|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
8.94e-137 |
|
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: 383.18 E-value: 8.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGFF-TEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYArRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYLGG 233
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
5.17e-127 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 358.81 E-value: 5.17e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 161 SLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYLGG 233
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
3.18e-119 |
|
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: 338.25 E-value: 3.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 162 LGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-220 |
5.40e-74 |
|
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: 223.94 E-value: 5.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGgFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 162 LGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.36e-61 |
|
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: 193.33 E-value: 1.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAv 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 vpegR-----RVFARLTVEENLAMG--------------GFFTEKADYQEQMDKVLQL--FPRLKERFNQRGGTMSGGEQ 139
Cdd:COG0411 83 ----RtfqnpRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 140 QMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGE 218
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|....*
gi 492048676 219 ELLVDPKVRDAYLGG 233
Cdd:COG0411 239 EVRADPRVIEAYLGE 253
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
4.28e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.43 E-value: 4.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAVV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLA-MGGFF-TEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRfFARLYgLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-226 |
1.47e-57 |
|
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: 182.25 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIavv 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 peGR-----RVFARLTVEENLAMG------------GFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAI 144
Cdd:cd03219 78 --GRtfqipRLFPELTVLENVMVAaqartgsglllaRARREEREARERAEELLERV-GLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 492048676 225 KV 226
Cdd:cd03219 235 RV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
3.13e-54 |
|
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: 173.88 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENL--AMGGFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03218 81 PQEASIFRKLTVEENIlaVLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYLG 232
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-231 |
3.62e-51 |
|
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: 166.19 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAV 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAmggFFTE-----KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:COG4555 79 LPDERGLYDRLTVRENIR---YFAElyglfDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL---VDPKVRDAYL 231
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeiGEENLEDAFV 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
6.06e-49 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 160.98 E-value: 6.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAV 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-SRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG------GFFTEKADYQEQMDKVLQLF--PRLKERfnqRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlgLFGRPSAEDREAVEEALERTglEHLADR---PVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAY 230
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-232 |
7.72e-49 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 160.19 E-value: 7.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiiM----RK 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MhkraRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLAMggfFTE-----KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILA---VLElrklsKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYL 231
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYL 234
|
.
gi 492048676 232 G 232
Cdd:COG1137 235 G 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-211 |
8.03e-49 |
|
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: 157.94 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAVV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLamggfftekadyqeqmdkvlqlfprlkerfnqrggTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492048676 162 LGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-232 |
9.97e-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: 159.75 E-value: 9.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFprlkERFN------QRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALL----EEFQishlrdNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYLG 232
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
8.30e-47 |
|
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: 154.80 E-value: 8.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVS-TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIAV 80
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 V---PEgRRVFARlTVEENLAMG----GFftEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPK 153
Cdd:COG1122 80 VfqnPD-DQLFAP-TVEEDVAFGpenlGL--PREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 154 LLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-220 |
1.95e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 151.18 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG-----SPRAHSGSIRYMGEELVGLESSII-MR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLeLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 76 KSIAVVPEGRRVFaRLTVEENLAMGGFFTEKADYQEQMDKVLQ------LFPRLKERFNQRGgtMSGGEQQMLAIGRALM 149
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEEalrkaaLWDEVKDRLHALG--LSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-210 |
1.58e-44 |
|
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: 148.38 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 3 QFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIAV 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 V---PEGRrvFARLTVEENLAMG--GFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:cd03225 80 VfqnPDDQ--FFGPTVEEEVAFGleNLGLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGR 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-212 |
2.02e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 148.28 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKS 77
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARLTVEENLA-----MGgffTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAlplrvTG---KSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
2.26e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiiMRKSIAV 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEgRRVFAR---LTVEENLAMG-----GFF--TEKADYQ---EQMDKVlqlfpRLKERFNQRGGTMSGGEQQMLAIGRA 147
Cdd:COG1121 80 VPQ-RAEVDWdfpITVRDVVLMGrygrrGLFrrPSRADREavdEALERV-----GLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 148 LMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLeNGRVVMQGTGEELLVDPKVR 227
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLS 232
|
...
gi 492048676 228 DAY 230
Cdd:COG1121 233 RAY 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
5.34e-44 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 148.21 E-value: 5.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENL-----------AMGGFFTEKA---DYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLlvaqhqqlktgLFSGLLKTPAfrrAESEALDRAATWLERvgLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
....*....
gi 492048676 224 PKVRDAYLG 232
Cdd:PRK11300 245 PDVIKAYLG 253
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-160 |
2.80e-43 |
|
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: 143.17 E-value: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiIMRKSIAVVPEGRRVFARLTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 97 LAMGG--FFTEKADYQEQMDKVLQLFPR---LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:pfam00005 80 LRLGLllKGLSKREKDARAEEALEKLGLgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
3.67e-43 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 144.60 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 3 QFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiiMRKSIAVVP 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 83 EgRRVFAR---LTVEENLAMG-----GFFteKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:cd03235 75 Q-RRSIDRdfpISVRDVVLMGlyghkGLF--RRLSKADKAKVDEALERvgLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLeNGRVVMQG 215
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.09e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.67 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-MRKSIA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINkLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERvgLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-230 |
1.47e-41 |
|
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: 141.55 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG-KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSI 78
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAMG------------GFFTeKADYQeqmdKVLQLFPR--LKERFNQRGGTMSGGEQQMLAI 144
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslfGLFP-KEEKQ----RALAALERvgLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEElLVD 223
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTD 234
|
....*..
gi 492048676 224 PKVRDAY 230
Cdd:cd03256 235 EVLDEIY 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-220 |
4.25e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 146.32 E-value: 4.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG------GFFtekaDYQEQMDKVLQLFPRLKERFN--QRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGreprrgGLI----DWRAMRRRARELLARLGLDIDpdTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-211 |
5.64e-41 |
|
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: 139.16 E-value: 5.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSIIM 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARLTVEENLAMGGFFTEKAdYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVP-KKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNaNQALKVADRAYVLENGRV 211
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
6.95e-41 |
|
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: 139.56 E-value: 6.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS--IIMRKSIA 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARLTVEENLAMggFFTEKADYQEQM--DKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF--PLREHTRLSEEEirEIVLEKLEAvgLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLV--DPKVRD 228
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLVRQ 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
1.98e-40 |
|
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: 135.84 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 3 QFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRKSIAVVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD-IAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 83 egrrvfarltveenlamggfftekadyqeqmdkvlQLfprlkerfnqrggtmSGGEQQMLAIGRALMSKPKLLLLDEPSL 162
Cdd:cd00267 80 -----------------------------------QL---------------SGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492048676 163 GLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGR 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
3.18e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 138.71 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAV 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW-SPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRV-FArLTVEENLAMG--GFFTEKADYQEQMDKVLQLF--PRLKERFNQrggTMSGGEQQMLAIGRAL------- 148
Cdd:COG4559 80 LPQHSSLaFP-FTVEEVVALGraPHGSSAAQDRQIVREALALVglAHLAGRSYQ---TLSGGEQQRVQLARVLaqlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 149 MSKPKLLLLDEP--SLGLAPiiIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKV 226
Cdd:COG4559 156 DGGPRWLFLDEPtsALDLAH--QHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELL 233
|
....
gi 492048676 227 RDAY 230
Cdd:COG4559 234 ERVY 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
9.67e-40 |
|
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: 135.01 E-value: 9.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSI-IMRKSIAV 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGgfftekadyqeqmdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 161 SLGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKVADRAYVLENGR 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-211 |
1.15e-39 |
|
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: 135.74 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSI-IMRKSIAV 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492048676 159 EPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.27e-39 |
|
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: 142.73 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY-----GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-- 73
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVV---PEGrRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQ------LFPRLKERFnqrGGTMSGGEQQMLAI 144
Cdd:COG1123 340 LRRRVQMVfqdPYS-SLNPRMTVGDIIAEPLRLHGLLSRAERRERVAEllervgLPPDLADRY---PHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
..
gi 492048676 224 PK 225
Cdd:COG1123 496 PQ 497
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-212 |
3.03e-39 |
|
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: 132.94 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 pegrrvfarltveenlamggfftekadYQeqmdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:cd03216 81 ---------------------------YQ-----------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 162 LGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-220 |
3.09e-39 |
|
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: 134.80 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAVVPEG 84
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 RRVFARLTVEENLAMGG--FFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSL 162
Cdd:cd03265 82 LSVDDELTGWENLYIHArlYGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 163 GLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
9.03e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 9.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL-----VGLESSIIMRK 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLK-----ERFNQRggtMSGGEQQMLAIGRALMSK 151
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRltdkaDRFPLH---LSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGE 218
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.62e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.38 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiimrksiav 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 vPEGRRV---------FARLTVEENLA----MGGFftEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRA 147
Cdd:COG3842 74 -PEKRNVgmvfqdyalFPHLTVAENVAfglrMRGV--PKAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 148 LMSKPKLLLLDEPSLGL-APIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:COG3842 150 LAPEPRVLLLDEPLSALdAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
1.93e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 133.68 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSI-IMRKSIA 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
2.30e-38 |
|
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: 132.26 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiIMRKSIAVV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMG--GFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGlkLRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 160 PSLGLAPIIIQQIF-EIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03259 157 PLSALDAKLREELReELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
2.41e-38 |
|
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: 133.18 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS--IIMRKSI 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAmggF----FTE--KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVA---FplreHTDlsEAEIRELVLEKLELV-GLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL--VDPKVRD 228
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDPWVRQ 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
2.78e-38 |
|
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: 131.02 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAVVPeg 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELARKIAYVP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 rrvfarltveenlamggfftekadyqeQMDKVLQLFPrLKER-FNqrggTMSGGEQQMLAIGRALMSKPKLLLLDEPSLG 163
Cdd:cd03214 80 ---------------------------QALELLGLAH-LADRpFN----ELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492048676 164 LAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
3.46e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.47 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYG----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSII 73
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVVPEGRRVFARLTVEENLAMGGFF--TEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLagVSRKERRERARELLERV-GLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 152 PKLLLLDEP--SL----GlapiiiQQIFEIVEQLRRD-GVTVFLVEQNANQAlKVADRAYVLENGRVV 212
Cdd:COG1136 163 PKLILADEPtgNLdsktG------EEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
1.07e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 132.13 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS-TFY-GKI---QALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLessiimr 75
Cdd:COG1101 1 MLELKNLSkTFNpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 76 ksiavvPEGRR------VF--------ARLTVEENLAM----GGFFT--------EKADYQEQMdKVLQLfpRLKERFNQ 129
Cdd:COG1101 74 ------PEYKRakyigrVFqdpmmgtaPSMTIEENLALayrrGKRRGlrrgltkkRRELFRELL-ATLGL--GLENRLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 130 RGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLEN 208
Cdd:COG1101 145 KVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
250
....*....|.
gi 492048676 209 GRVVMQGTGEE 219
Cdd:COG1101 225 GRIILDVSGEE 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
1.10e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL-----VGLESSIIMRK 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLK-----ERFNQRggtMSGGEQQMLAIGRALMSK 151
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRlkpyaDRFPLH---LSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGT 216
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
1.41e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 131.36 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG-SPRAHSGSIRYMGEELvGLESSIIMRKSIA 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERR-GGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VV-PE-GRRVFARLTVEEnLAMGGFF--------TEKADyQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:COG1119 82 LVsPAlQLRFPRDETVLD-VVLSGFFdsiglyrePTDEQ-RERARELLELL-GLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDG-VTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRD 228
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
|
..
gi 492048676 229 AY 230
Cdd:COG1119 239 AF 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.60e-37 |
|
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: 136.96 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG---SPRAHSGSIRYMGEELVGLeSSIIMR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLEL-SEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 76 KSIAVVP-EGRRVFARLTVEENLAMGgFFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG1123 83 RRIGMVFqDPMTQLNPVTVGDQIAEA-LENLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
3.17e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCgspRAH--------SGSIRYMGEElvglessiI 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN---RMNdlipgarvEGEILLDGED--------I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVVPEGRR---VFAR-----LTVEENLAMG----GfFTEKADYQEQMDKVLQ---LFPRLKERFNQRGGTMSGGE 138
Cdd:COG1117 81 YDPDVDVVELRRRvgmVFQKpnpfpKSIYDNVAYGlrlhG-IKSKSELDEIVEESLRkaaLWDEVKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 139 QQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGE 218
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTE 238
|
....*..
