDEMHRRVSEALKQV-----DMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 149 AVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQvADYAYVLETGTVTLEGPAAKVA 227
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
..
gi 2495741221 228 QD 229
Cdd:PRK13648 231 DH 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-237 |
9.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAYDK---VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAG 80
Cdd:PRK13642 3 KILEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEKRE-LFAEMTVEDNLmlgAFDRYRRGLrDQDQTLAEVFE--LFPRLQERRAQLAGTLSGGERQMLAVGRALMAK 157
Cdd:PRK13642 83 IGMVFQNPDnQFVGATVEDDV---AFGMENQGI-PREEMIKRVDEalLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 158 PRLLMLDEPSLGLAPRIVREVFRIVARLRE-MGVSILLIEQNARAALQvADYAYVLETGTVTLE-GPAAKVAQDPRVVEV 235
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEaAPSELFATSEDMVEI 237
|
..
gi 2495741221 236 YL 237
Cdd:PRK13642 238 GL 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-215 |
9.44e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIEEMVAAGMNLV---PEKrELFaEMTV 96
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAGYhitPETGNKNLKKLRKKVSLVfqfPEA-QLF-ENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 97 EDNLMLGAFDRyrrGLRDQDQTLAEVfELFPR--LQERRAQLAG-TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPR 173
Cdd:PRK13641 104 LKDVEFGPKNF---GFSEDEAKEKAL-KWLKKvgLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2495741221 174 IVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETG 215
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-224 |
1.24e-11 |
|
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: 62.90 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 23 GVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEMVAAGMNLVpeKRELfaEMTVEDNLm 101
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQ-----DLYQLDRKQRRAF--RRDV--QLVFQDSP- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 102 lGAFDRyRRGLRdqdQTLAEVFELFPRL----QERRAQ---------------LAGTLSGGERQMLAVGRALMAKPRLLM 162
Cdd:TIGR02769 99 -SAVNP-RMTVR---QIIGEPLRHLTSLdeseQKARIAelldmvglrsedadkLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 163 LDEPSLGLAPRIVREVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAA 224
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-165 |
1.50e-11 |
|
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: 62.17 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 9 RDLRVAYDK---VEAVSGVSLEVGEGQIVTVIGPNGAGKTTllsaIMGVL-----PSQGGITFGGKAQEHAEIEEmVAAG 80
Cdd:cd03249 4 KNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLerfydPTSGEILLDGVDIRDLNLRW-LRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLVPEKRELFAeMTVEDNLMLGAFDRyrrglrdqdqTLAEVFE------------LFP-RLQERRAQLAGTLSGGERQM 147
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGKPDA----------TDEEVEEaakkanihdfimSLPdGYDTLVGERGSQLSGGQKQR 147
|
170
....*....|....*...
gi 2495741221 148 LAVGRALMAKPRLLMLDE 165
Cdd:cd03249 148 IAIARALLRNPKILLLDE 165
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
1.54e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGvLPS----QGGITFGGKAQEHAEIEEM 76
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykilEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 77 VAAGMNLVPEKRELFAEMTVEDNLMLgAFDRYRRGLRDQDQTLAEVFELF----------PRLQERraQLAGTLSGGER- 145
Cdd:CHL00131 82 AHLGIFLAFQYPIEIPGVSNADFLRL-AYNSKRKFQGLPELDPLEFLEIIneklklvgmdPSFLSR--NVNEGFSGGEKk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 146 -----QMlavgrALMaKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARaALQ--VADYAYVLE----- 213
Cdd:CHL00131 159 rneilQM-----ALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR-LLDyiKPDYVHVMQngkii 231
|
....*..
gi 2495741221 214 -TGTVTL 219
Cdd:CHL00131 232 kTGDAEL 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-231 |
1.80e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAY-----------DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEH 70
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 71 AEIEEMVaagmnlvPEKREL---FAEMTVEDNLMLGAFDRYRRGLR---------DQDQTLAEVFELFPRLQERRAQLAG 138
Cdd:PRK15134 352 LNRRQLL-------PVRHRIqvvFQDPNSSLNPRLNVLQIIEEGLRvhqptlsaaQREQQVIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 139 TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREM-GVSILLIEQNARAALQVADYAYVLETGTV 217
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250
....*....|....
gi 2495741221 218 TLEGPAAKVAQDPR 231
Cdd:PRK15134 505 VEQGDCERVFAAPQ 518
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-231 |
1.89e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYD----------KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAI-MGVLPSQGGITFGGKAQE 69
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLtMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 70 HAEIEE---------MV----AAGMNlvPEKR-ELFAEMTVEDNLMLGAFDRYRRGLrdqdQTLAEVfELFPRLQERRAQ 135
Cdd:PRK11308 81 KADPEAqkllrqkiqIVfqnpYGSLN--PRKKvGQILEEPLLINTSLSAAERREKAL----AMMAKV-GLRPEHYDRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 136 LagtLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLET 214
Cdd:PRK11308 154 M---FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYL 230
|
250
....*....|....*..
gi 2495741221 215 GTVTLEGPAAKVAQDPR 231
Cdd:PRK11308 231 GRCVEKGTKEQIFNNPR 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-194 |
2.01e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 19 EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEM--VAAGMNLVPEKRELFAEMT 95
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLML-----GAFDRYRRglRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGL 170
Cdd:PRK10908 96 VYDNVAIpliiaGASGDDIR--RRVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180
....*....|....*....|....
gi 2495741221 171 APRIVREVFRIVARLREMGVSILL 194
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLM 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-218 |
2.32e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHAEIEEMVAAGMNLVPEKRE---LFAEMTV 96
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGeIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 97 EDNLMLGAFDRYRR-----GL---RDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSL 168
Cdd:PRK09700 359 AQNMAISRSLKDGGykgamGLfheVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2495741221 169 GLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVT 218
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-188 |
3.11e-11 |
|
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: 60.74 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 16 DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS----QGGITFGGKaqEHAEIEEMVAAGMNLVPEKRELF 91
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYNGI--PYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 92 AEMTVEDNL-----MLGafDRYRRGlrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:cd03233 96 PTLTVRETLdfalrCKG--NEFVRG----------------------------ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|..
gi 2495741221 167 SLGLAPRIvreVFRIVARLREM 188
Cdd:cd03233 146 TRGLDSST---ALEILKCIRTM 164
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-193 |
4.38e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 25 SLEVGEGQIVTviGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAqehaeieemVAAgmnLVPEK-RE----------LFA 92
Cdd:PRK10247 29 SLRAGEFKLIT--GPSGCGKSTLLKIVASLIsPTSGTLLFEGED---------IST---LKPEIyRQqvsycaqtptLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 93 EmTVEDNLmlgAFDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAP 172
Cdd:PRK10247 95 D-TVYDNL---IFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|..