gi 492048676 219 ELLVDPK 225
Cdd:COG1117 239 QIFTNPK 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
3.73e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.66 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW-SPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGG--FFTEKADYQEQMDKVLQL--FPRLKERFNQrggTMSGGEQQMLAIGRALM------S 150
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRapHGLSRAEDDALVAAALAQvdLAHLAGRDYP---QLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 151 KPKLLLLDEP--SLGLApiiiQQ--IFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK13548 158 PPRWLLLDEPtsALDLA----HQhhVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
....*
gi 492048676 226 VRDAY 230
Cdd:PRK13548 234 LRRVY 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
3.97e-37 |
|
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: 129.55 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY----GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSI--IM 74
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPE--GRRVFARLTVEENLAMG----GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPlrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
4.18e-37 |
|
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: 130.31 E-value: 4.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRK 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP-VTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVV---PEGRrVFARLTVEENLAMGGFFTEKADYQEQMDKVLQ---LFPRLKERFnqrGGTMSGGEQQMLAIGRALMS 150
Cdd:COG1124 80 RVQMVfqdPYAS-LHPRHTVDRILAEPLRIHGLPDREERIAELLEqvgLPPSFLDRY---PHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-210 |
6.44e-37 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 128.91 E-value: 6.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKS 77
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLplLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARLTVEENLAM-----GgffTEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALplevrG---KKEREIQRRVGAALRQVG-LEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGR 210
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-232 |
1.38e-36 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 128.86 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFprlkERF------NQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELM----EEFhiehlrDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAYLG 232
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
2.34e-36 |
|
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: 134.12 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIAV 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFArLTVEENLAMGgffTEKADyQEQMDKVLQ------LFPRLKERFN----QRGGTMSGGEQQMLAIGRALMS 150
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLG---RPDAS-DEELEAALEaagldeFVAALPDGLDtplgEGGRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVEQNAnQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-212 |
3.84e-36 |
|
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: 126.82 E-value: 3.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLessiimRKS 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP------GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARLTVEENLAMG--GFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGleLQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 156 LLDEPSLGLAPII---IQQifEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLEN--GRVV 212
Cdd:cd03293 154 LLDEPFSALDALTreqLQE--ELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-211 |
4.11e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.47 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAVV 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 P------EGrrvfarlTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:COG4619 80 PqepalwGG-------TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIV-EQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLrEYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
1.00e-35 |
|
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: 126.20 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiIMRKSIAVV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGFF--TEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLkkLPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 160 PSLGLAPIIIQQI-FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:cd03300 157 PLGALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
1.01e-35 |
|
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: 133.42 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIA 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAMGGfftEKADyQEQMDKVLQLF------PRLKERFNQ----RGGTMSGGEQQMLAIGRALM 149
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGD---PDAT-DEEIIEAARLAglhdfiEALPMGYDTvvgeGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVeqnAN--QALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIII---AHrlSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
1.48e-35 |
|
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: 125.02 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAVV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA---LRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGG--FFTEKADYQEQMDKVLqlfprLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLArlLGIRKKRIDEVLDVVG-----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
1.50e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 125.56 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRK 76
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLA-MGGFFTEKADYQEQ-MDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTArLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
3.03e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.76 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvglesSIIMRKSIAV 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAmggFFTE-----KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:COG4152 76 LPEERGLYPKMKVGEQLV---YLARlkglsKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-225 |
3.43e-35 |
|
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: 125.00 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYG----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--M 74
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARLTVEENLA----MGGffTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAlpleIAG--VPKAEIEERVLELLELV-GLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
9.78e-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: 122.97 E-value: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIimRKSIAV 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY--RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENL----AMGGFFTEKADYQEQMDKVlqlfpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:COG4133 80 LGHADGLKPELTVRENLrfwaALYGLRADREAIDEALEAV-----GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 157 LDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVeqnANQALKV-ADRAYVLENGR 210
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLT---THQPLELaAARVLDLGDFK 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
1.35e-34 |
|
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: 129.50 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIA 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-RRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAMGgffTEKADyQEQMDKVLQ------LFPRLKERFN----QRGGTMSGGEQQMLAIGRALM 149
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLA---RPDAT-DEELWAALErvglgdWLAALPDGLDtwlgEGGRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGvTVFLVEQNAnQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
4.19e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.80 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS-TFY---GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS--IIM 74
Cdd:COG1135 1 MIELENLSkTFPtkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARLTVEENLAM-----GgffTEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALpleiaG---VPKAEIRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-212 |
5.15e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVS-TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvgleSSIIMRKSIAVVP- 82
Cdd:cd03226 3 ENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVMq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 83 EGRRVFARLTVEENLAMGGffTEKADYQEQMDKVLQLFP--RLKERFNQrggTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:cd03226 79 DVDYQLFTDSVREELLLGL--KELDAGNEQAETVLKDLDlyALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492048676 161 SLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
1.39e-33 |
|
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: 120.30 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQ--ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIA 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARLTVEENLAmggFFT-----EKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:cd03263 79 YCPQFDALFDELTVREHLR---FYArlkglPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-225 |
1.50e-33 |
|
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: 120.52 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQaLHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAVV 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGgFFTEKADYQEQMDKVLQLFPRLK--ERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
2.46e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.58 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS----TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLessiimRK 76
Cdd:COG1116 7 ALELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------GP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLAMG----GffTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGlelrG--VPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPsLG----LAPIIIQQifEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLEN--GRVVmqgtgEELLVD-PK 225
Cdd:COG1116 158 EVLLMDEP-FGaldaLTRERLQD--ELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV-----EEIDVDlPR 229
|
....
gi 492048676 226 VRDA 229
Cdd:COG1116 230 PRDR 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-210 |
6.89e-33 |
|
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: 117.10 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIA 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLamggfftekadyqeqmdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRdGVTVFLVEQNANqALKVADRAYVLENGR 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAK-GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-215 |
7.39e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 118.15 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvglesSIIMRKSIAVV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAmggFFTE-----KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLV---YLAQlkglkKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 157 LDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
8.55e-33 |
|
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: 118.94 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQ-ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRKSIAV 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED-IREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLA----MGGFftEKADYQEQMDKVLQLFPRLKERFNQR-GGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAlvpkLLKW--PKEKIRERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
8.25e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 8.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKiQALHsVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiimrksiav 80
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 vPEGRRV---------FARLTVEENLAMGgfF--------TEKADYQEQMDKV-----LQLFPrlkerfnqrgGTMSGGE 138
Cdd:COG3840 68 -PAERPVsmlfqennlFPHLTVAQNIGLG--LrpglkltaEQRAQVEQALERVglaglLDRLP----------GQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 139 QQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTG 217
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
250
....*....|....*..
gi 492048676 218 EELLV--DPKVRDAYLG 232
Cdd:COG3840 215 AALLDgePPPALAAYLG 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-227 |
9.22e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 121.04 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGFFTEK------ADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-225 |
1.85e-31 |
|
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: 115.51 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiIMRKSIAVV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMG------GFFTEKADYQEQMDKVLQL--FPRLKERF-NQrggtMSGGEQQMLAIGRALMSKP 152
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGlrvkprSERPPEAEIRAKVHELLKLvqLDWLADRYpAQ----LSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-211 |
2.71e-31 |
|
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: 114.04 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSI 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAMGGFFTEKA--DYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPprEIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 157 LDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-212 |
1.54e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG-----GFFTEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGleptkGGRLDRKAARARIRELSERYG-LDVDPDAKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:COG3845 164 ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-225 |
3.42e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.56 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG----SPRAH-SGSIRYMGEELVGLESSII-M 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTiTGSIVYNGHNIYSPRTDTVdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFArLTVEENLAMG---GFFTEKADYQEQMDKVLQ---LFPRLKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGlrlKGIKDKQVLDEAVEKSLKgasIWDEVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-211 |
3.80e-30 |
|
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: 110.21 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTfygkIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRR---VFARLTVEENLAMGGFFtekadyqeqmdkvlqlfprlkerfnqrggtmSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:cd03215 80 VPEDRKregLVLDLSVAENIALSSLL-------------------------------SGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-224 |
4.44e-30 |
|
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: 114.44 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIM---RKSIAVVPEGRRVFARLTVEEN 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMGGFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIV 176
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492048676 177 EQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:TIGR02142 175 ERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-225 |
6.41e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAV 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK---DRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG----GffTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPlklrK--VPKAEIDRRVREAAELL-GLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 157 LDEPslgL----APIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:COG3839 157 LDEP---LsnldAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPA 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-222 |
1.11e-29 |
|
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: 110.39 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 3 QFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAVV 81
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARlTVEENLAMGGFFTEKADYQE-----QMDKVLQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEaakeaGAHDFIMKLPNgYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLrRDGVTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELLV 222
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-224 |
1.36e-29 |
|
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: 112.89 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIM---RKSIAVVPEGRRVFARLTVEEN 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpphRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMGGFFTEKADYQEQMDKVLQLF---PRLkerfNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP--SLGLApiIIQQ 171
Cdd:COG4148 98 LLYGRKRAPRAERRISFDEVVELLgigHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPlaALDLA--RKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 172 IFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:COG4148 172 ILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-221 |
1.42e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKSI 78
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGgffTEKADYQE--------QMDKVLQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:COG1132 417 GVVPQDTFLFSG-TIRENIRYG---RPDATDEEveeaakaaQAHEFIEALPDgYDTVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVeqnanqA-----LKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI------AhrlstIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
2.27e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.16 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvglessiimrkSIAVV 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-----------FTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRV---------FARLTVEENLAMG--GFFTEKADYQEQMDKVLQLF--PRLKERF-NQrggtMSGGEQQMLAIGRA 147
Cdd:COG1118 72 PRERRVgfvfqhyalFPHMTVAENIAFGlrVRPPSKAEIRARVEELLELVqlEGLADRYpSQ----LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 148 LMSKPKLLLLDEPslglapiiiqqiF---------EIVEQLRR-----DGVTVFlVEQNANQALKVADRAYVLENGRVVM 213
Cdd:COG1118 148 LAVEPEVLLLDEP------------FgaldakvrkELRRWLRRlhdelGGTTVF-VTHDQEEALELADRVVVMNQGRIEQ 214
|
250
....*....|..
gi 492048676 214 QGTGEELLVDPK 225
Cdd:COG1118 215 VGTPDEVYDRPA 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-215 |
3.26e-29 |
|
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: 108.73 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 6 NVSTFYGKIQALHsVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAVVPEGR 85
Cdd:cd03298 4 DKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 86 RVFARLTVEENLAMG---GFFTEKADyQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSL 162
Cdd:cd03298 80 NLFAHLTVEQNVGLGlspGLKLTAED-RQAIEVALARVG-LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 163 GLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
3.63e-29 |
|
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: 108.50 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAVV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMG----GFftEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlklrKV--PKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 158 DEPSLGL-APIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03301 155 DEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-215 |
8.74e-29 |
|
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: 107.77 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 18 HSVNVD-VRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIM---RKSIAVVPEGRRVFARLTV 93
Cdd:cd03297 13 FTLKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAMGGFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIF 173
Cdd:cd03297 93 RENLAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492048676 174 EIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.16e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRksIAVV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--VGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGG--FFTEKADYQEQMDKVLQlFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGryFGLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-228 |
1.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIA 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VV---PEGRrvFARLTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERFnQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:PRK13644 81 IVfqnPETQ--FVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQaLKVADRAYVLENGRVVMQGTGEELLVDPKVRD 228
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-215 |
6.60e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 104.32 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiiMRKSIA 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAmggfftekadyqeqmdkvlqlfprlkERFnqrggtmSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNLG--------------------------RRF-------SGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGvTVFLVEQNAnQALKVADRAYVLENGRVVMQG 215
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDK-TLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-220 |
6.70e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRR---VFARLT 92
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 93 VEENLAM--------GGFF---TEKADYQEQMDKVlqlfpRLK-ERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:COG1129 347 IRENITLasldrlsrGGLLdrrRERALAEEYIKRL-----RIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 161 SLGlapiiI-----QQIFEIVEQLRRDGVTVFLV-----EqnanqALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:COG1129 422 TRG-----IdvgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRIVGELDREEA 481
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
1.06e-27 |
|
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: 107.45 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY----GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG--SPRAH-SGSIRYMGEELVGL---ES 70
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllPPPGItSGEILFDGEDLLKLsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 71 SIIMRKSIAVV---------PegrrvfaRLTVEENLAMGGFFTEKADYQEQMDKVLQLF-----PRLKERFNQRGGTMSG 136
Cdd:COG0444 81 RKIRGREIQMIfqdpmtslnP-------VMTVGDQIAEPLRIHGGLSKAEARERAIELLervglPDPERRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 137 GEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|
gi 492048676 216 TGEELLVDPK 225
Cdd:COG0444 234 PVEELFENPR 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.69e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGleSSIIMRKSIAVV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAM-GGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVfGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 161 SLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
2.40e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 104.92 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMT------LCGSPRAHsGSIRYMGEELVGLE-SSIIM 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVE-GEVRLFGRNIYSPDvDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQ-------LFPRLKERFNQRGGTMSGGEQQMLAIGRA 147
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 148 LMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-201 |
4.05e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.48 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMT------LCGSPRAhSGSIRYMGEELVGLE-SSIIM 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRV-EGKVTFHGKNLYAPDvDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARlTVEENLAMG----GFfteKADYQEQMDKVLQ---LFPRLKERFNQRGGTMSGGEQQMLAIGRA 147
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYGarinGY---KGDMDELVERSLRqaaLWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 148 LMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVAD 201
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-212 |
5.17e-27 |
|
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: 103.67 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSIIMRKSIAVvpegrrVF 88
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARHVGF------VF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ------ARLTVEENLAMGgffTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:COG4181 97 qsfqllPTLTALENVMLP---LELAGRRDARARARALLERvgLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 161 SLGL----APIIIQQIFEiveqLRRD-GVTVFLVEQNANQALKvADRAYVLENGRVV 212
Cdd:COG4181 174 TGNLdaatGEQIIDLLFE----LNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
5.49e-27 |
|
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: 103.05 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIA 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAMGGFFtekADYQEQMDK-----VLQLFPRLKERFN----QRGGTMSGGEQQMLAIGRALMS 150
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPL---ADDERILRAaelagVTDFVNKHPNGLDlqigERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNAnqALKVADRAYVLENGRVVMQG 215
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-225 |
9.60e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 105.27 E-value: 9.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS-TFYGK---IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS--IIM 74
Cdd:PRK11153 1 MIELKNISkVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARLTVEENLAM----GGffTEKADYQEqmdKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALplelAG--TPKAEIKA---RVTELLELvgLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-218 |
1.03e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 102.65 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKS 77
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARLTVEENLAM----GGFFTE--KADYQEQMDKVlQLFPRLKERFNQrggtMSGGEQQMLAIGRALMSK 151
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIpliiAGASGDdiRRRVSAALDKV-GLLDKAKNFPIQ----LSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGE 218
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-230 |
1.27e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsIAV 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG-----GFF-----TEKADYQEQMDKVlqlfprLKERFNQRGGT-MSGGEQQMLAIGRALM 149
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphrSRFdtwteTDRAAVERAMERT------GVAQFADRPVTsLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 150 SKPKLLLLDEPSLGLApiIIQQI--FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQVrtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
...