gi 2495741221 173 RIVREVFRIVARL-REMGVSIL 193
Cdd:PRK10247 171 SNKHNVNEIIHRYvREQNIAVL 192
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-195 |
4.43e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGItfGGKAQ-EHAEIee 75
Cdd:PRK09473 8 QADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI--GGSATfNGREI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 mvaagMNLvPEKR--ELFAE---MTVEDNLMlgAFDRYRRgLRDQdqtLAEVFEL---------------------FPRL 129
Cdd:PRK09473 84 -----LNL-PEKElnKLRAEqisMIFQDPMT--SLNPYMR-VGEQ---LMEVLMLhkgmskaeafeesvrmldavkMPEA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 130 QERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLI 195
Cdd:PRK09473 152 RKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMI 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-167 |
5.68e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGgkaqehaeieEMVAAGMn 82
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqEQPDSGTIEIG----------ETVKLAY- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 83 lVPEKRE-LFAEMTV-------EDNLMLGAFDRYRR------GLRDQDQtlaevfelfprlQERraqlAGTLSGGERQML 148
Cdd:TIGR03719 390 -VDQSRDaLDPNKTVweeisggLDIIKLGKREIPSRayvgrfNFKGSDQ------------QKK----VGQLSGGERNRV 452
|
170
....*....|....*....
gi 2495741221 149 AVGRALMAKPRLLMLDEPS 167
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPT 471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-241 |
6.83e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAgmnlvpekrelfaemTVEDNLML 102
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELePSEGKIKHSGRISFSPQTSWIMPG---------------TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 103 G-AFDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVF- 179
Cdd:TIGR01271 510 GlSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFe 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 180 RIVARLREMGVSILLIEQNARaaLQVADYAYVLETGTVTLEGPAAKV-AQDPRVVEVYLGLGH 241
Cdd:TIGR01271 590 SCLCKLMSNKTRILVTSKLEH--LKKADKILLLHEGVCYFYGTFSELqAKRPDFSSLLLGLEA 650
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
7.85e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 22 SGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP--SQGGITFGGKaqehaeieemVAagmnLVPEKRELFaEMTVEDN 99
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprSDASVVIRGT----------VA----YVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 LMLGA-FD--RYRRGLRdqDQTLAEVFELFP-----RLQERRAQlagtLSGGERQMLAVGRALMAKPRLLMLDEPSLGLA 171
Cdd:PLN03130 699 ILFGSpFDpeRYERAID--VTALQHDLDLLPggdltEIGERGVN----ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2495741221 172 PRIVREVFRIVARlREMGVSILLIEQNARAALQVADYAYVLETGTVTLEG 221
Cdd:PLN03130 773 AHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-202 |
7.97e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDK----VEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEH---AE 72
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPMSKlssAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 73 IEEMVAAGMNLVPEKRELFAEMTVEDN----LMLGAFDRYRRGLRDQDQtLAEVfelfpRLQERRAQLAGTLSGGERQML 148
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENvampLLIGKKKPAEINSRALEM-LAAV-----GLEHRANHRPSELSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 149 AVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAA 202
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLA 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-166 |
1.03e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 36 VIGPNGAGKTTLLSAIMGV--------LPSQGgITFGGKAQE---------HAEIEEMVAAGMNLVPEKRELFAEMTVED 98
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVdkdfngeaRPQPG-IKVGYLPQEpqldptktvRENVEEGVAEIKDALDRFNEISAKYAEPD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 99 NlmlgafdryrrglrDQDQTLAEVFELFPRLQ-------ERRAQLA-------------GTLSGGERQMLAVGRALMAKP 158
Cdd:TIGR03719 115 A--------------DFDKLAAEQAELQEIIDaadawdlDSQLEIAmdalrcppwdadvTKLSGGERRRVALCRLLLSKP 180
|
....*...
gi 2495741221 159 RLLMLDEP 166
Cdd:TIGR03719 181 DMLLLDEP 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-166 |
1.32e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGI-------TFGGKAQEHAeieEMVA 78
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTvkwsenaNIGYYAQDHA---YDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNlvpekreLFAEMTvednlmlgafdRYRRGlRDQDQTLAEVFE--LFPrlQERRAQLAGTLSGGERQMLAVGRALMA 156
Cdd:PRK15064 397 NDLT-------LFDWMS-----------QWRQE-GDDEQAVRGTLGrlLFS--QDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|
gi 2495741221 157 KPRLLMLDEP 166
Cdd:PRK15064 456 KPNVLVMDEP 465
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-165 |
1.52e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVA-YDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS-QGGITFggkaqehAEIEEMVaagmnL 83
Cdd:COG4178 363 LALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIAR-------PAGARVL-----F 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELFaemtvednlmLGAfdryrrgLRDQ-----------DQTLAEVFE------LFPRLQERrAQLAGTLSGGERQ 146
Cdd:COG4178 431 LPQRPYLP----------LGT-------LREAllypataeafsDAELREALEavglghLAERLDEE-ADWDQVLSLGEQQ 492
|
170
....*....|....*....
gi 2495741221 147 MLAVGRALMAKPRLLMLDE 165
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDE 511
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-196 |
1.63e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDkveavsGVSLEVGEGQI-----VTVIGPNGAGKTTLLSAIMGVL-PSQGGITFG----GKAQEhaeie 74
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPElkisYKPQY----- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 emvaagmnLVPEKrelfaEMTVEDNLMlGAFDRYRRGLRDQDqtLAEVFELfPRLQERRaqlAGTLSGGERQMLAVGRAL 154
Cdd:PRK13409 409 --------IKPDY-----DGTVEDLLR-SITDDLGSSYYKSE--IIKPLQL-ERLLDKN---VKDLSGGELQRVAIAACL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2495741221 155 MAKPRLLMLDEPS--LGLAPRIVreVFRIVARL-REMGVSILLIE 196
Cdd:PRK13409 469 SRDADLYLLDEPSahLDVEQRLA--VAKAIRRIaEEREATALVVD 511
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-196 |
1.64e-10 |
|
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: 60.57 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAYDkveavsGVSLEVGEGQI-----VTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG----KAQEh 70
Cdd:COG1245 337 EEETLVEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLkisyKPQY- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 71 aeieemvaagmnLVPEkrelfAEMTVEDNLMLGAFDRYrrglrdqDQTLAEVfELFPRLQERR--AQLAGTLSGGERQML 148
Cdd:COG1245 410 ------------ISPD-----YDGTVEEFLRSANTDDF-------GSSYYKT-EIIKPLGLEKllDKNVKDLSGGELQRV 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 149 AVGRALMAKPRLLMLDEPS--LGLAPRIvrEVFRIVARL-REMGVSILLIE 196
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSahLDVEQRL--AVAKAIRRFaENRGKTAMVVD 513
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-221 |
1.75e-10 |
|
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: 59.04 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 10 DLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEiEEMVAAGMNLVPEKR 88
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALAD-PAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 89 ELFAEmTVEDNLMLG--AFDRYRRglrDQDQTLAEVFELFPRLQERRAQLAG----TLSGGERQMLAVGRALMAKPRLLM 162
Cdd:cd03252 86 VLFNR-SIRDNIALAdpGMSMERV---IEAAKLAGAHDFISELPEGYDTIVGeqgaGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 163 LDEPSLGLAPR----IVREVFRIVArlremGVSILLIEQNArAALQVADYAYVLETGTVTLEG 221
Cdd:cd03252 162 FDEATSALDYEsehaIMRNMHDICA-----GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQG 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-208 |
2.53e-10 |
|
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: 57.72 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVaydkvEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMgvlpsqggitfggkaqehaeieemVAAGMNLVP 85
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL------------------------YASGKARLI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 86 EKRELFAEMTVednLMLgafdryrrglrDQDQTLAEVFELFPRLQerraQLAGTLSGGERQMLAVGRALMA--KPRLLML 163
Cdd:cd03238 52 SFLPKFSRNKL---IFI-----------DQLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSepPGTLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADY 208
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADW 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
2.56e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEmVA 78
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKIDGITISKENLKE-IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNLV---PEKRelFAEMTVEDNLMLGAFDRY--RRGLRDQDQTLAEVFELFPRLqERRAQlagTLSGGERQMLAVGRA 153
Cdd:PRK13632 83 KKIGIIfqnPDNQ--FIGATVEDDIAFGLENKKvpPKKMKDIIDDLAKKVGMEDYL-DKEPQ---NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILL-IEQNARAALQvADYAYVLETGTVTLEGPAAKVAQDPRV 232
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
...
gi 2495741221 233 VEV 235
Cdd:PRK13632 236 LEK 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-234 |
3.60e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.66 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 1 MSAKLLQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQG--------GITFGGKAQe 69
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNpnskitvdGITLTAKTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 70 hAEIEEMVAagmnLV---PEKRelFAEMTVEDNLmlgAFDRYRRGL-RDQDQTL-AEVFELFPRLQERRAQLAgTLSGGE 144
Cdd:PRK13640 80 -WDIREKVG----IVfqnPDNQ--FVGATVGDDV---AFGLENRAVpRPEMIKIvRDVLADVGMLDYIDSEPA-NLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 145 RQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQvADYAYVLETGTVTLEGPA 223
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSP 227
|
250
....*....|.
gi 2495741221 224 AKVAQDPRVVE 234
Cdd:PRK13640 228 VEIFSKVEMLK 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-166 |
6.57e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 36 VIGPNGAGKTTLLSAIMGV-LPSQG------GITFGGKAQE---------HAEIEEMVAAGMNLVPEKRELFAEMTVEDN 99
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVdKEFEGearpapGIKVGYLPQEpqldpektvRENVEEGVAEVKAALDRFNEIYAAYAEPDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 lmlgafdryrrglrDQDQTLAEVFELFPRLQ-------ERRAQLA-------------GTLSGGERQMLAVGRALMAKPR 159
Cdd:PRK11819 118 --------------DFDALAAEQGELQEIIDaadawdlDSQLEIAmdalrcppwdakvTKLSGGERRRVALCRLLLEKPD 183
|
....*..
gi 2495741221 160 LLMLDEP 166
Cdd:PRK11819 184 MLLLDEP 190
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-195 |
8.19e-10 |
|
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: 56.01 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGitfggkaqehaEIEEMVAAGMNLVPEkRELFAEMTvednl 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-----------RIGMPEGEDLLFLPQ-RPYLPLGT----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 101 mlgafdryrrgLRDQdqtLAevfelFPRLQErraqlagtLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFR 180
Cdd:cd03223 80 -----------LREQ---LI-----YPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*
gi 2495741221 181 IvarLREMGVSILLI 195
Cdd:cd03223 133 L---LKELGITVISV 144
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-197 |
8.78e-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: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPsqggiTFGGKAQEHAEieemvaAGMNLVPEkRELFAEMTVEDNL 100
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-----VYGGRLTKPAK------GKLFYVPQ-RPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 101 ML--GAFDRYRRGLRDQD--QTLAEVfELFPRLQERRAQLA-----GTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLA 171
Cdd:TIGR00954 536 IYpdSSEDMKRRGLSDKDleQILDNV-QLTHILEREGGWSAvqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*.
gi 2495741221 172 PRIVREVFRIvarLREMGVSILLIEQ 197
Cdd:TIGR00954 615 VDVEGYMYRL---CREFGITLFSVSH 637
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-192 |
9.64e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGIT--FGgkaqehaeieEMVAAGmNLVPEKR--------E 89
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlFG----------QPVDAG-DIATRRRvgymsqafS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 LFAEMTVEDNLMLGAfdR-YRRGLRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSL 168
Cdd:NF033858 350 LYGELTVRQNLELHA--RlFHLPAAEIAARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180
....*....|....*....|....*.
gi 2495741221 169 GLAPrIVREVF-RIVARL-REMGVSI 192
Cdd:NF033858 427 GVDP-VARDMFwRLLIELsREDGVTI 451
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-236 |
1.01e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPS---------QGGITFGGKAQehAEIEE 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGEPL--AAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 MVAAGMNLV-PEKRELFAEMTVEDNLMLGAFDRYRRG--LRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGR 152
Cdd:PRK13547 79 PRLARLRAVlPQAAQPAFAFSAREIVLLGRYPHARRAgaLTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 153 AL---------MAKPRLLMLDEPSLGL----APRIVREVfRIVARLREMGVsiLLIEQNARAALQVADYAYVLETGTVTL 219
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALdlahQHRLLDTV-RRLARDWNLGV--LAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|....*..
gi 2495741221 220 EGPAAKVAQDPRVVEVY 236
Cdd:PRK13547 236 HGAPADVLTPAHIARCY 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-231 |
1.07e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDL------------RVAYDkVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGKAQEHA 71
Cdd:PRK10261 313 ILQVRNLvtrfplrsgllnRVTRE-VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGeIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 72 EIEEMVAAGMNLVPEKRELFAEM----TVEDNLMlgafDRYR-RGLRDQDQTLAEVFELFPR---LQERRAQLAGTLSGG 143
Cdd:PRK10261 392 SPGKLQALRRDIQFIFQDPYASLdprqTVGDSIM----EPLRvHGLLPGKAAAARVAWLLERvglLPEHAWRYPHEFSGG 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 144 ERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGP 222
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
....*....