gi 492048676 228 DAY 230
Cdd:PRK09536 234 AAF 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
1.44e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 106.55 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG-SPRA-HSGSIRYMGEELVGleSSI------ 72
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGtYEGEIIFEGEELQA--SNIrdtera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 ---IMRKSIAVVPEgrrvfarLTVEENLAMGGFFTEKA--DYQEQMDKVLQLFPRLKERFN--QRGGTMSGGEQQMLAIG 145
Cdd:PRK13549 83 giaIIHQELALVKE-------LSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 146 RALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVM 213
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-225 |
1.74e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLL------MTLCGSPRAhSGSIRYMGEELVGLESsIIMRKSIAVVPEG 84
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrlIELYPEARV-SGEVYLDGQDIFKMDV-IELRRRVQMVFQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 RRVFARLTVEENLAMG----GFFTEKADYQEQMDKVL---QLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK14247 91 PNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALekaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.90e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-MRKSI 78
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVV---PEGrRVFARlTVEENLAMGGFftekaDYQEQMDKVLQlfpRLKERFNQRGGT---------MSGGEQQMLAIGR 146
Cdd:PRK13639 81 GIVfqnPDD-QLFAP-TVEEDVAFGPL-----NLGLSKEEVEK---RVKEALKAVGMEgfenkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK- 225
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEt 230
|
....*.
gi 492048676 226 VRDAYL 231
Cdd:PRK13639 231 IRKANL 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
2.82e-26 |
|
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: 105.68 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG-SPRA-HSGSIRYMGEELVGLESSIIMRKSI 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGtWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAMGGFFTEKA---DYQEQMDKVLQLFPRLK---ERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGgrmAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-221 |
4.36e-26 |
|
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: 101.15 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK--IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLcgsPRAH---SGSIRYMGEEL--VGLESsiiM 74
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---PRFYdvdSGRILIDGHDVrdYTLAS---L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARlTVEENLAMGGFFTEKADYQE--QMDKVLQLFPRLKERFN----QRGGTMSGGEQQMLAIGRAL 148
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENIAYGRPGATREEVEEaaRAANAHEFIMELPEGYDtvigERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGvTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-227 |
4.73e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESsiiMRKSIAV 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMgGFFTEKADYQEQMDKVLQLFP--RLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLD 158
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAF-GLKQDKLPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 159 EPSLGLAPIIIQQI-FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK11607 175 EPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-222 |
1.23e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.84 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELV------GLESSI-IM 74
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAGVaII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEgrrvfarLTVEENLAMG------GFFTEKADYQEqmdkVLQLFPRLKERF--NQRGGTMSGGEQQMLAIGR 146
Cdd:PRK11288 85 YQELHLVPE-------MTVAENLYLGqlphkgGIVNRRLLNYE----AREQLEHLGVDIdpDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV-----MQGTGEELL 221
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVatfddMAQVDRDQL 233
|
.
gi 492048676 222 V 222
Cdd:PRK11288 234 V 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-225 |
1.28e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 6 NVSTFYGKIQ---ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTL------CGSPRAHSGSIRYMGEELVGLESsIIMRK 76
Cdd:PRK14246 12 NISRLYLYINdkaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQIDA-IKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLAM---GGFFTEKADYQEQMDKVLQ---LFPRLKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYplkSHGIKEKREIKKIVEECLRkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-215 |
1.67e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.80 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGeIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIimRKSIAVV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL--RRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLA----MGGFftEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:cd03264 78 PQEFGVYPNFTVREFLDyiawLKGI--PSKEVKARVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 158 DEPSLGLAPiiIQQI-F-EIVEQLRRDGVTVF---LVEQNANQALKVAdrayVLENGRVVMQG 215
Cdd:cd03264 155 DEPTAGLDP--EERIrFrNLLSELGEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-224 |
2.20e-25 |
|
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: 100.03 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSIIMRKSIAVVPEGRRVFARLT 92
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 93 VEENLAMG----GffTEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPII 168
Cdd:cd03294 119 VLENVAFGlevqG--VPRAEREERAAEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 169 IQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:cd03294 196 RREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-220 |
2.33e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.09 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG------SPRAHsgsIRYMGEElVGLESSII- 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdkSAGSH---IELLGRT-VQREGRLAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 -MRKSIA---VVPEGRRVFARLTVEENLAMGG------------FFTekadyQEQMDKVLQLFPR--LKERFNQRGGTMS 135
Cdd:PRK09984 80 dIRKSRAntgYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfsWFT-----REQKQRALQALTRvgMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 136 GGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRR-DGVTVFLVEQNANQALKVADRAYVLENGRVVMQ 214
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*.
gi 492048676 215 GTGEEL 220
Cdd:PRK09984 235 GSSQQF 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-189 |
3.36e-25 |
|
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: 102.75 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVS-TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiIMRKSIAV 80
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-SWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARlTVEENLAMGGFFTEKADYQEQMDKV-----LQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAgldefVAALPQgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLV 189
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLV 513
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-221 |
3.89e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYgkiQALH-SVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVgleSSIIMRKSIA 79
Cdd:PRK10771 1 MLKLTDITWLY---HHLPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT---TTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARLTVEENLAMG---GfFTEKADYQEQMDKVLQ------LFPRLKerfnqrgGTMSGGEQQMLAIGRALMS 150
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGlnpG-LKLNAAQREKLHAIARqmgiedLLARLP-------GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-231 |
3.93e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.44 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGgffteKADYQEQMDKVLQLFPRLKERFN--QRGGTMSGGEQQMLAIGRALMSKPKLLLLD 158
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG-----LPKRQASMQKMKQLLAALGCQLDldSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 159 EPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD-------PKVRDAYL 231
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdiiqaitPAAREKSL 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-221 |
5.14e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 3 QFENVS-TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLcgsPRAH---SGSIRYMGEEL--VGLESsiiMRK 76
Cdd:PRK13657 336 EFDDVSfSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL---QRVFdpqSGRILIDGTDIrtVTRAS---LRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARlTVEENLAMG------GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:PRK13657 410 NIAVVFQDAGLFNR-SIEDNIRVGrpdatdEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVeqnANQALKV--ADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMK-GRTTFII---AHRLSTVrnADRILVFDNGRVVESGSFDELV 557
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-210 |
6.50e-25 |
|
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: 97.89 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS-TFY-----GK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEE----LVGLE 69
Cdd:COG4778 4 LLEVENLSkTFTlhlqgGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 70 SSIIM---RKSIA-------VVPegrRVFARLTVEENLAMGGFFTEKADyqeqmDKVLQLFPRL--KER-FNQRGGTMSG 136
Cdd:COG4778 84 PREILalrRRTIGyvsqflrVIP---RVSALDVVAEPLLERGVDREEAR-----ARARELLARLnlPERlWDLPPATFSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 137 GEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVT---VF----LVEQnanqalkVADRAYVLENG 209
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAiigIFhdeeVREA-------VADRVVDVTPF 228
|
.
gi 492048676 210 R 210
Cdd:COG4778 229 S 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
9.55e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFEN-VSTFYGKiQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL-----VGLESSII- 73
Cdd:PRK11264 3 AIEVKNlVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarsLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 -MRKSIAVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRL----KERFNQRggTMSGGEQQMLAIGRAL 148
Cdd:PRK11264 82 qLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVglagKETSYPR--RLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-225 |
1.19e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiimrksiaVV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH------------VP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRV---------FARLTVEENLAMGGFF--TEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:PRK09452 83 AENRHVntvfqsyalFPHMTVFENVAFGLRMqkTPAAEITPRVMEALRMV-QLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-227 |
1.28e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.77 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSiimRKSIAVV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR---DRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGgfFT-----EKADYQEQMDKVLQL-----FPRLKERFNQRggtMSGGEQQMLAIGRALMSK 151
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG--LTvlprrERPNAAAIKAKVTQLlemvqLAHLADRYPAQ---LSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-215 |
1.59e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH---SGSIRYMGEELVGLEssiimrks 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 iavvPEGRRV---------FARLTVEENLAMGgfFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGR 146
Cdd:COG4136 73 ----AEQRRIgilfqddllFPHLSVGENLAFA--LPPTIGRAQRRARVEQALEEagLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIV-EQLRRDGVTVFLVEQnanqalkvaDRAYVLENGRVVMQG 215
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTH---------DEEDAPAAGRVLDLG 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-202 |
1.70e-24 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 96.15 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSIIMRKSIAVV 81
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnskKASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGFFTE--KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKlsKKEKREKKKEALEKV-GLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQAlKVADR 202
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADR 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
1.81e-24 |
|
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: 96.06 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSP--RAHSGSIRYMGEELVGLEssiimrksia 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLP---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 vvpegrrvfarltVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFnqrggtmSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03217 71 -------------PEERARLGIFLAFQYPPEIPGVKNADFLRYVNEGF-------SGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKV-ADRAYVLENGRVVMQGtGEELL 221
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELA 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-221 |
4.79e-24 |
|
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: 96.02 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvGLESSIIMRKSIA 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERFNQ----RGGTMSGGEQQMLAIGRALMSKPK 153
Cdd:cd03252 80 VVLQENVLFNR-SIRDNIALAdpGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 154 LLLLDEPSLGL----APIIIQQIFEIVeqlrrDGVTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:cd03252 159 ILIFDEATSALdyesEHAIMRNMHDIC-----AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
5.26e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHS-----GSIRYMGEELVGLESSI-IMR 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 76 KSIAVVPEGRRVFArLTVEENLAMG----GFF--TEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGvkivGWRpkLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKVAD-RAYVLEN----GRVVMQGTGEELL-- 221
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDfTAFFKGNenriGQLVEFGLTKKIFns 246
|
....*...
gi 492048676 222 -VDPKVRD 228
Cdd:PRK14258 247 pHDSRTRE 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-212 |
1.19e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTF-YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:COG3845 258 LEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRR---VFARLTVEENLAMGGFFTEKadYQE----QMDKVLQLFPRLKERF-------NQRGGTMSGGEQQMLAIGR 146
Cdd:COG3845 338 IPEDRLgrgLVPDMSVAENLILGRYRRPP--FSRggflDRKAIRAFAEELIEEFdvrtpgpDTPARSLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 147 ALMSKPKLLLLDEPSLGL---ApiiIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLdvgA---IEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
1.33e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL-ESSiiMRKSI 78
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAA--LRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGgffTEKADyQEQM---------DKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLA---APNAS-DEALievlqqvglEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGvTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-224 |
1.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRyMGEELVGLESS----IIMRKSIAVV---PEgRRVF 88
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVITAGKKnkklKPLRKKVGIVfqfPE-HQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ARlTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAP 166
Cdd:PRK13634 100 EE-TVEKDICFGpmNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 167 IIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-221 |
1.94e-23 |
|
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: 97.90 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRkSIA 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR-HIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLAMggfFTEkADyqeqMDKVLQ---------LFPRLKERFN----QRGGTMSGGEQQMLAIGR 146
Cdd:COG4618 410 YLPQDVELFDG-TIAENIAR---FGD-AD----PEKVVAaaklagvheMILRLPDGYDtrigEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-219 |
2.48e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK-----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-MR 75
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 76 KSIAVV---PEgRRVFARlTVEENLAMG----GFFTE--KADYQEQMDKVLQLFPRLKER--FNqrggtMSGGEQQMLAI 144
Cdd:PRK13637 83 KKVGLVfqyPE-YQLFEE-TIEKDIAFGpinlGLSEEeiENRVKRAMNIVGLDYEDYKDKspFE-----LSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEE 219
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-221 |
2.72e-23 |
|
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: 93.83 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG-KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKSI 78
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDS---LRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGgffTEKADYQEQMD--KVLQLFPRLkERFNQ--------RGGTMSGGEQQMLAIGRAL 148
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYG---RPDATDEEVIEaaKAAQIHDKI-MRFPDgydtivgeRGLKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRdGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELL 221
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-215 |
3.54e-23 |
|
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: 93.55 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeeLVGLESSIIMRKSIAVVpEGRR--VF 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVV-FGQKtqLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ARLTVEENLAMGG--FFTEKADYQEQMDKV---LQLFPRLKERFNQrggtMSGGEQQMLAIGRALMSKPKLLLLDEPSLG 163
Cdd:cd03267 108 WDLPVIDSFYLLAaiYDLPPARFKKRLDELselLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492048676 164 LAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
3.95e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 10 FYGKiQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGsIRYMGEELVGLESSIIMRKSIAVVPEGRRVFA 89
Cdd:PRK14271 31 FAGK-TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 90 R-----LTVEENLaMGGFFTEKADYQEQMDKVLQ-------LFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK14271 109 RpnpfpMSIMDNV-LAGVRAHKLVPRKEFRGVAQarltevgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLrRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-215 |
5.95e-23 |
|
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: 91.84 E-value: 5.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 8 STFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH--SGSIRYMGEELvgleSSIIMRKSIAVVPEGR 85
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL----DKRSFRKIIGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 86 RVFARLTVEENLamggfftekaDYQEQMdkvlqlfprlkerfnqRGgtMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLA 165
Cdd:cd03213 92 ILHPTLTVRETL----------MFAAKL----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 166 PIIIQQIFEIVEQLRRDGVTV-FLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIiCSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-227 |
8.38e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.71 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 6 NVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrYMGEELVG-LESSiimRKSIAVVPEG 84
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNdVPPA---ERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 RRVFARLTVEENLAMGGFF--TEKADYQ---EQMDKVLQLfPRLKERfnqRGGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLagAKKEEINqrvNQVAEVLQL-AHLLDR---KPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 160 PSLGL-APIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK11000 160 PLSNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-221 |
8.43e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRK---- 76
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 -SIAVVPEGrrvfarLTVEENLAMG--------GFFTEK--ADYQEQMDKVlqlfpRLKERFNQRGGTMSGGEQQMLAIG 145
Cdd:PRK11231 82 pQHHLTPEG------ITVRELVAYGrspwlslwGRLSAEdnARVNQAMEQT-----RINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 146 RALMSKPKLLLLDEPSLGLApiIIQQI--FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD--INHQVelMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-220 |
1.14e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvGLESSIIMRKSIAVV---PEGRRVFArl 91
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWDVRRQVGMVfqnPDNQFVGA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 TVEENLAMG----GffTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPI 167
Cdd:PRK13635 98 TVQDDVAFGleniG--VPREEMVERVDQALRQV-GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 168 IIQQIFEIVEQLRRD-GVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK13635 175 GRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
1.49e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS----------------------TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSI 58
Cdd:COG1134 4 MIEVENVSksyrlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 59 RYMGE--ELVGLessiimrkSIAVVPEgrrvfarLTVEEN-----LAMGgfFTeKADYQEQMDKVLQlFPRLKERFNQRG 131
Cdd:COG1134 84 EVNGRvsALLEL--------GAGFHPE-------LTGRENiylngRLLG--LS-RKEIDEKFDEIVE-FAELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 132 GTMSGGEQQMLAIGRALMSKPKLLLLDEpslGLA---PIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLEN 208
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDE---VLAvgdAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
250
....*....|.