gi 2495741221 223 AAKVAQDPR 231
Cdd:PRK10261 548 RRAVFENPQ 556
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-167 |
1.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAY-DKVeAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQehaeieemvaagM 81
Cdd:PRK11819 323 KVIEAENLSKSFgDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEqPDSGTIKIGETVK------------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRE-LFAEMTV-------EDNLMLGAFD---R-Y--RRGLRDQDQtlaevfelfprlQERraqlAGTLSGGERQM 147
Cdd:PRK11819 390 AYVDQSRDaLDPNKTVweeisggLDIIKVGNREipsRaYvgRFNFKGGDQ------------QKK----VGVLSGGERNR 453
|
170 180
....*....|....*....|
gi 2495741221 148 LAVGRALMAKPRLLMLDEPS 167
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-236 |
1.21e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSaIMG--VLPSQGGITFGGKAQEHAEiEEMVAAGMNLVPEKRELFAEMTVEDNLM 101
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLGrhQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQLPAAEGMTVRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 102 L------GAFDRYRRGLRDQDQTLAEVFELFPRLQerraQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIV 175
Cdd:PRK10575 108 IgrypwhGALGRFGAADREKVEEAISLVGLKPLAH----RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 176 REVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPRVVEVY 236
Cdd:PRK10575 184 VDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-230 |
1.89e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGG---KAQEHAEIEEMVAAGMNLVPEKRELFAEMT 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLMLGAFDRYRRGLRDQDQTLAEVFELfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIV 175
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 176 REVFRIVARLR-EMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK10070 201 TEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-167 |
1.98e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIE---EMVAAGMNLVPEKRELFAEMTV 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEEaraKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495741221 97 EDNLMLGAFDR--YRRGLRDQDQTLAEVFELFPRLQERRAQLagtlSGGERQMLAVGRALMAKPRLLMLDEPS 167
Cdd:PRK10584 106 LENVELPALLRgeSSRQSRNGAKALLEQLGLGKRLDHLPAQL----SGGEQQRVALARAFNGRPDVLFADEPT 174
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-230 |
2.11e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.03 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQEHAEIEEMvAAGMNLVPEKRELFAEmTVED 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSW-RSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 99 NLMLGAFDRYRRGLrDQDQTLAEVFELFPRLQERRAQLAG----TLSGGERQMLAVGRALMAKPRLLMLDEpslGLAPRI 174
Cdd:PRK10789 408 NIALGRPDATQQEI-EHVARLASVHDDILRLPQGYDTEVGergvMLSGGQKQRISIARALLLNAEILILDD---ALSAVD 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 175 VREVFRIVARLREMGVSILLIEQNAR-AALQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PRK10789 484 GRTEHQILHNLRQWGEGRTVIISAHRlSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-230 |
2.19e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAY---------DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG--------ITFGGK 66
Cdd:PRK15112 3 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelliddhpLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 67 AQEHAEIEEMVA-AGMNLVPEKR-ELFAEMTVEDNLMLGAFDRYRRglrdQDQTLAEVfELFPrlqERRAQLAGTLSGGE 144
Cdd:PRK15112 83 SYRSQRIRMIFQdPSTSLNPRQRiSQILDFPLRLNTDLEPEQREKQ----IIETLRQV-GLLP---DHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 145 RQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLRE-MGVSILLIEQNARAALQVADYAYVLETGTVTLEGPA 223
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
....*..
gi 2495741221 224 AKVAQDP 230
Cdd:PRK15112 235 ADVLASP 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-167 |
2.32e-09 |
|
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: 55.58 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAY--DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKaqehaEIEEM----VA 78
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGV-----DISKIglhdLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 79 AGMNLVPEKRELFaEMTVEDNlmLGAFDRYrrglrdQDQTLAEVFELFpRLQERRAQLAGTL-----------SGGERQM 147
Cdd:cd03244 78 SRISIIPQDPVLF-SGTIRSN--LDPFGEY------SDEELWQALERV-GLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180
....*....|....*....|
gi 2495741221 148 LAVGRALMAKPRLLMLDEPS 167
Cdd:cd03244 148 LCLARALLRKSKILVLDEAT 167
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-216 |
2.41e-09 |
|
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: 56.40 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAgmnlvpekrelfaemTVEDNLML 102
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELePSEGKIKHSGRISFSSQFSWIMPG---------------TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 103 G-AFDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVF- 179
Cdd:cd03291 121 GvSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFe 200
|
170 180 190
....*....|....*....|....*....|....*..
gi 2495741221 180 RIVARLREMGVSILLieQNARAALQVADYAYVLETGT 216
Cdd:cd03291 201 SCVCKLMANKTRILV--TSKMEHLKKADKILILHEGS 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-166 |
2.51e-09 |
|
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: 55.80 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAA---GMNLVPEKRELFAEMTVE 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495741221 98 DNLMLGA-FDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:cd03290 97 ENITFGSpFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-165 |
3.74e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVEAV-SGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-SQGGITFGGKAQE---HAEIEEMVAag 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSslsHSVLRQGVA-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 mnLVPEKRELFAEmTVEDNLMLGafdryrrglRDQDQT----------LAEVFELFPR-LQERRAQLAGTLSGGERQMLA 149
Cdd:PRK10790 419 --MVQQDPVVLAD-TFLANVTLG---------RDISEEqvwqaletvqLAELARSLPDgLYTPLGEQGNNLSVGQKQLLA 486
|
170
....*....|....*.
gi 2495741221 150 VGRALMAKPRLLMLDE 165
Cdd:PRK10790 487 LARVLVQTPQILILDE 502
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-166 |
6.33e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAgmnLVPEKrelfaemTVEDNL 100
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAE---LDPEK-------TVMDNL 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 101 -------MLGAFDRYRRG-LRDqdqtlaevFeLFPRLQERRAQLAgtLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:PRK11147 405 aegkqevMVNGRPRHVLGyLQD--------F-LFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-187 |
6.53e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 3 AKLLQVRDLRVAYDKVE---AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG--ITFGGKAQEHAEIEEMV 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqiIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AAGMNLV-PEKRelFAEMTVEDNLmlgAFdryrrGLRDQDQTLAEVFElfpRLQERrAQLAGT----------LSGGERQ 146
Cdd:PRK13650 82 KIGMVFQnPDNQ--FVGATVEDDV---AF-----GLENKGIPHEEMKE---RVNEA-LELVGMqdfkereparLSGGQKQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2495741221 147 MLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLRE 187
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRD 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-205 |
8.28e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMVAAGMNL 83
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 84 VPEKRELfaeMTVEDNLMLGAFdRYRRGLRDQDQTLAEVfelfpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLML 163
Cdd:PRK13543 91 PGLKADL---STLENLHFLCGL-HGRRAKQMPGSALAIV-----GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2495741221 164 DEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQV 205
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPV 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-229 |
1.10e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAEIEEMVAAgmnlvpeKRELfaEMTVEDN 99
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGEPLAKLNRAQRKAF-------RRDI--QMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 100 LmlGAFDRYRRGLRDQDQTLAEVFELFPRLQERRA---------------QLAGTLSGGERQMLAVGRALMAKPRLLMLD 164
Cdd:PRK10419 99 I--SAVNPRKTVREIIREPLRHLLSLDKAERLARAsemlravdlddsvldKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 165 EPSLGLAPRIVREVFRIVARLRE-MGVSILLIEQNAR------AALQVADYAYVLETGTV----TLEGPAAKVAQD 229
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRlverfcQRVMVMDNGQIVETQPVgdklTFSSPAGRVLQN 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-195 |
1.12e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 13 VAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGitfggkaqehaeieemvaAGMNLVPEKrEL 90
Cdd:COG2401 36 VELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------------------AGCVDVPDN-QF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 91 FAEMTVEDNLmlgafdryrrglrDQDQTLAEVFELFPRLQERRAQL----AGTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:COG2401 97 GREASLIDAI-------------GRKGDFKDAVELLNAVGLSDAVLwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|
gi 2495741221 167 SLGLAPRIVREVFRIVARL-REMGVSILLI 195
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLaRRAGITLVVA 193
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-194 |
1.42e-08 |
|
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: 55.02 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFGGKAQeHAEIEEmVAAGMNLVPEKRELFAEMTVED 98
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdTTVTSGDATVAGKSI-LTNISD-VHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 99 NLMLGAfdRYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREV 178
Cdd:TIGR01257 2032 HLYLYA--RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170
....*....|....*.
gi 2495741221 179 FRIVARLREMGVSILL 194
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVL 2125
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-193 |
1.98e-08 |
|
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: 52.63 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVsleVGEGQIVTVIGPNGAGKTTLLSAI-----MGVLpsQGGITFGGKaqehaEIEEMVAAGMNLVPEKRELFAEMT 95
Cdd:cd03232 26 ISGY---VKPGTLTALMGESGAGKTTLLDVLagrktAGVI--TGEILINGR-----PLDKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 96 VEDNLMLGAfdrYRRGlrdqdqtlaevfelfprlqerraqlagtLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIV 175
Cdd:cd03232 96 VREALRFSA---LLRG----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170
....*....|....*...
gi 2495741221 176 REVFRIVARLREMGVSIL 193
Cdd:cd03232 145 YNIVRFLKKLADSGQAIL 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-228 |
2.32e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVaYDKVEA----VSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGvlPS-----QGGITFGGKAQEHAEIE 74
Cdd:NF040905 256 VVFEVKNWTV-YHPLHPerkvVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSygrniSGTVFKDGKEVDVSTVS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAAGMNLVPEKRE---LFAEMTVEDNLMLGAFDRY-RRGLRDQDQTLaEVFELFPRLQERRA----QLAGTLSGGERQ 146
Cdd:NF040905 333 DAIDAGLAYVTEDRKgygLNLIDDIKRNITLANLGKVsRRGVIDENEEI-KVAEEYRKKMNIKTpsvfQKVGNLSGGNQQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 147 MLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKV 226
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEA 491
|
..
gi 2495741221 227 AQ 228
Cdd:NF040905 492 SQ 493
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-172 |
3.83e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPsQGG----ITFG---GKAQEHAEIEE-- 75
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGYsndlTLFGrrrGSGETIWDIKKhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 76 -MVAAGMNLvpEKRelfAEMTVEDNLMLGAFDR---YrRGLRDQDQTLAEvfELFPRLQeRRAQLAG----TLSGGERQM 147
Cdd:PRK10938 339 gYVSSSLHL--DYR---VSTSVRNVILSGFFDSigiY-QAVSDRQQKLAQ--QWLDILG-IDKRTADapfhSLSWGQQRL 409
|
170 180
....*....|....*....|....*
gi 2495741221 148 LAVGRALMAKPRLLMLDEPSLGLAP 172
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-222 |
4.85e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 14 AYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPsqggitfggKAQEHAEIEEMVAagmnLVPEKrELFAE 93
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD---------KVEGHVHMKGSVA----YVPQQ-AWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 MTVEDNLMLGAF---DRYRRGLrdQDQTLAEVFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMAKPRLLMLDEPSLG 169
Cdd:TIGR00957 713 DSLRENILFGKAlneKYYQQVL--EACALLPDLEILPSGDRTEIGEKGvNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2495741221 170 LAPRIVREVFRIVARLREM--GVSILLIEQNARAALQVaDYAYVLETGTVTLEGP 222
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVlkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-200 |
4.92e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 4.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 139 TLSGGERQMLAVGRALMAKPRLLM--LDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNAR 200
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-165 |
5.19e-08 |
|
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: 52.90 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 3 AKLLQVRDLRVAYDKV--------EAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK-----AQ 68
Cdd:COG5265 348 APPLVVGGGEVRFENVsfgydperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRILIDGQdirdvTQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 69 E--HAEIeemvaaGMnlVPEKRELFAEmTVEDNLmlgafdRYRRglrdQDQTLAEVFElfprlQERRAQLAGT------- 139
Cdd:COG5265 428 AslRAAI------GI--VPQDTVLFND-TIAYNI------AYGR----PDASEEEVEA-----AARAAQIHDFieslpdg 483
|
170 180 190
....*....|....*....|....*....|....*..
gi 2495741221 140 -----------LSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:COG5265 484 ydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDE 520
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-217 |
5.60e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 2 SAKLLQVRDLRVAYD----KVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGK------AQEHA 71
Cdd:PRK10261 9 ARDVLAVENLNIAFMqeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 72 EIEEMVAAGMNLV--PEKRELFAEMTVEDNLMLGAFDRYRRGLR-----DQDQTLAEVFELF-----PRLQERRAQLAGT 139
Cdd:PRK10261 89 ELSEQSAAQMRHVrgADMAMIFQEPMTSLNPVFTVGEQIAESIRlhqgaSREEAMVEAKRMLdqvriPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 140 LSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVL------ 212
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMyqgeav 248
|
....*
gi 2495741221 213 ETGTV 217
Cdd:PRK10261 249 ETGSV 253
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-166 |
7.12e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 22 SGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIEEMV----AAGMnlvpeKRELfae 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEVLWQGEpirRQRDEYHQDLLylghQPGI-----KTEL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 94 mTVEDNLmlgAFDRYRRGLRDQDQT---LAEV----FELFPrlqerraqlAGTLSGGERQMLAVGRALMAKPRLLMLDEP 166
Cdd:PRK13538 90 -TALENL---RFYQRLHGPGDDEALweaLAQVglagFEDVP---------VRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-182 |
1.02e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLlsaiMGVLpsqGGITFGGKAQEHAEIEEMvaagmnlvPE 86
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTL----MDVL---AGRKTGGYIEGDIRISGF--------PK 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 87 KRELFA--------------EMTVEDNLMLGAFDRYRRGLRDQDQT--LAEVFEL--FPRLQERRAQLAGT--LSGGERQ 146
Cdd:PLN03140 947 KQETFArisgyceqndihspQVTVRESLIYSAFLRLPKEVSKEEKMmfVDEVMELveLDNLKDAIVGLPGVtgLSTEQRK 1026
|
170 180 190
....*....|....*....|....*....|....*.