gi 492048676 209 GRVVMQGTGEE 219
Cdd:COG1134 222 GRLVMDGDPEE 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
2.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRKSI 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT-ISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVV---PEGRrvFARLTVEENLA------------MGGFFTEKADyQEQMDKVLQlfprlKERFNqrggtMSGGEQQMLA 143
Cdd:PRK13632 86 GIIfqnPDNQ--FIGATVEDDIAfglenkkvppkkMKDIIDDLAK-KVGMEDYLD-----KEPQN-----LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 144 IGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGV-TVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELLV 222
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
....
gi 492048676 223 DPKV 226
Cdd:PRK13632 232 NKEI 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
3.38e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsIAV 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGF------FTeKADYQ--EQMDKVLQLFPrLKERFNqrgGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFpyskgrLT-AEDREiiDEAIAYLDLED-LADRYL---DELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPslgLAPIIIQQIFEIVEQLRR----DGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRD 228
Cdd:COG4604 155 DYVLLDEP---LNNLDMKHSVQMMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSD 231
|
..
gi 492048676 229 AY 230
Cdd:COG4604 232 IY 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-209 |
3.78e-22 |
|
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: 90.60 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELV--GLESsiimrksiAVVPEGRRVFARLTVE 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDR--------MVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 95 ENLAMG----GFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPI--- 167
Cdd:TIGR01184 73 ENIALAvdrvLPDLSKSERRAIVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALtrg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492048676 168 -IIQQIFEIVEQlrrDGVTVFLVEQNANQALKVADRAYVLENG 209
Cdd:TIGR01184 152 nLQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-227 |
5.56e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRkSIAVV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQR-DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEEN----LAMGGffTEKADYQEQMDKVLQL--FPRLKERF-NQrggtMSGGEQQMLAIGRALMSKPKL 154
Cdd:PRK11432 84 FQSYALFPHMSLGENvgygLKMLG--VPKEERKQRVKEALELvdLAGFEDRYvDQ----ISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVR 227
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-225 |
6.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG-----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL---VGLESSII 73
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVV---PEGRrVFARlTVEENLAMG----GFFTEKAdyQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGR 146
Cdd:PRK13641 83 LRKKVSLVfqfPEAQ-LFEN-TVLKDVEFGpknfGFSEDEA--KEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
8.72e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.30 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 14 IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYM----------GEELVGLESSIIMR---KSIAV 80
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktKEKEKVLEKLVIQKtrfKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRR----VFA-------RLTVEENLAMG--GFFTEKADYQEQMDKVLQLFPrLKERFNQRGG-TMSGGEQQMLAIGR 146
Cdd:PRK13651 100 IKEIRRrvgvVFQfaeyqlfEQTIEKDIIFGpvSMGVSKEEAKKRAAKYIELVG-LDESYLQRSPfELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-227 |
8.73e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.12 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGsirymgEELVGlessiimRKSIAVV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAG-------TAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVF---ARL----TVEENLAMGgfftEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:PRK11247 80 REDTRLMfqdARLlpwkKVIDNVGLG----LKGQWRDAALQALAAVG-LADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 155 LLLDEPsLG----LAPIIIQQIfeIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVvmqgtGEELLVD---PKVR 227
Cdd:PRK11247 155 LLLDEP-LGaldaLTRIEMQDL--IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-----GLDLTVDlprPRRR 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
1.08e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-MRKSIA 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLaLRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VV---PEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPrlKERFNQRG-GTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK13638 81 TVfqdPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-210 |
1.30e-21 |
|
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: 88.68 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK-----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRymgeelvglessiiMRK 76
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--------------VPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEgrrvFARL---TVEENLAMGGFFtEKADYQE-----QMDKVLQLFP-RLKERFNQRGGTMSGGEQQMLAIGRA 147
Cdd:cd03250 67 SIAYVSQ----EPWIqngTIRENILFGKPF-DEERYEKvikacALEPDLEILPdGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 148 LMSKPKLLLLDEPSLGLAPIIIQQIFE-IVEQLRRDGVTVFLVEQNAnQALKVADRAYVLENGR 210
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRKSIAV 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 V---PEGRrVFArLTVEENLAMGGFFTE--KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK13647 84 VfqdPDDQ-VFS-STVWDDVAFGPVNMGldKDEVERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGtGEELLVDPKV 226
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-221 |
1.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYG-----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRyMGEELVGLESSII-- 73
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIVVSSTSKQKei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 --MRKSIAVV---PEGRrVFARlTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGR 146
Cdd:PRK13643 80 kpVRKKVGVVfqfPESQ-LFEE-TVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-212 |
2.05e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.77 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 9 TFYGkIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG-SPRA-HSGSIRYMGEE--LVGLESS-----IIMRKSIA 79
Cdd:NF040905 10 TFPG-VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGsYEGEILFDGEVcrFKDIRDSealgiVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEgrrvfarLTVEENLAMGgffTEKA-----DYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:NF040905 89 LIPY-------LSIAENIFLG---NERAkrgviDWNETNRRARELLAKvgLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-215 |
7.99e-21 |
|
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: 86.82 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeelvglESSIIMRKSIAVVPEgrrvfar 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLGGGFNPE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 LTVEENLAMGGFF--TEKADYQEQMDKVLQlFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEpSLGLAPII 168
Cdd:cd03220 99 LTGRENIYLNGRLlgLSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-VLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492048676 169 IQQ-IFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03220 177 FQEkCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-202 |
9.41e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 9.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY--GKIQA--LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSI---I 73
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQmDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEIN-SRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVeqnANQALKVADR 202
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-189 |
1.07e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeelvglessiimRKSIAVVPEGRRVFAR 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 L--TVEENLAMGGF----------FTEKADYQEQMDKVlqlfpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLD 158
Cdd:NF040873 70 LplTVRDLVAMGRWarrglwrrltRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|.
gi 492048676 159 EPSLGLAPIIIQQIFEIVEQLRRDGVTVFLV 189
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
1.10e-20 |
|
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: 86.39 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLEssiIMRKS 77
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIskIGLH---DLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARlTVEENLAmggFFTEKADyqEQMDKVLQLFpRLKERFNQ-----------RGGTMSGGEQQMLAIGR 146
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLD---PFGEYSD--EELWQALERV-GLKEFVESlpggldtvveeGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQNANQALKvADRAYVLENGRVVMQGT 216
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKD-CTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-214 |
1.27e-20 |
|
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: 87.17 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL--ESSIIMRKSIAVVPEG--RRV 87
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQRRAFRRDVQLVFQDspSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 88 FARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLK---ERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL 164
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGlrsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 165 APIIIQQIFEIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVVMQ 214
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLfITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-215 |
1.61e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGspRAHSGSIRYmGEELV-GLESSI-IMRKSIAVVPEGRRVFARLT 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTS-GQILFnGQPRKPdQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 93 VEE------NLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGtMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAP 166
Cdd:cd03234 98 VREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492048676 167 IIIQQIFEIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-224 |
1.71e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 9 TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlESSIIMRKSIAVVPEG--RR 86
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQNpdDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 87 VFARlTVEENLAMG--GFFTEKADYQEQMDKVLQLF--PRLKERFNQRggtMSGGEQQMLAIGRALMSKPKLLLLDEPSL 162
Cdd:PRK13652 91 IFSP-TVEQDIAFGpiNLGLDEETVAHRVSSALHMLglEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 163 GLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-219 |
2.10e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLEssiimrKSIAVVPEGRR---VF--ARL--- 91
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAE------KGICLPPEKRRigyVFqdARLfph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 -TVEENLAMGgfftEKADYQEQMDKVLQLF---PRLKeRFNqrgGTMSGGEQQMLAIGRALMSKPKLLLLDEPslgLAPI 167
Cdd:PRK11144 91 yKVRGNLRYG----MAKSMVAQFDKIVALLgiePLLD-RYP---GSLSGGEKQRVAIGRALLTAPELLLMDEP---LASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 168 II---QQIFEIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVVMQGTGEE 219
Cdd:PRK11144 160 DLprkRELLPYLERLAREINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-221 |
2.19e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.58 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsIAVV 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVFARLTVEENLAMGGF-----FTE-KADYQEQMDKVLQLfPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYphqplFTRwRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 156 LLDEPSLGLApiIIQQI--FEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK10253 166 LLDEPTTWLD--ISHQIdlLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-215 |
2.61e-20 |
|
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: 86.16 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH--SGSIRYMGEELVGLESSIIMRKSIA 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELEPDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 V-------VP------------EGRRvfaRLTVEENLAMGGFFTEkadyQEQMDKVLQLFPRLKERFNQRGgtMSGGEQQ 140
Cdd:TIGR01978 81 LafqypeeIPgvsnleflrsalNARR---SARGEEPLDLLDFEKL----LKEKLALLDMDEEFLNRSVNEG--FSGGEKK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 141 MLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNAN--QALKvADRAYVLENGRVVMQG 215
Cdd:TIGR01978 152 RNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRllNYIK-PDYVHVLLDGRIVKSG 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-225 |
3.28e-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: 88.59 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCgspR--AHSGSIRYMGEELVGLESSII--MRKSIAVV---Peg 84
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALL---RliPSEGEIRFDGQDLDGLSRRALrpLRRRMQVVfqdP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 rrvFA----RLTVEENLAMG-GFFTEKADYQEQMDKVLQLF------PRLKER----FnqrggtmSGGEQQMLAIGRALM 149
Cdd:COG4172 372 ---FGslspRMTVGQIIAEGlRVHGPGLSAAERRARVAEALeevgldPAARHRypheF-------SGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNanqaLKV----ADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHD----LAVvralAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
.
gi 492048676 225 K 225
Cdd:COG4172 518 Q 518
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
3.53e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.44 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII-MRKSI 78
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVV---PEGRRVFArlTVEENLAMGGFFTE--KADYQEQMDKVLQL--FPRLKerfNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:PRK13636 85 GMVfqdPDNQLFSA--SVYQDVSFGAVNLKlpEDEVRKRVDNALKRtgIEHLK---DKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKV 226
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-221 |
4.41e-20 |
|
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: 88.26 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG-KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIiMRKSIAV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARlTVEENLAMGGffTEKADyQEQMDKVLQL---------FPR-LKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGA--KENVS-QDEIWAACEIaeikddienMPLgYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDgvTVFLVEQNANQAlKVADRAYVLENGRVVMQGTGEELL 221
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-221 |
6.64e-20 |
|
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: 84.90 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 4 FENVSTFY---GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG--SPRahSGSIRYMGEELVGLESSIImRKSI 78
Cdd:cd03249 3 FKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERfyDPT--SGEILLDGVDIRDLNLRWL-RSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGGFFT-----EKADYQEQMDKVLQLFPrlkERFN----QRGGTMSGGEQQMLAIGRALM 149
Cdd:cd03249 80 GLVSQEPVLFDG-TIAENIRYGKPDAtdeevEEAAKKANIHDFIMSLP---DGYDtlvgERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNAnqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLS--TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-221 |
6.90e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.75 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRR---VFARLTV 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAM--------GGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLA 165
Cdd:PRK10762 348 KENMSLtalryfsrAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 166 PIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV-----VMQGTGEELL 221
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
8.39e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiimrk 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 siavvPEGRR--VFAR------LTVEENLAMGGFFT--EKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGR 146
Cdd:COG4525 74 -----PGADRgvVFQKdallpwLNVLDNVAFGLRLRgvPKAERRARAEELLALV-GLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLEN--GRVV 212
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-224 |
1.35e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.21 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGE-----ELVGL---ESSI 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALseaERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRKSIAVVPEGRRVFARLTV-------EENLAMG----GFFTEKAdyQEQMDKVlQLFPrlkERFNQRGGTMSGGEQQM 141
Cdd:PRK11701 86 LLRTEWGFVHQHPRDGLRMQVsaggnigERLMAVGarhyGDIRATA--GDWLERV-EIDA---ARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 142 LAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
....
gi 492048676 221 LVDP 224
Cdd:PRK11701 240 LDDP 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-209 |
1.77e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELV------GLESSI-I 73
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpksSQEAGIgI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVVPEgrrvfarLTVEENLAMGGFFTEK---ADYQEQMDKVLQLFPRLKERFN--QRGGTMSGGEQQMLAIGRAL 148
Cdd:PRK10762 84 IHQELNLIPQ-------LTIAENIFLGREFVNRfgrIDWKKMYAEADKLLARLNLRFSsdKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENG 209
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-216 |
2.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG-----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELV-GLESSII-- 73
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVV---PEGRrVFARlTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:PRK13649 83 IRKKVGLVfqfPESQ-LFEE-TVLKDVAFGpqNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGT 216
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-166 |
3.58e-19 |
|
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: 85.49 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIAV 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV-RRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARlTVEENLAMGGffTEKADyqEQMDKVLQ----------LFPRLKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLAR--PDATD--EELWAALErvgladwlraLPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170
....*....|....*.
gi 492048676 151 KPKLLLLDEPSLGLAP 166
Cdd:TIGR02868 489 DAPILLLDEPTEHLDA 504
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-221 |
4.05e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSpRAHSGSIRYMGEELVGLESSIIMRKSiAVVPEGRRVFARLTVEEN 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR-AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMGGFFTEKADYQEQ-MDKV---LQLFPRLKERFNQrggtMSGGEQQ-------MLAIGRALMSKPKLLLLDEPSLGLA 165
Cdd:COG4138 90 LALHQPAGASSEAVEQlLAQLaeaLGLEDKLSRPLTQ----LSGGEWQrvrlaavLLQVWPTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 166 piIIQQI--FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG4138 166 --VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
11-220 |
4.78e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.40 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAG--KSTLLMTLCGsPRAHSGSIRYMgeelVGLESSIIMRKSIAV---VPEGR 85
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-PDAGRRPWRF*----TWCANRRALRRTIG*hrpVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 86 RvfARLTVEENLAMGGFFTE--KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLG 163
Cdd:NF000106 98 R--ESFSGRENLYMIGR*LDlsRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 164 LAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-221 |
4.96e-19 |
|
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: 85.15 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYG--KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLcgsPRAH---SGSIRYMGEEL--VGLESsiiM 74
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRFYepdSGQILLDGHDLadYTLAS---L 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVVPEGRRVFARlTVEENLAMGGffTEKADYQE---------QMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIG 145
Cdd:TIGR02203 405 RRQVALVSQDVVLFND-TIANNIAYGR--TEQADRAEieralaaayAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 146 RALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTvfLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-221 |
6.30e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElvglessiiMRKS------- 77
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD---------MADArhrravc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 --IAVVPE--GRRVFARLTVEENLAmggFFT-----EKADYQEQMDKVLQ---LFPrlkerFNQR-GGTMSGGEQQMLAI 144
Cdd:NF033858 76 prIAYMPQglGKNLYPTLSVFENLD---FFGrlfgqDAAERRRRIDELLRatgLAP-----FADRpAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLR--RDGVTVFlveqnanqalkVADrAYVLE-----------NGRV 211
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRaeRPGMSVL-----------VAT-AYMEEaerfdwlvamdAGRV 215
|
250
....*....|
gi 492048676 212 VMQGTGEELL 221
Cdd:NF033858 216 LATGTPAELL 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-225 |
7.45e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS------------IIMRKSI 78
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGG---TMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
8.55e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS-TFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrYMGEELVG-LESSiimRKSI 78
Cdd:PRK11650 3 GLKLQAVRkSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVNeLEPA---DRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARLTVEENLAMG----GffTEKADYQEQMDKV---LQLFPRLKERFNQrggtMSGGEQQMLAIGRALMSK 151
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGlkirG--MPKAEIEERVAEAariLELEPLLDRKPRE----LSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 152 PKLLLLDEPSLGL-APIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK11650 153 PAVFLFDEPLSNLdAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-227 |
1.01e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSIAVVPEGRRVFARLTVEENL 97
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 98 AMGgfFTEKADYQEQmdkVLQLFPRLK-ERFNQRGGT------MSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQ 170
Cdd:PRK11831 106 AYP--LREHTQLPAP---LLHSTVMMKlEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 171 QIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLV--DPKVR 227
Cdd:PRK11831 181 VLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRVR 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-212 |
1.22e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY----GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLES---SII 73
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVVPEGRRVFARLTVEENLAMGGFF--TEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYagLERKQRLLRAQELLQRLG-LEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKvADRAYVLENGRVV 212
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-221 |
1.97e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH--SGSIRYMGEELVGLEssiimrksiavvPEGRrvfARL--- 91
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILELS------------PDER---ARAgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 ------------TVEE--NLAMGGFFTEKADYQEQMDKVLQLFPRLK--ERFNQRG--GTMSGGEQ------QMLAIgra 147
Cdd:COG0396 81 lafqypveipgvSVSNflRTALNARRGEELSAREFLKLLKEKMKELGldEDFLDRYvnEGFSGGEKkrneilQMLLL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 148 lmsKPKLLLLDEPSLGL---ApiiIQQIFEIVEQLRRDGVTVFLVEQnaNQAL---KVADRAYVLENGRVVMQGtGEELL 221
Cdd:COG0396 158 ---EPKLAILDETDSGLdidA---LRIVAEGVNKLRSPDRGILIITH--YQRIldyIKPDFVHVLVDGRIVKSG-GKELA 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-223 |
1.98e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRRVFArLTVEENLAM 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSG-LYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 100 G---------GFFTEKAdyqeQMDKVLQLFPR-LKERFN---QRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAP 166
Cdd:PRK15439 361 NvcalthnrrGFWIKPA----RENAVLERYRRaLNIKFNhaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 167 IIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
2.11e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRR---VFARLTVEEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAM--------GGFFTEKADYQEQMDKVLQLFpRLKER-FNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPI 167
Cdd:PRK11288 352 INIsarrhhlrAGCLINNRWEAENADRFIRSL-NIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492048676 168 IIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVV 212
Cdd:PRK11288 431 AKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-211 |
2.35e-18 |
|
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: 83.34 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY---GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGS-PRAHSGSIRYMGEELVGLESSIIMRK 76
Cdd:TIGR02633 257 ILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRR---VFARLTVEENLAMGGF----FTEKADYQEQMDKVLQLFPRLKERFNQRG---GTMSGGEQQMLAIGR 146
Cdd:TIGR02633 337 GIAMVPEDRKrhgIVPILGVGKNITLSVLksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFlpiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-211 |
2.78e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRR---VFARLTVEEN 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMG------------GFFTEK--ADYQEQMDKVLQlfprLK-ERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:PRK09700 362 MAISrslkdggykgamGLFHEVdeQRTAENQRELLA----LKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492048676 162 LGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-225 |
2.90e-18 |
|
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: 82.81 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK----IQALHSVNVDVRQGEIVTLIGANGAGKS-TLL--MTLCGSPRAH-SGSIRYMGEELVGLeSSI 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALsiLRLLPDPAAHpSGSILFDGQDLLGL-SER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRK----SIAVV---------PegrrVFarlTVEENLA--------MGGfftekadyQEQMDKVLQLF-----PRLKER 126
Cdd:COG4172 85 ELRRirgnRIAMIfqepmtslnP----LH---TIGKQIAevlrlhrgLSG--------AAARARALELLervgiPDPERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 127 FNQRGGTMSGGEQQ--MLAIgrALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRA 203
Cdd:COG4172 150 LDAYPHQLSGGQRQrvMIAM--ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRV 227
|
250 260
....*....|....*....|..
gi 492048676 204 YVLENGRVVMQGTGEELLVDPK 225
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAAPQ 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-216 |
3.04e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.14 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvglESSI-IMRKSIAVVPEGRRVFARLTVE 94
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLdAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 95 ENL----AMGGFFTEKAdyQEQMDKVLQlFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQ 170
Cdd:TIGR01257 1022 EHIlfyaQLKGRSWEEA--QLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492048676 171 QIFEIVEQLrRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGT 216
Cdd:TIGR01257 1099 SIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-211 |
3.07e-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: 78.80 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQA--LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIImRKSIA 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 VVPEGRRVFARlTVEENLamggfftekadyqeqmdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:cd03246 80 YLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANqALKVADRAYVLENGRV 211
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.13e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYG-----KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIR----YMGEELVGLESS 71
Cdd:PRK13631 21 ILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 72 II-----------MRKSIAVV---PEgRRVFaRLTVEENLAMG--GFFTEKADYQEQMDKVLQLFPrLKERFNQRGG-TM 134
Cdd:PRK13631 101 TNpyskkiknfkeLRRRVSMVfqfPE-YQLF-KDTIEKDIMFGpvALGVKKSEAKKLAKFYLNKMG-LDDSYLERSPfGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 135 SGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQ 214
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|
gi 492048676 215 GTGEELLVDP 224
Cdd:PRK13631 258 GTPYEIFTDQ 267
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-232 |
3.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK-----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVG-LESSII-- 73
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIrp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 MRKSIAVV---PEGRrVFARlTVEENLAMG--GFfteKADYQEQMDKVLQL-----FPRlkERFNQRGGTMSGGEQQMLA 143
Cdd:PRK13646 83 VRKRIGMVfqfPESQ-LFED-TVEREIIFGpkNF---KMNLDEVKNYAHRLlmdlgFSR--DVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 144 IGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLV 222
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
250
....*....|.
gi 492048676 223 D-PKVRDAYLG 232
Cdd:PRK13646 236 DkKKLADWHIG 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-225 |
7.81e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 10 FYGKIQALHSVN-VDVR--QGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLE--------SSIIM---- 74
Cdd:PRK15079 27 FWQPPKTLKAVDgVTLRlyEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewravrSDIQMifqd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 -------RKSIA-VVPEGRRVF-ARLTVEEnlamggfftEKADYQEQMDKVlQLFPRLKERFNQRggtMSGGEQQMLAIG 145
Cdd:PRK15079 107 plaslnpRMTIGeIIAEPLRTYhPKLSRQE---------VKDRVKAMMLKV-GLLPNLINRYPHE---FSGGQCQRIGIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 146 RALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
.
gi 492048676 225 K 225
Cdd:PRK15079 254 L 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-160 |
9.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYmGEELvglessiimrkSIAV 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVF-ARLTVEENLamggfftekADYQEQMDKV-----LQ--LFPRlkERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:COG0488 383 FDQHQEELdPDKTVLDEL---------RDGAPGGTEQevrgyLGrfLFSG--DDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
....*...
gi 492048676 153 KLLLLDEP 160
Cdd:COG0488 452 NVLLLDEP 459
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-230 |
1.73e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSpRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRRVFArLTVEEN 96
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAM-GGFFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQ-------MLAIGRALMSKPKLLLLDEPSLGLApiI 168
Cdd:PRK03695 90 LTLhQPDKTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLD--V 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 169 IQQ--IFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAY 230
Cdd:PRK03695 167 AQQaaLDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-160 |
1.83e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 4 FENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeelvglessiimRKSIAVVPE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 84 GRRVFARLTVEENLAMGgfFTEKADYQEQMDKVLQLFP----------RLKERFNQRGG--------------------- 132
Cdd:COG0488 69 EPPLDDDLTVLDTVLDG--DAELRALEAELEELEAKLAepdedlerlaELQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190
....*....|....*....|....*....|...
gi 492048676 133 -----TMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-221 |
2.02e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 11 YGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeeLVGLESSIIMRKSIAVVpEGRR--VF 88
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARRIGVV-FGQRsqLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ARLTVEENLAMGG--FFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGeQQMLA-IGRALMSKPKLLLLDEPSLGLA 165
Cdd:COG4586 109 WDLPAIDSFRLLKaiYRIPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMRCeLAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 166 PIIIQQIFEIVEQL-RRDGVTVFL-------VEQnanqalkVADRAYVLENGRVVMQGTGEELL 221
Cdd:COG4586 187 VVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELK 243
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-221 |
2.62e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQ-ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAV 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARlTVEENLAMGGFFTEKADYQE----QMDKVLQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDISEEQVWQAletvQLAELARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 156 LLDEPSlglAPI------IIQQIFEIVeqlrRDGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK10790 499 ILDEAT---ANIdsgteqAIQQALAAV----REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-223 |
2.72e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.16 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAVVPEG 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 RRVFARLTVEENLAMG-----GFFTekaDYQEQMDKVLQLFPRLKERFNQR--GGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGryptkGMFV---DQDKMYRDTKAIFDELDIDIDPRakVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-226 |
3.11e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY---GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsI 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGGFFTEKADYQE--QMDKVLQLFPRLKERFN----QRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:TIGR00958 558 ALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAaaKAANAHDFIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 153 KLLLLDEPSLGLApiiiQQIFEIVEQLR-RDGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELLVDPKV 226
Cdd:TIGR00958 637 RVLILDEATSALD----AECEQLLQESRsRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-224 |
3.91e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG--SPRAHSGS-IRYMGEELvGLESSIIMRK 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGllLPDDNPNSkITVDGITL-TAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVV---PEGRRVFArlTVEENLAMGgfFTEKADYQEQMDKVLQLFPR---LKERFNQRGGTMSGGEQQMLAIGRALMS 150
Cdd:PRK13640 85 KVGIVfqnPDNQFVGA--TVGDDVAFG--LENRAVPRPEMIKIVRDVLAdvgMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 151 KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQAlKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-211 |
5.41e-17 |
|
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: 76.74 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK---IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsI 78
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMG------GFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKP 152
Cdd:cd03248 91 SLVGQEPVLFAR-SLQDNIAYGlqscsfECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 153 KLLLLDEPSLGLAPIIIQQifeiVEQLRRDGV---TVFLVEQNANQALKvADRAYVLENGRV 211
Cdd:cd03248 170 QVLILDEATSALDAESEQQ----VQQALYDWPerrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-220 |
5.43e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.12 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSpRAHSGSIRYMGEELVGLESSIiMRKSIAVVPEGRRVFARlTVEENLAM 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPES-WRKHLSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 100 GgffteKADY-QEQMDKVLQL------FPRLKERFN----QRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPII 168
Cdd:PRK11174 446 G-----NPDAsDEQLQQALENawvsefLPLLPQGLDtpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492048676 169 IQQIFEIVEQLRRDGVTVFLVEQnaNQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQ--LEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-221 |
9.74e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 4 FENVSTFYGK-----IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSprahsgSIRYMGEELVG----------L 68
Cdd:PRK13645 9 LDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIVGdyaipanlkkI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 69 ESSIIMRKSIAVV---PEgRRVFARlTVEENLAMGGFFTeKADYQEQMDKVLQLFP--RLKERFNQRGG-TMSGGEQQML 142
Cdd:PRK13645 83 KEVKRLRKEIGLVfqfPE-YQLFQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKlvQLPEDYVKRSPfELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 143 AIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
1.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQ---ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVgLESSIIMRKS 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-EENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVV---PEGRRVFArlTVEENLAMG----GFftEKADYQEQMDKVLQL--FPRLKERFNQRggtMSGGEQQMLAIGRAL 148
Cdd:PRK13650 83 IGMVfqnPDNQFVGA--TVEDDVAFGlenkGI--PHEEMKERVNEALELvgMQDFKEREPAR---LSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQaLKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-220 |
2.15e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGsprahsgsirymgeELVGLE-SSIIMRKSIAVVPEGRRVFaRLTVEE 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHAEtSSVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 96 NLAMGGFFtEKADYQEQMDKV-----LQLFP-RLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIII 169
Cdd:PLN03232 698 NILFGSDF-ESERYWRAIDVTalqhdLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492048676 170 QQIFE--IVEQLRrdGVTVFLVeQNANQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PLN03232 777 HQVFDscMKDELK--GKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-212 |
3.22e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSIAVVPEGR--RVFAR 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkaFRRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 LTVEENLA--MGGFFT-EKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPI 167
Cdd:PRK10419 106 KTVREIIRepLRHLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492048676 168 IIQQIFEIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVV 212
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLfITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-223 |
3.23e-16 |
|
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: 77.15 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY-----GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRY-MGEELVGLESSIIM 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 -----RKSIAVVPEGRRVFARLTVEENL--AMG-----GFFTEKADYQEQM-----DKVLQLFPRLKErfnqrggTMSGG 137
Cdd:TIGR03269 359 grgraKRYIGILHQEYDLYPHRTVLDNLteAIGlelpdELARMKAVITLKMvgfdeEKAEEILDKYPD-------ELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 138 EQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGT 216
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*..