gi 2495741221 147 MLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIV 182
Cdd:PLN03140 1027 RLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
93-208 |
1.05e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 93 EMTVEDNL-MLGAFDRYRRGLrdqdQTLAEVFELFPRLqerrAQLAGTLSGGERQMLAVGRALMAK---PRLLMLDEPSL 168
Cdd:TIGR00630 790 DMTVEEAYeFFEAVPSISRKL----QTLCDVGLGYIRL----GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTT 861
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2495741221 169 GLAPRIVREVFRIVARLREMGVSILLIEQNARaALQVADY 208
Cdd:TIGR00630 862 GLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTADY 900
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-229 |
1.21e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 25 SLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPsqggitfggkaQEHAEIEEMVAAGMNLVPEKRELFAEMTVEDNL--ML 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP-----------LLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNtdML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 103 GAfdryrrGLRDQDQTLAEVFELFPRLQERRAQLAGT-------------LSGGERQMLAVGRALMAKPRLLMLDEPSLG 169
Cdd:PRK10938 92 SP------GEDDTGRTTAEIIQDEVKDPARCEQLAQQfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 170 LAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQD 229
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-82 |
1.42e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGV-LPSQGGITFGGKAQEHAeieemVAAGMN 82
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGSAALIA-----ISSGLN 97
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-231 |
1.45e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 137 AGTLSGGERQMLA----VGRALMAKprLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARaALQVADYAYVL 212
Cdd:TIGR00630 486 AGTLSGGEAQRIRlatqIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDI 562
|
90 100
....*....|....*....|....*
gi 2495741221 213 ------ETGTVTLEGPAAKVAQDPR 231
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILANPD 587
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-231 |
1.69e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVeAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLP-----SQGGITFGGKAQEHAEIE-EMVAA 79
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrqTAGRVLLDGKPVAPCALRgRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 80 GMNlvpEKRELF---AEMTVEDNLMLGAfdryrRGLRDQDQTLAEVFELFPrLQERRAQL---AGTLSGGERQMLAVGRA 153
Cdd:PRK10418 84 IMQ---NPRSAFnplHTMHTHARETCLA-----LGKPADDATLTAALEAVG-LENAARVLklyPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 154 LMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPAAKVAQDPR 231
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-215 |
1.82e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 139 TLSGGERQMLAVGRALMA---KPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARaALQVADyaYVLETG 215
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVAD--YVLELG 885
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-165 |
2.11e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.17 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVRDLRVAYDKVE--AVSGVSLEVGEGQIVTVIGPNGAGKTT---LLSAIMGVlpSQGGITFGG---KAQEHAEIEEMV 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDI--DEGEILLDGhdlRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AagmnLVPEKRELFAEmTVEDNLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAG----TLSGGERQMLAVGRA 153
Cdd:PRK11176 420 A----LVSQNVHLFND-TIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGengvLLSGGQRQRIAIARA 494
|
170
....*....|..
gi 2495741221 154 LMAKPRLLMLDE 165
Cdd:PRK11176 495 LLRDSPILILDE 506
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-231 |
2.53e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVE----AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGIT-----FGG---KAQEHAE 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekleFNGqdlQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 73 IEEMVAAGMNLVPEK--RELFAEMTVEDNLM------LGAFDRYRRGLRDQDQTLAEVFELFPRLQERRAQLAGTLSggE 144
Cdd:PRK11022 83 RRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMS--Q 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 145 RQMLAVgrALMAKPRLLMLDEPSLGLAPRIVREVFRIVARL-REMGVSILLIEQNARAALQVADYAYVLETGTVTLEGPA 223
Cdd:PRK11022 161 RVMIAM--AIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*...
gi 2495741221 224 AKVAQDPR 231
Cdd:PRK11022 239 HDIFRAPR 246
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-193 |
2.59e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 21 VSGVsleVGEGQIVTVIGPNGAGKTTLLSAIMGVLpSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRELFAEMTVEDNL 100
Cdd:TIGR00956 782 VDGW---VKPGTLTALMGASGAGKTTLLNVLAERV-TTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 101 MLGAFDRYRRGL--RDQDQTLAEVFELFpRLQERRAQLAGT----LSGGERQMLAVGRALMAKPRLLM-LDEPSLGLAPR 173
Cdd:TIGR00956 858 RFSAYLRQPKSVskSEKMEYVEEVIKLL-EMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170 180
....*....|....*....|
gi 2495741221 174 IVREVFRIVARLREMGVSIL 193
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAIL 956
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-228 |
6.11e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAYDKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMG---VLPSQGGITFGGKAQEHAEIEEMVAAGM 81
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NL-------VPEKRELFAEMT----VEDNLMLGAFDRYrrGLRDQDQTLAEVFELFPRLQERRAQLAgtLSGGERQMLAV 150
Cdd:PRK09580 81 FMafqypveIPGVSNQFFLQTalnaVRSYRGQEPLDRF--DFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495741221 151 GRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVA-DYAYVLETGTVTLEGPAAKVAQ 228
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDFTLVKQ 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-232 |
7.04e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY---DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGK---AQEHAEIEEMV 77
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVplvQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 78 AagmnLVPEKRELFAEmTVEDNLMLGaFDRYrrglrDQDQTLAEVFEL--------FPRLQERRAQLAGT-LSGGERQML 148
Cdd:TIGR00958 558 A----LVGQEPVLFSG-SVRENIAYG-LTDT-----PDEEIMAAAKAAnahdfimeFPNGYDTEVGEKGSqLSGGQKQRI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 149 AVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARlreMGVSILLIEQN---ARAALQVAdyayVLETGTVTLEGPAAK 225
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRlstVERADQIL----VLKKGSVVEMGTHKQ 699
|
....*..
gi 2495741221 226 VAQDPRV 232
Cdd:TIGR00958 700 LMEDQGC 706
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-215 |
7.61e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 5 LLQVRDLRVAY----DKVEAVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITfggkaqehaeIEEMVAAG 80
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVT----------ADRMRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLV----PEKRELfaemtVEDNLMLgAFDRYRRGLRDQDQTLAEVFELFP------------RLQERRA---------- 134
Cdd:PRK15093 73 IDLLrlspRERRKL-----VGHNVSM-IFQEPQSCLDPSERVGRQLMQNIPgwtykgrwwqrfGWRKRRAiellhrvgik 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 135 -------QLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLRE-MGVSILLIEQNARAALQVA 206
Cdd:PRK15093 147 dhkdamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWA 226
|
....*....
gi 2495741221 207 DYAYVLETG 215
Cdd:PRK15093 227 DKINVLYCG 235
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-215 |
1.32e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGvlPSQGGITFGGKAQ--EHAEIEEMVAAG----MNLVPEKRelfaemTVE 97
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLINDTLY--PALARRLHLKKEQpgNHDRIEGLEHIDkvivIDQSPIGR------TPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 98 DN--LMLGAFDRYR-------RGLRDQDQTL--------------------AEVFELFPRLQERRA-------------Q 135
Cdd:cd03271 86 SNpaTYTGVFDEIRelfcevcKGKRYNRETLevrykgksiadvldmtveeaLEFFENIPKIARKLQtlcdvglgyiklgQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 136 LAGTLSGGERQMLAVGRALMAKPR---LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaraaLQVADYA-YV 211
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN----LDVIKCAdWI 241
|
....