gi 492048676 217 GEELLVD 223
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-230 |
3.79e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsIAVVPEGRRVFARLTVEEN 96
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMG--------GFFteKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLApiI 168
Cdd:PRK10575 106 VAIGrypwhgalGRF--GAADREKVEEAISLVG-LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--I 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 169 IQQI--FEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPKVRDAY 230
Cdd:PRK10575 181 AHQVdvLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-218 |
6.98e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLessiimrksiav 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGY------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFAR--LTVEENLAMGGfFTEKADYQEQMDKV----LQLFPRLKerfnqrggtMSGGEQQMLAIGRALMSKPKL 154
Cdd:PRK09544 72 VPQKLYLDTTlpLTVNRFLRLRP-GTKKEDILPALKRVqaghLIDAPMQK---------LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLeNGRVVMQGTGE 218
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPE 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-212 |
7.14e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 73.22 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK--IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKS 77
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstIPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARlTVEENLAMggfftekadYQEQMDKvlQLFPRLkeRFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLDP---------FDEYSDE--EIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 158 DEPSlglAPIIIQQIFEIVEQLRRD--GVTVFLVeqnANQALKVA--DRAYVLENGRVV 212
Cdd:cd03369 150 DEAT---ASIDYATDALIQKTIREEftNSTILTI---AHRLRTIIdyDKILVMDAGEVK 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-211 |
1.24e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY---GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGS-PRAHSGSIRYMGEELVGLESSIIMRK 76
Cdd:PRK13549 259 ILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRR---VFARLTVEEN--LAMGGFFTEKA--DYQEQMDKVLQLFPRLKERFN---QRGGTMSGGEQQMLAIGR 146
Cdd:PRK13549 339 GIAMVPEDRKrdgIVPVMGVGKNitLAALDRFTGGSriDDAAELKTILESIQRLKVKTAspeLAIARLSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-211 |
1.43e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.15 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFygKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKSIAV 80
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRR---VFARLTVEEN---LAMGGFFTE---------KADYQEQMDKVLQLFPRLKERFnqrgGTMSGGEQQMLAIG 145
Cdd:PRK10982 328 VTEERRstgIYAYLDIGFNsliSNIRNYKNKvglldnsrmKSDTQWVIDSMRVKTPGHRTQI----GSLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 146 RALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-215 |
1.84e-15 |
|
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: 71.91 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 13 KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH---SGSIRYMGEElvGLESSIIMRKSIAVVPEGRRVFA 89
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP--YKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 90 RLTVEENLamggfftekadyqeqmDKVLQLfprlkeRFNQ--RGgtMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL--- 164
Cdd:cd03233 97 TLTVRETL----------------DFALRC------KGNEfvRG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLdss 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492048676 165 -APIIIQQIFEIVEQLRrdGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:cd03233 153 tALEILKCIRTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
2.13e-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: 74.45 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG--SPRAHSGSIRY------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 61 ----MGEELVGLESSII---------MRKSIAVVPEgrRVFARL---TVEENL--AMggfftEKADY--QEQMDKVLQLF 120
Cdd:TIGR03269 81 pcpvCGGTLEPEEVDFWnlsdklrrrIRKRIAIMLQ--RTFALYgddTVLDNVleAL-----EEIGYegKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 121 P--RLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFE-IVEQLRRDGVTVFLVEQNANQAL 197
Cdd:TIGR03269 154 EmvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 492048676 198 KVADRAYVLENGRVVMQGTGEEL 220
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-224 |
2.84e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 24 VRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL---ESSIIMRKSIAVVPEGRRVFARLTVEENLAMG 100
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 101 GFFTEKADyQEQMDKVLQLFPRLKERFNQRG--GTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIF-EIVE 177
Cdd:PRK10070 131 MELAGINA-EERREKALDALRQVGLENYAHSypDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492048676 178 QLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK10070 210 LQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-221 |
5.20e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.51 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GK-IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKS 77
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLAS---LRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARlTVEENLAM--GGFFT----EKA-------DYQEQMDKVLQLFprlkerFNQRGGTMSGGEQQMLAI 144
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYarTEQYSreqiEEAarmayamDFINKMDNGLDTV------IGENGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 145 GRALMSKPKLLLLDEPSLGL---APIIIQqifEIVEQLRRDGvTVfLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK11176 492 ARALLRDSPILILDEATSALdteSERAIQ---AALDELQKNR-TS-LVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-221 |
8.95e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMT----LCGSPRAH----SGSIRYMGEELVGLESSI 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRKSiAVVPE-GRRVFArLTVEENLAMGGFFTEK---ADYQEQMDKVLQLFPRL-KERFNQRG-GTMSGGEQQMLAIGR 146
Cdd:PRK13547 81 LARLR-AVLPQaAQPAFA-FSAREIVLLGRYPHARragALTHRDGEIAWQALALAgATALVGRDvTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 147 AL---------MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGT 216
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
....*
gi 492048676 217 GEELL 221
Cdd:PRK13547 239 PADVL 243
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-221 |
1.10e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAH---SGSIRYMGEElVGLESsiiMRKSIAVVPEGRRVFARLTV 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMP-IDAKE---MRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAMGGFFTEKADY-----QEQMDKVLQLFpRLKERFNQRGGT------MSGGEQQMLAIGRALMSKPKLLLLDEPSL 162
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVtkkekRERVDEVLQAL-GLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 163 GLAPIIIQQIFEIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-220 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK------IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIM 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 75 RKSIAVV---PEGRRVFArlTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLKERfNQRGGTMSGGEQQMLAIGRALM 149
Cdd:PRK13633 84 RNKAGMVfqnPDNQIVAT--IVEEDVAFGpeNLGIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEEL 220
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
1.68e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAV 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMGGFFTEKAdyqEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGA---VGITELCRLF-SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180
....*....|....*....|....*...
gi 492048676 161 SLGLAPIIIQQIFEIVEQLRRDGVTVFL 188
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-211 |
1.75e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 13 KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGL--ESSIIMR-KSIAVVPEGRRVFA 89
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 90 RLTVEENLAMGGFFTEKADYQEQmDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPI 167
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSR-NGAKALLEQlgLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492048676 168 IIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-223 |
2.50e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGS--------IRYMGEELVGLESSI 72
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRKSIAVVPEGRRVFARlTVEENLAMGgffTEKADYQEQMDKVLQLFPRLKERFNQrggtMSGGEQQMLAIGRALMSKP 152
Cdd:PRK10938 83 WQRNNTDMLSPGEDDTGR-TTAEIIQDE---VKDPARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 153 KLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVD 223
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-225 |
2.63e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.76 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 14 IQALHSVNVDVRQGEIVTLIGANGAGKSTL--LMTLCGSPRahSGSIRYMGEELVGLESSII--MRKSIAVV---PEG-- 84
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIETPT--GGELYYQGQDLLKADPEAQklLRQKIQIVfqnPYGsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 ---RRVFARLtvEENLAMggffTEKADYQEQMDKVLQLFPR--LKERFNQRGGTM-SGGEQQMLAIGRALMSKPKLLLLD 158
Cdd:PRK11308 106 nprKKVGQIL--EEPLLI----NTSLSAAERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 159 EPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-230 |
2.65e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKSIAVVPEGRRVFARlTV 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLDS---WRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAMGgfftEKADYQEQMDKVLQL------FPRLKERFN----QRGGTMSGGEQQMLAIGRALMSKPKLLLLDEpslG 163
Cdd:PRK10789 406 ANNIALG----RPDATQQEIEHVARLasvhddILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDD---A 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 164 LAPIIIQQIFEIVEQLR--RDGVTVfLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK-VRDAY 230
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRqwGEGRTV-IISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwYRDMY 547
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-220 |
4.40e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSirymgeelvglesSIIMRKSIAVVPEGRRVFaRLTVEEN 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA-------------SVVIRGTVAYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMGGFFT----EKADYQEQMDKVLQLFP--RLKErFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQ 170
Cdd:PLN03130 699 ILFGSPFDperyERAIDVTALQHDLDLLPggDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 171 QIFE--IVEQLRrdGVTVFLVeqnANQA--LKVADRAYVLENGRVVMQGTGEEL 220
Cdd:PLN03130 778 QVFDkcIKDELR--GKTRVLV---TNQLhfLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-225 |
6.38e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 18 HSVNVDVRQGEIVTLIGANGAGKS----TLLMTLCGSPRAHSGSIRYMGEELVGleSSIIMRKSIAVVPEGRRVFARL-- 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP--CALRGRKIATIMQNPRSAFNPLht 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 ----TVEENLAMGGFFTEKADYQ-------EQMDKVLQLFPrlkerFNqrggtMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK10418 98 mhthARETCLALGKPADDATLTAaleavglENAARVLKLYP-----FE-----MSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 161 SLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-225 |
7.87e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSIAVV---Pegrr 86
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrpLRRRMQMVfqdP---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 87 vFA----RLTVEENLAMGGFFTEKADYQEQMDKVLQLFPR--LKERFNQRGGTM-SGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:COG4608 105 -YAslnpRMTVGDIIAEPLRIHGLASKAERRERVAELLELvgLRPEHADRYPHEfSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 160 P------SlglapiiIQ-QIFEIVEQLRRD-GVT-VF------LVEQnanqalkVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:COG4608 184 PvsaldvS-------IQaQVLNLLEDLQDElGLTyLFishdlsVVRH-------ISDRVAVMYLGKIVEIAPRDELYARP 249
|
.
gi 492048676 225 K 225
Cdd:COG4608 250 L 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-221 |
1.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK---IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlESSIIMRKS 77
Cdd:PRK13642 4 ILEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVV---PEGRrvFARLTVEENLAMGgfFTEKADYQEQMDKVLQ---LFPRLKERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:PRK13642 83 IGMVfqnPDNQ--FVGATVEDDVAFG--MENQGIPREEMIKRVDealLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 152 PKLLLLDEPSLGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-232 |
1.99e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvgleSSIIMRKSIAVVPEGRRV---FARLt 92
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLVAYVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 93 VEENLAMG-----GFFTE-KADYQEQMDKVLQLFPRLKERFNQRgGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAP 166
Cdd:PRK15056 97 VEDVVMMGryghmGWLRRaKKRDRQIVTAALARVDMVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 167 IIIQQIFEIVEQLRRDGVTVFLVEQNANQALKVADRAyVLENGRVVMQGTGEELLVDPKVRDAYLG 232
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSG 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-231 |
2.39e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.89 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIimRKSIAVVPEGRRVFARLTVEE 95
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--HQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 96 NLAMggFFTEKADYQEQMDKVLQLFPR---LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQI 172
Cdd:TIGR01257 2032 HLYL--YARLRGVPAEEIEKVANWSIQslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 173 FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELlvDPKVRDAYL 231
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL--KSKFGDGYI 2166
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-221 |
2.49e-13 |
|
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: 68.69 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFY-GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKSI 78
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQAS---LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEGRRVFARlTVEENLAMGgffTEKADyQEQMDKVLQL-----F-PRLKERFN----QRGGTMSGGEQQMLAIGRAL 148
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYG---RPDAS-EEEVEAAARAaqihdFiESLPDGYDtrvgERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 149 MSKPKLLLLDEPSLGLapiiiqqifeiveqlrrDGVTvflvEQNANQALKV-------------------ADRAYVLENG 209
Cdd:COG5265 510 LKNPPILIFDEATSAL-----------------DSRT----ERAIQAALREvargrttlviahrlstivdADEILVLEAG 568
|
250
....*....|..
gi 492048676 210 RVVMQGTGEELL 221
Cdd:COG5265 569 RIVERGTHAELL 580
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-224 |
3.45e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 8 STFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTL---LMTLCGSPRAHSGSIRYMGEELVGLessiimrksiavvPEg 84
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTafaLMGLLAANGRIGGSATFNGREILNL-------------PE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 85 rRVFARLTVEEnLAMggFF----TEKADYQ---EQMDKVLQL---------------------FPRLKERFNQRGGTMSG 136
Cdd:PRK09473 89 -KELNKLRAEQ-ISM--IFqdpmTSLNPYMrvgEQLMEVLMLhkgmskaeafeesvrmldavkMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 137 GEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
....*....
gi 492048676 216 TGEELLVDP 224
Cdd:PRK09473 245 NARDVFYQP 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
4.35e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIimrksiAV 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLTVEENLAMG----GffTEKADYQEQMDKVLQLFPrLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGlqlaG--VEKMQRLEIAHQMLKKVG-LEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 157 LDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLE--NGRVV 212
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
9.17e-13 |
|
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: 63.62 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiimrksiavv 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 pegrrvfarltveenlamggfftekadYQEQmdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:cd03221 67 ---------------------------YFEQ---------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
1.66e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQA--LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrYMGEELVGLESSIIMRKSI 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVV---PEGRrvFARLTVEENLAMG--GFFTEKADYQEQMDKVLQLFPRLkERFNQRGGTMSGGEQQMLAIGRALMSKPK 153
Cdd:PRK13648 86 GIVfqnPDNQ--FVGSIVKYDVAFGleNHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 154 LLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELLVD 223
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-220 |
2.95e-12 |
|
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: 64.49 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIqaLHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsiavv 81
Cdd:cd03291 40 LFFSNLCLVGAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 pegrrvfarlTVEENLAMGGFFTE---KADYQE-QMDKVLQLFPRLKERFNQRGG-TMSGGEQQMLAIGRALMSKPKLLL 156
Cdd:cd03291 113 ----------TIKENIIFGVSYDEyryKSVVKAcQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492048676 157 LDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQaLKVADRAYVLENGRVVMQGTGEEL 220
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-209 |
3.21e-12 |
|
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: 63.50 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 14 IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRY---MGEELVGLESSIIMRKSIAVVPEgRRVFAR 90
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnkNESEPSFEATRSRNRYSVAYAAQ-KPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 LTVEENLAMGGFFTeKADYQEQMDKV-----LQLFPRLKE-RFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL 164
Cdd:cd03290 93 ATVEENITFGSPFN-KQRYKAVTDACslqpdIDLLPFGDQtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492048676 165 APIIIQQIFE--IVEQLRRDGVTVFLVEQNAnQALKVADRAYVLENG 209
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-224 |
3.22e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSP----RAHSGSIRYMGEELVGL---ESSIIMRKSIAVV--- 81
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLsprERRKIIGREIAMIfqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEG-----RRVFARLtvEENL---AMGGFFTEKADYQEQmdKVLQLFPRL-----KERFNQRGGTMSGGEQQ--MLAIgr 146
Cdd:COG4170 98 PSScldpsAKIGDQL--IEAIpswTFKGKWWQRFKWRKK--RAIELLHRVgikdhKDIMNSYPHELTEGECQkvMIAM-- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492048676 147 ALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRR-DGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
3.38e-12 |
|
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: 65.35 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGsprahsgsirymgeELVGLESSIIMRKSIAVVPEGRRVfARLTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMGGFFTEKadYQEQMDKVLQLFPRL-------KERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIII 169
Cdd:TIGR00957 719 ILFGKALNEK--YYQQVLEACALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 170 QQIFEIV---EQLRRdGVTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:TIGR00957 797 KHIFEHVigpEGVLK-NKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-209 |
5.32e-12 |
|
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: 62.26 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFEN----VSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLcgSPRAHSGSIRymGEELV-GLESSIIMRK 76
Cdd:cd03232 4 LTWKNlnytVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAGVIT--GEILInGRPLDKNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARLTVEENLamggfftekadyqeqmdkvlqlfprlkeRF--NQRGgtMSGGEQQMLAIGRALMSKPKL 154
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREAL----------------------------RFsaLLRG--LSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 155 LLLDEPSLGL----APIIIQqifeIVEQLRRDGVTVFL-VEQNANQALKVADRAYVLENG 209
Cdd:cd03232 130 LFLDEPTSGLdsqaAYNIVR----FLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-224 |
8.47e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCG----SPRAHSGSIRYMGEELVGLESsiimrksiavvPEGRRV 87
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSP-----------RERRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 88 farltVEENLAMggFFTEKA---DYQEQMDKVL-QLFP------RLKERFNQRGG-----------------------TM 134
Cdd:PRK15093 87 -----VGHNVSM--IFQEPQsclDPSERVGRQLmQNIPgwtykgRWWQRFGWRKRraiellhrvgikdhkdamrsfpyEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 135 SGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVM 213
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250
....*....|.
gi 492048676 214 QGTGEELLVDP 224
Cdd:PRK15093 240 TAPSKELVTTP 250
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-164 |
8.78e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElvglesSIIMRKSIAV 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVF--ARLTVEENLAmggFFTE-KADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK13539 76 HYLGHRNAmkPALTVAENLE---FWAAfLGGEELDIAAALEAV-GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
....*..
gi 492048676 158 DEPSLGL 164
Cdd:PRK13539 152 DEPTAAL 158
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-224 |
1.26e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKS-TLL--MTLCGSPRAH--SGSIRYMGEELVGLESSIIMR---KSIAVVPEGRR 86
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALsiLRLLPSPPVVypSGDIRFHGESLLHASEQTLRGvrgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 87 VFAR--LTVEENLA-----MGGFFTEKAdyqeqMDKVLQLFPRL-----KERFNQRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:PRK15134 103 VSLNplHTLEKQLYevlslHRGMRREAA-----RGEILNCLDRVgirqaAKRLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 155 LLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-220 |
1.65e-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: 63.39 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIqaLHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIIMRKsiavv 81
Cdd:TIGR01271 429 LFFSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPG----- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 pegrrvfarlTVEENLAMGGFFTEkADYQE-----QMDKVLQLFPRLKERFNQRGG-TMSGGEQQMLAIGRALMSKPKLL 155
Cdd:TIGR01271 502 ----------TIKDNIIFGLSYDE-YRYTSvikacQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 156 LLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNAnQALKVADRAYVLENGRVVMQGTGEEL 220
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-188 |
1.79e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 6 NVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGS-PRAHS------GSIRYMGEEL------VG-LESS 71
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhPQGYSndltlfGRRRGSGETIwdikkhIGyVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 72 IIM--RKSIAVvpegrrvfarltveENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGT-------MSGGEQQML 142
Cdd:PRK10938 345 LHLdyRVSTSV--------------RNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTadapfhsLSWGQQRLA 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492048676 143 AIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFL 188
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-219 |
2.17e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQ-ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEElVGLESSIIMRKSIAV 80
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP-VTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARLtveenLAMGGFFTEKADYQEQMDKvLQLFPRLKERFNQRGGT-MSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:PRK10522 402 VFTDFHLFDQL-----LGPEGKPANPALVEKWLER-LKMAHKLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 160 PSLGLAPiIIQQIF--EIVEQLRRDGVTVFLVEQNaNQALKVADRAYVLENGRVVmQGTGEE 219
Cdd:PRK10522 476 WAADQDP-HFRREFyqVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLS-ELTGEE 534
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-164 |
2.22e-11 |
|
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: 60.97 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSIimRKSIAVVPEGRRVFARLTVEENLAM 99
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI--ARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 100 GGFFTEKADYQEQMDKVlqlfprlkerfNQRG------GTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL 164
Cdd:cd03231 97 WHADHSDEQVEEALARV-----------GLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-225 |
2.41e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKSTL---LMTLCGSprahSGSIRYMGEELVGLESSIIM--RKSIAVV---PEGRr 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglaLLRLINS----QGEIWFDGQPLHNLNRRQLLpvRHRIQVVfqdPNSS- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 87 VFARLTVEENLAMGGFFTEK----ADYQEQMDKVLQ---LFPRLKERFNqrgGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPtlsaAQREQQVIAVMEevgLDPETRHRYP---AEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 160 PSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANQALK-VADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRaLCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-191 |
3.91e-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: 62.24 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCgspRAHS--GSIRYMGeelVGLESSIIM--RKSIAVVPEGRRVFArlt 92
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLLSteGEIQIDG---VSWNSVTLQtwRKAFGVIPQKVFIFS--- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 93 veenlamgGFFTEKADYQEQ--------------MDKVLQLFP-RLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:TIGR01271 1306 --------GTFRKNLDPYEQwsdeeiwkvaeevgLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....
gi 492048676 158 DEPSLGLAPIIIQQIFEIVEQLRRDgVTVFLVEQ 191
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEH 1410
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-160 |
5.48e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 18 HSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELvglessiimRKsiavvpeGRRVFAR------- 90
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI---------RR-------QRDEYHQdllylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 -------LTVEENLAmggFFTEKADYQEQmDKVLQLFprlkERFNQRG------GTMSGGEQQMLAIGRALMSKPKLLLL 157
Cdd:PRK13538 82 qpgikteLTALENLR---FYQRLHGPGDD-EALWEAL----AQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWIL 153
|
...
gi 492048676 158 DEP 160
Cdd:PRK13538 154 DEP 156
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-186 |
5.72e-11 |
|
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: 59.68 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 27 GEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglESSIIMRKSIAVVPEGRRVFARLTVEENLAmggFFteK 106
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHENILYLGHLPGLKPELSALENLH---FW--A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 107 ADYQEQMDKVLQLFPR--LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQ-LRRDG 183
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGG 178
|
...
gi 492048676 184 VTV 186
Cdd:TIGR01189 179 IVL 181
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-219 |
9.75e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLeSSIIMRKSIAV 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL-KPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 81 VPEGRRVFARlTVEENLAMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 161 SLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQaLKVADRAYVLENGRVVMQGTGEE 219
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDE-INHADKVITLQPHAGEMQEARYE 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-219 |
1.22e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 15 QALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSP--RAHSGSIRYMGEELVGLESSIIMRKSIAVVPEGRRVFARL- 91
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNl 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 --TVEEN--------LAMGGFFTEKADYqeqmdKVLQlfpRLKERFN-------QRGGTMSGGEQQMLAIGRALMSKPKL 154
Cdd:NF040905 354 idDIKRNitlanlgkVSRRGVIDENEEI-----KVAE---EYRKKMNiktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 155 LLLDEPSLGlapiiIQ-----QIFEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEE 219
Cdd:NF040905 426 LILDEPTRG-----IDvgakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE 490
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-221 |
1.32e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFY--GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELV--GLESsiiMRK 76
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEGRRVFARlTVEENLAMggfFTEK--ADYQEQMDK-----VLQLFP-RLKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDP---FSEHndADLWEALERahikdVIDRNPfGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 149 MSKPKLLLLDEPSLGL---APIIIQQIfeIVEQLRrdGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELL 221
Cdd:PLN03232 1387 LRRSKILVLDEATASVdvrTDSLIQRT--IREEFK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-221 |
1.34e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGK--IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKS 77
Cdd:PLN03130 1238 IKFEDVVLRYRPelPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIskFGLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 78 IAVVPEGRRVFARlTVEENLAMggfFTE--KADYQEQMDK-----VLQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALM 149
Cdd:PLN03130 1315 LGIIPQAPVLFSG-TVRFNLDP---FNEhnDADLWESLERahlkdVIRRNSLgLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 150 SKPKLLLLDEPSLGL---APIIIQQIfeIVEQLRrdGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEELL 221
Cdd:PLN03130 1391 RRSKILVLDEATAAVdvrTDALIQKT--IREEFK--SCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLL 1460
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-159 |
1.72e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYmgeelvglessiimrksiavvPEGRRVF-----ARL 91
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------------------PAGARVLflpqrPYL 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 92 ---TVEENLAMGGffTEKADYQEQMDKVLQLF--PRLKERFNQR---GGTMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:COG4178 438 plgTLREALLYPA--TAEAFSDAELREALEAVglGHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-224 |
1.73e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGsirymgeelvglesSIIMRKSIAVVPEGRRVFaRLTVEEN 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--------------RVWAERSIAYVPQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAmggFFTEK--ADYQE-----QMDKVLQLFPR-LKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPII 168
Cdd:PTZ00243 741 IL---FFDEEdaARLADavrvsQLEADLAQLGGgLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 169 IQQIFEIVEQLRRDGVTVFLVEQNANqALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVH-VVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
128-192 |
2.51e-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: 2.51e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492048676 128 NQRGGTMSGGEQQMLAIGRALMSKPK--LLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQN 192
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-189 |
3.04e-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: 57.16 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVS--TFYGKIqALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYmgeelvglessiimrksia 79
Cdd:cd03223 1 IELENLSlaTPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 vvPEGRRVFarltveenlamggFFTEKAdY------QEQM----DKVLqlfprlkerfnqrggtmSGGEQQMLAIGRALM 149
Cdd:cd03223 61 --PEGEDLL-------------FLPQRP-YlplgtlREQLiypwDDVL-----------------SGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIveqLRRDGVTVFLV 189
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQL---LKELGITVISV 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-170 |
4.14e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 21 NVD--VRQGEIVTLIGANGAGKSTLLMTLcgSPRAHSGSIRyMGEELVG---LESSiiMRKSIAVVPEGRRVFARLTVEE 95
Cdd:TIGR00956 781 NVDgwVKPGTLTALMGASGAGKTTLLNVL--AERVTTGVIT-GGDRLVNgrpLDSS--FQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 96 NLAMGGFF--------TEKADYQEQMDKVLQLfPRLKERFNQRGGTMSGGEQ-QMLAIGRALMSKPKLLL-LDEPSLGL- 164
Cdd:TIGR00956 856 SLRFSAYLrqpksvskSEKMEYVEEVIKLLEM-ESYADAVVGVPGEGLNVEQrKRLTIGVELVAKPKLLLfLDEPTSGLd 934
|
....*....