gi 2495741221 212 LETG 215
Cdd:cd03271 242 IDLG 245
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-230 |
1.70e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGitfggkaqehaeiEEMVAAGMNLVPEKRELFaEMTVEDNLMLg 103
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-------------RVWAERSIAYVPQQAWIM-NATVRGNILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 104 aFDRyRRGLRDQD-----QTLAEVFELFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGL----APRI 174
Cdd:PTZ00243 744 -FDE-EDAARLADavrvsQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALdahvGERV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 175 VREVF--RIVARLREMGVSILLIeqnaraaLQVADYAYVLETGTVTLEGPAAKVAQDP 230
Cdd:PTZ00243 822 VEECFlgALAGKTRVLATHQVHV-------VPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-168 |
3.46e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 30 EGQIVTVIGPNGAGKTTLLSAIMGVL------PSQGGITFGGKAQEHAEIE----------------EMVAAGMNLVP-E 86
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILEAIRYALygkarsRSKLRSDLINVGSEEASVElefehggkryrierrqGEFAEFLEAKPsE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 87 KRELFAEMtvednLMLGAFDRYRRGLRDQDQTLAEVFELFPRLQERRAQL---------AGTLSGGERQMLAVGRALMak 157
Cdd:COG0419 102 RKEALKRL-----LGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS-- 174
|
170
....*....|.
gi 2495741221 158 prlLMLDEPSL 168
Cdd:COG0419 175 ---LILDFGSL 182
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-208 |
8.55e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 30 EGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGIT-----------FGGKA-QEHAE--IEEMVAAGM-----NLVPEKre 89
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFDdppdwdeildeFRGSElQNYFTklLEGDVKVIVkpqyvDLIPKA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 90 lfAEMTVEDNLMlgafdryRRGLRDQDQTLAEVFELFPRLqERRAQlagTLSGGERQMLAVGRALMAKPRLLMLDEPS-- 167
Cdd:cd03236 103 --VKGKVGELLK-------KKDERGKLDELVDQLELRHVL-DRNID---QLSGGELQRVAIAAALARDADFYFFDEPSsy 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2495741221 168 LGLAPRIvrEVFRIVARLREMGVSILLIEQNaraaLQVADY 208
Cdd:cd03236 170 LDIKQRL--NAARLIRELAEDDNYVLVVEHD----LAVLDY 204
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-208 |
8.85e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 8.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 137 AGTLSGGERQMLAVGRALMAKPR--LLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADY 208
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADH 207
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-194 |
9.89e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 9.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 24 VSLEVGEGqIVTVIGPNGAGKTTLLSAIMGVLPSQGG----------------------ITFG-------GKAQEHAEIE 74
Cdd:COG3593 17 LSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieieLTFGsllsrllRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 75 EMVAAGMNLVPEKRELFAEMT--VEDNLMLGAFDR--YRRGLRDQDQTLAEVFEL-FPRLQERRAQLAGTlsgGERQM-- 147
Cdd:COG3593 96 ELEEALEELNEELKEALKALNelLSEYLKELLDGLdlELELSLDELEDLLKSLSLrIEDGKELPLDRLGS---GFQRLil 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2495741221 148 LAVGRALM-----AKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILL 194
Cdd:COG3593 173 LALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-212 |
1.15e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 30 EGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGIT-----------FGGKA-QEHAEieeMVAAG----------MNLVPE 86
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkPNLGDYDeepswdevlkrFRGTElQDYFK---KLANGeikvahkpqyVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 87 krelFAEMTVEDNLMlgafdRY-RRGLRDQdqtLAEVFELFPRLqERRAqlaGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:COG1245 175 ----VFKGTVRELLE-----KVdERGKLDE---LAEKLGLENIL-DRDI---SELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2495741221 166 PS--LGLAPRIvrEVFRIVARLREMGVSILLIEQNArAALQ-VADYAYVL 212
Cdd:COG1245 239 PSsyLDIYQRL--NVARLIRELAEEGKYVLVVEHDL-AILDyLADYVHIL 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-165 |
4.04e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 33 IVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFggkaqEHAEIEEMVAAGMNLVPEKRELFAEMTVEDNLMLGAfdryrrG 111
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMqPSSGNIYY-----KNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWS------E 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 112 LRDQDQTLAEVFELFpRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:PRK13541 97 IYNSAETLYAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-195 |
4.62e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 4 KLLQVRDLRVAYDKVE-AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAEIEEMvaagm 81
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVTAEQPEDY----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 nlvpekRELFAEMTVEDNLmlgaFDRyrrgLRDQDQTLAE---VFELFPRLQ-ERRAQLAG------TLSGGERQMLAVG 151
Cdd:PRK10522 396 ------RKLFSAVFTDFHL----FDQ----LLGPEGKPANpalVEKWLERLKmAHKLELEDgrisnlKLSKGQKKRLALL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2495741221 152 RALMAKPRLLMLDEPSLGLAPRIVREVFR-IVARLREMGVSILLI 195
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAI 506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-170 |
6.92e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 82 NLVPEKRELFaEMTVEDNLMLGAFDRYRRGLRDQDQTLA--EVFELFPRLQERRAQLAG-TLSGGERQMLAVGRALMAKP 158
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAidEFIESLPNKYDTNVGPYGkSLSGGQKQRIAIARALLREP 1377
|
90
....*....|..
gi 2495741221 159 RLLMLDEPSLGL 170
Cdd:PTZ00265 1378 KILLLDEATSSL 1389
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-69 |
1.26e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 1.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2495741221 22 SGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQE 69
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARFNKAANA 60
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-166 |
1.46e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 26 LEVGEGQIVTVIGPNGAGKTTLLSAIMG-VLPSQGGITFggkAQE------------HAE--IEEMVAAGMNLVPEKREL 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIY---EQDlivarlqqdpprNVEgtVYDFVAEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 91 FAEMtvednLMLGAFDRYRRGLRdQDQTLAEVFE------LFPRLQERRAQLA-------GTLSGGERQMLAVGRALMAK 157
Cdd:PRK11147 101 YHDI-----SHLVETDPSEKNLN-ELAKLQEQLDhhnlwqLENRINEVLAQLGldpdaalSSLSGGWLRKAALGRALVSN 174
|
....*....
gi 2495741221 158 PRLLMLDEP 166
Cdd:PRK11147 175 PDVLLLDEP 183
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-210 |
2.15e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 34 VTVI-GPNGAGKTTLLSAIMGVLpsqggitFGGKAQehaeieemvaaGMNLVPEKRELFAEMTVEDNLML---GAFDRYR 109
Cdd:cd03240 24 LTLIvGQNGAGKTTIIEALKYAL-------TGELPP-----------NSKGGAHDPKLIREGEVRAQVKLafeNANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 110 RGLRDQDQTLAEVF----ELF-PRLQERraqlaGTLSGGERQM------LAVGRALMAKPRLLMLDEPSLGL-APRIVRE 177
Cdd:cd03240 86 TITRSLAILENVIFchqgESNwPLLDMR-----GRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLdEENIEES 160
|
170 180 190
....*....|....*....|....*....|...
gi 2495741221 178 VFRIVARLREMGVSILLIEQNARAALQVADYAY 210
Cdd:cd03240 161 LAEIIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-167 |
2.16e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 6 LQVR-DLRVAYDKVEAVsgvsleVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGG-ITFGGK---AQEHAEIEEMVAAG 80
Cdd:PRK10636 7 LQIRrGVRVLLDNATAT------INPGQKVGLVGKNGCGKSTLLALLKNEISADGGsYTFPGNwqlAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 81 MNLV----PEKRELFAEMTVEDNLMLGAFDRYRRGLRDQDQTL---AEVFELFPRL---QERRAQLAGTLSGGERQMLAV 150
Cdd:PRK10636 81 LEYVidgdREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWtirSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNL 160
|
170
....*....|....*..
gi 2495741221 151 GRALMAKPRLLMLDEPS 167
Cdd:PRK10636 161 AQALICRSDLLLLDEPT 177
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-231 |
3.95e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 137 AGTLSGGERQ--MLA--VGRALMAKprLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaRAALQVADyaYVL 212
Cdd:COG0178 483 AGTLSGGEAQriRLAtqIGSGLVGV--LYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHD-EDTIRAAD--YII 557
|
90 100
....*....|....*....|....*..
gi 2495741221 213 ET--------GTVTLEGPAAKVAQDPR 231
Cdd:COG0178 558 DIgpgagehgGEVVAQGTPEEILKNPD 584
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-165 |
5.43e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 20 AVSGVSLEVGEGQIVTVIGPNGAGKTTLLSAIMGVL-PSQGGITFGGKAQEHAeieemVAAGMNlvpekRELFAEMTVED 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLsPTVGKVDRNGEVSVIA-----ISAGLS-----GQLTGIENIEF 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2495741221 99 NLMLGAFDRyrrglRDQDQTLAEVFElFPRLQERRAQLAGTLSGGERQMLAVGRALMAKPRLLMLDE 165
Cdd:PRK13546 109 KMLCMGFKR-----KEIKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
34-55 |
5.94e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 5.94e-04
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
13-185 |
8.23e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 39.50 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 13 VAYDKVEAVSGVSLEVgegqivtVIGPNGAGKTTLLSAImgVLPSQGGITFGGKAqehAEIEEMVAAGmnlvpeKRELFA 92
Cdd:cd03277 12 VTYDETEFRPGPSLNM-------IIGPNGSGKSSIVCAI--CLGLGGKPKLLGRA---KKVGEFVKRG------CDEGTI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 93 EMTVE--------DNLM-------LGAFDRyrrglrdqdQTLAEVFELFpRLQERRAQLAGTL-SGGERQmLAVGRALMA 156
Cdd:cd03277 74 EIELYgnpgniqvDNLCqflpqdrVGEFAK---------LSPIELLVKF-REGEQLQELDPHHqSGGERS-VSTMLYLLS 142
|
170 180 190
....*....|....*....|....*....|....
gi 2495741221 157 KPRLL-----MLDEPSLGLAPRIVREVFRIVARL 185
Cdd:cd03277 143 LQELTrcpfrVVDEINQGMDPTNERKVFDMLVET 176
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
7-195 |
9.40e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 38.64 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 7 QVRDLRVAYDKVEAvsgvslevGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAgmnlvPE 86
Cdd:pfam13191 8 ELEQLLDALDRVRS--------GRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEA-----LT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 87 KRELFAEmtVEDNLMLGAFDRYRRGLrdqDQTLAEVFELFPRLQERRAQLAgtlsggeRQMLAVGRALmAKPRLLMLDEp 166
Cdd:pfam13191 75 REGLLRQ--LLDELESSLLEAWRAAL---LEALAPVPELPGDLAERLLDLL-------LRLLDLLARG-ERPLVLVLDD- 140
|
170 180
....*....|....*....|....*....
gi 2495741221 167 sLGLAPRIVREVFRIVARLREMgVSILLI 195
Cdd:pfam13191 141 -LQWADEASLQLLAALLRLLES-LPLLVV 167
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-133 |
1.09e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 33 IVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRELFAEMTVEDNLMlgafDRYRRGL 112
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDG----VRYRYGL 76
|
90 100
....*....|....*....|.
gi 2495741221 113 RDQDQTLAEVFELFPRLQERR 133
Cdd:pfam13304 77 DLEREDVEEKLSSKPTLLEKR 97
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
93-208 |
1.31e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 93 EMTVEDnlmlgAFD------RYRRGLrdqdQTLAEVFELFPRLqerrAQLAGTLSGGERQ--MLA-------VGRALMak 157
Cdd:PRK00349 791 DMTVEE-----ALEffeaipKIARKL----QTLVDVGLGYIKL----GQPATTLSGGEAQrvKLAkelskrsTGKTLY-- 855
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2495741221 158 prllMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNaraaLQV---ADY 208
Cdd:PRK00349 856 ----ILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN----LDViktADW 901
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-212 |
1.40e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2495741221 137 AGTLSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLREMGVSILLIEQNARAALQVADYAYVL 212
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-167 |
1.65e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2495741221 127 PRLQERRAQlagTLSGGERQMLAVGRALMAKPRLLMLDEPS 167
Cdd:PLN03073 335 PEMQVKATK---TFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-98 |
1.72e-03 |
|
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: 37.74 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2495741221 31 GQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITFGGKAQEHAEIEEMVAAGMNLVPEKRELFAEMTVED 98
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-213 |
2.85e-03 |
|
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: 37.55 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 27 EVGEGQIVTVIGPNGAGKTTLLSAIMGVLPSQGGITfggkaqehaeieemvaagmnlvpekrelfaemtvednlmlgAFD 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----------------------------------------EWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 107 RYRRGLRDQDQTLaevfelfprlqerraqlagtlSGGERQMLAVGRALMAKPRLLMLDEPSLGLAPRIVREVFRIVARLR 186
Cdd:cd03222 60 GITPVYKPQYIDL---------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 2495741221 187 EMGV-SILLIEQNARAALQVADYAYVLE 213
Cdd:cd03222 119 EEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
34-51 |
2.95e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 2.95e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
93-208 |
3.93e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495741221 93 EMTVEDNL-MLGAFDRYRRGLrdqdQTLAEVfelfpRLqerrAQLAGTLSGGERQMLAVGRALMAKPR---LLMLDEPSL 168
Cdd:COG0178 787 DMTVEEALeFFENIPKIARKL----QTLQDVglgyiKL----GQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTT 858
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2495741221 169 GLAPRIVR---EVFRivaRLREMGVSILLIEQNaraaLQV---ADY 208
Cdd:COG0178 859 GLHFHDIRkllEVLH---RLVDKGNTVVVIEHN----LDViktADW 897
|
|
| |