gi 492048676 165 ---APIIIQ 170
Cdd:TIGR00956 935 sqtAWSICK 943
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
4.75e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGK----IQALHSVNVDVRQGEIVTLIGANGAGKST---LLMTLCGSP-RAHSGSIRYMGEEL------- 65
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVsslAIMGLIDYPgRVMAEKLEFNGQDLqriseke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 66 ----VGLESSIIMRKSIAVVPE----GRRVFARLTVEEnlamGGffTEKADYQEQMDKVLQL-FPRLKERFNQRGGTMSG 136
Cdd:PRK11022 83 rrnlVGAEVAMIFQDPMTSLNPcytvGFQIMEAIKVHQ----GG--NKKTRRQRAIDLLNQVgIPDPASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 137 GEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQL-RRDGVTVFLVEQNANQALKVADRAYVLENGRVVMQG 215
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
250
....*....|
gi 492048676 216 TGEELLVDPK 225
Cdd:PRK11022 237 KAHDIFRAPR 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
5.61e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSP--RAHSGSIRYMGEELVGLESSIIMRKSI 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AV-------VP------------EGRRVFARLTVEENLAMGGFFTEKAdyqeqmdKVLQLFPRLKERFNQRGgtMSGGEQ 139
Cdd:CHL00131 87 FLafqypieIPgvsnadflrlayNSKRKFQGLPELDPLEFLEIINEKL-------KLVGMDPSFLSRNVNEG--FSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 140 QMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVE--QNANQALKvADRAYVLENGRVVMQGTG 217
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyQRLLDYIK-PDYVHVMQNGKIIKTGDA 236
|
.
gi 492048676 218 E 218
Cdd:CHL00131 237 E 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-211 |
6.55e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAhSGSIRYMGeelVGLESSIIM--RKSIAVVPEGRRVFARlTVE 94
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDG---VSWNSVPLQkwRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 95 ENLAMGGFFTE----KADYQEQMDKVLQLFP-RLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIII 169
Cdd:cd03289 95 KNLDPYGKWSDeeiwKVAEEVGLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492048676 170 QQIFEIVEQLRRDgVTVFLVEQNAnQALKVADRAYVLENGRV 211
Cdd:cd03289 175 QVIRKTLKQAFAD-CTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-220 |
6.57e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGleSSIIMRksiavvpegRRV---------FAR 90
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDIATR---------RRVgymsqafslYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 91 LTVEENLAMGG--FFTEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPII 168
Cdd:NF033858 354 LTVRQNLELHArlFHLPAAEIAARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492048676 169 IQQIFEIVEQL-RRDGVTVFLVEQNANQALKvADRAYVLENGRVVMQGTGEEL 220
Cdd:NF033858 433 RDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
2.04e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL--VGLESsiiMRKSIAVVPEGRRVFARlTVE 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIakIGLHD---LRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 95 ENLAMGGFFTEKA-----DYQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSlglAPIII 169
Cdd:TIGR00957 1378 MNLDPFSQYSDEEvwwalELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT---AAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492048676 170 QQIFEIVEQLRR--DGVTVFLVEQNANQALKVAdRAYVLENGRVVMQGTGEELL 221
Cdd:TIGR00957 1455 ETDNLIQSTIRTqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-161 |
3.26e-09 |
|
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: 56.33 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 23 DVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrymgeelvglessiIMRKSIAVVPEGRRVFARLTVEENL--AMG 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------------DEDLKISYKPQYISPDYDGTVEEFLrsANT 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492048676 101 GFFTEKAdYQEQMDKVLQLfprlKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:COG1245 428 DDFGSSY-YKTEIIKPLGL----EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
3.53e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 23 DVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrymgeelvglessIIMRKSIAVVPEGRRVFARLTVEENLA--MG 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------EIELDTVSYKPQYIKADYEGTVRDLLSsiTK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 101 GFFTEkADYQEQMDKVLQLFPRLKERFNqrggTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL-------APIIIQQIF 173
Cdd:cd03237 88 DFYTH-PYFKTEIAKPLQIEQILDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLdveqrlmASKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|....
gi 492048676 174 EIVEQlrrdgvTVFLVEQNANQALKVADRAYVLE 207
Cdd:cd03237 163 ENNEK------TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-160 |
3.58e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 24 VRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglessiimrksiavvpegrrvfARL----------TV 93
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIV----------------------ARLqqdpprnvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAMGgfFTEKADY------------QEQMDKVLQLFPRLKERFNQRGG-----------------------TMSGGE 138
Cdd:PRK11147 84 YDFVAEG--IEEQAEYlkryhdishlveTDPSEKNLNELAKLQEQLDHHNLwqlenrinevlaqlgldpdaalsSLSGGW 161
|
170 180
....*....|....*....|..
gi 492048676 139 QQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEP 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-233 |
3.92e-09 |
|
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: 56.17 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 128 NQRGGTMSGGEQQMLA----IGRALMSKpkLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNaNQALKVADra 203
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRlatqIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAAD-- 557
|
90 100 110
....*....|....*....|....*....|....*....
gi 492048676 204 YVLE--------NGRVVMQGTGEELLVDPK-VRDAYLGG 233
Cdd:TIGR00630 558 YVIDigpgagehGGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
4.17e-09 |
|
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: 56.10 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRyMGEELVglessiimrksIAVV 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK-----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 PEGRRVF-ARLTVEENLAMGGFFTEKADYQEQMDKVLQlfprlkeRFNQRG-------GTMSGGEQQMLAIGRALMSKPK 153
Cdd:TIGR03719 391 DQSRDALdPNKTVWEEISGGLDIIKLGKREIPSRAYVG-------RFNFKGsdqqkkvGQLSGGERNRVHLAKTLKSGGN 463
|
....*...
gi 492048676 154 LLLLDEPS 161
Cdd:TIGR03719 464 VLLLDEPT 471
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
14-224 |
4.76e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 14 IQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESS--------IIMRKSIAVVPEGR 85
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSyrsqrirmIFQDPSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 86 ---------RVFARLTVEE-------NLAMGGFFTEKADYQEQMdkvlqlfprlkerfnqrggtMSGGEQQMLAIGRALM 149
Cdd:PRK15112 106 isqildfplRLNTDLEPEQrekqiieTLRQVGLLPDHASYYPHM--------------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492048676 150 SKPKLLLLDEPSLGLAPIIIQQIFEIVEQLR-RDGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDP 224
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-65 |
5.81e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.57 E-value: 5.81e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEEL 65
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-220 |
7.16e-09 |
|
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: 55.40 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 126 RFNQRGGTMSGGEQQMLAIGRALMSK---PKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANqALKVADr 202
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTAD- 899
|
90 100
....*....|....*....|....*.
gi 492048676 203 aYVLE--------NGRVVMQGTGEEL 220
Cdd:TIGR00630 900 -YIIDlgpeggdgGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-161 |
9.16e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 24 VRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrymgeelvglESSIimrkSIAVVPEGRRVFARLTVEENLAMGGFF 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV----------DPEL----KISYKPQYIKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 104 TEKADYQEQMDKVLQLfPRLkerFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:PRK13409 428 LGSSYYKSEIIKPLQL-ERL---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-219 |
1.11e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 27 GEIVTLIGANGAGKSTLLMTLCGSPRAHS--GSIRYMGEELvgleSSIIMRKsIAVVPEGRRVFARLTVEENLAMGGFFT 104
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 105 -----EKADYQEQMDKVLQLFPRLKERFNQRGGT----MSGGEQQMLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEI 175
Cdd:PLN03211 169 lpkslTKQEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492048676 176 VEQLRRDGVTVFL-VEQNANQALKVADRAYVLENGRVVMQGTGEE 219
Cdd:PLN03211 249 LGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-221 |
1.23e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 133 TMSGGEQQMLAIGRALMSKPK--LLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNaNQALKVADRayVLE--- 207
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADR--IIDigp 552
|
90
....*....|....*....
gi 492048676 208 -----NGRVVMQGTGEELL 221
Cdd:PRK00635 553 gagifGGEVLFNGSPREFL 571
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-209 |
1.35e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 133 TMSGGEQQMLAIGRALMS---KPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANqALKVADraYVLENG 209
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVAD--YVLELG 885
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-160 |
2.59e-08 |
|
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: 53.79 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 32 LIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVG-------LESSIIMRKSI-AVVPEGRRVFARLTvEENLAMggff 103
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGylpqepqLDPTKTVRENVeEGVAEIKDALDRFN-EISAKY---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 104 tekADYQEQMDKVLQLFPRLKERFNQRGG------------------------TMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:TIGR03719 111 ---AEPDADFDKLAAEQAELQEIIDAADAwdldsqleiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
.
gi 492048676 160 P 160
Cdd:TIGR03719 188 P 188
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-215 |
4.03e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSP--RAHSGSIRYMGEELVGLESS------I 72
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdragegI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRKSIAVVPEG--RRVFARLTV--------EENLAMGGFftekADYQEQMDKVLQLFPRLKERFNQRGgtMSGGEQQML 142
Cdd:PRK09580 81 FMAFQYPVEIPGvsNQFFLQTALnavrsyrgQEPLDRFDF----QDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 143 AIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLrRDGVTVFLVEQNANQALKV--ADRAYVLENGRVVMQG 215
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-215 |
4.50e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLM-TLcgsprAHSGSIRYMG------------------EELVGLESSI-IMRK 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFdTI-----YAEGQRRYVEslsayarqflgqmdkpdvDSIEGLSPAIaIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPegrrvfaRLTVeenlamgGFFTEKADYqeqmdkVLQLFPR--LKERFNQ-------------RGGTMSGGEQQM 141
Cdd:cd03270 86 TTSRNP-------RSTV-------GTVTEIYDY------LRLLFARvgIRERLGFlvdvglgyltlsrSAPTLSGGEAQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 142 LA----IGRALMSKpkLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNaNQALKVADraYVL--------ENG 209
Cdd:cd03270 146 IRlatqIGSGLTGV--LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAAD--HVIdigpgagvHGG 220
|
....*.
gi 492048676 210 RVVMQG 215
Cdd:cd03270 221 EIVAQG 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-211 |
6.21e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 16 ALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGeelvglessiimrkSIAVVPEGRRVFARLTVEE 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------------SAALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 96 NLAMGGFFT--EKADYQEQMDKVLQlFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP-SLGlAPIIIQQI 172
Cdd:PRK13545 105 NIELKGLMMglTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKC 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 492048676 173 FEIVEQLRRDGVTVFLVEQNANQALKVADRAYVLENGRV 211
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-160 |
6.97e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGlessiimrksiavv 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIG-------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 82 pegrrVFARLTVEE-----NLA--MGGFFTEKADyqEQMdkVLQLFPRL---KERFNQRGGTMSGGEQQMLAIGRALMSK 151
Cdd:PRK15064 386 -----YYAQDHAYDfendlTLFdwMSQWRQEGDD--EQA--VRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
....*....
gi 492048676 152 PKLLLLDEP 160
Cdd:PRK15064 457 PNVLVMDEP 465
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-221 |
8.63e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 9 TFYgkiqALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEelvglessiimrksIAVVPEGRRVF 88
Cdd:PRK13546 36 TFF----ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ARLTVEEN-----LAMGgfFTEKaDYQEQMDKVLQlFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP-SL 162
Cdd:PRK13546 98 GQLTGIENiefkmLCMG--FKRK-EIKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 163 G---LAPIIIQQIFEIVEQlrrdGVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELL 221
Cdd:PRK13546 174 GdqtFAQKCLDKIYEFKEQ----NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
1.42e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIrymgeelvGLESSI-------- 72
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLAKGIklgyfaqh 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 ---IMRKSIAVVPEGRRVFARLTvEENLA--MGGF-FtekadyqeQMDKVLQlfprLKERFnqrggtmSGGEQQMLAIGR 146
Cdd:PRK10636 384 qleFLRADESPLQHLARLAPQEL-EQKLRdyLGGFgF--------QGDKVTE----ETRRF-------SGGEKARLVLAL 443
|
170
....*....|....*
gi 492048676 147 ALMSKPKLLLLDEPS 161
Cdd:PRK10636 444 IVWQRPNLLLLDEPT 458
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-221 |
1.72e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 131 GGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL----APIIIQQIFEIVEQLRRDGVTVflveQNANQALKVADRAYVL 206
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnsEKLIEKTIVDIKDKADKTIITI----AHRIASIKRSDKIVVF 1431
|
90 100
....*....|....*....|
gi 492048676 207 EN----GRVVM-QGTGEELL 221
Cdd:PTZ00265 1432 NNpdrtGSFVQaHGTHEELL 1451
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-225 |
3.68e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 13 KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVGLESSII--MRKSIAVVPEG--RRVF 88
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqaLRRDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 89 ARLTV----EENLAMGGFFTEKADyQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGL 164
Cdd:PRK10261 416 PRQTVgdsiMEPLRVHGLLPGKAA-AARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492048676 165 APIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-160 |
3.69e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 5 ENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRymgeelVG--LESSIIMRKSIAVVP 82
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH------CGtkLEVAYFDQHRAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 83 EGrrvfarlTVEENLAMGGfftekadyQEQMdkV----------LQ--LFPRLKERFNQRGgtMSGGEQQMLAIGRALMS 150
Cdd:PRK11147 397 EK-------TVMDNLAEGK--------QEVM--VngrprhvlgyLQdfLFHPKRAMTPVKA--LSGGERNRLLLARLFLK 457
|
170
....*....|
gi 492048676 151 KPKLLLLDEP 160
Cdd:PRK11147 458 PSNLLILDEP 467
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-225 |
5.22e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 12 GKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLC-------GSPRAHSGSIRYMGEELVGL--ESSIIMRK----SI 78
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagGLVQCDKMLLRRRSRQVIELseQSAAQMRHvrgaDM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 79 AVVPEG-----RRVFarlTVEENLAMGGFFTEKADYQEQMDKVLQLF-----PRLKERFNQRGGTMSGGEQQMLAIGRAL 148
Cdd:PRK10261 107 AMIFQEpmtslNPVF---TVGEQIAESIRLHQGASREEAMVEAKRMLdqvriPEAQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 149 MSKPKLLLLDEPSLGLAPIIIQQIFEIVEQLRRD-GVTVFLVEQNANQALKVADRAYVLENGRVVMQGTGEELLVDPK 225
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-190 |
3.94e-06 |
|
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: 47.09 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 25 RQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSI-----------RYMGEELVGLESSI------IMRKS--IAVVPegr 85
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDYFKKLangeikVAHKPqyVDLIP--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 86 RVFaRLTVEENLamggfftEKADYQEQMDKVLQLFpRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPSLGLA 165
Cdd:COG1245 174 KVF-KGTVRELL-------EKVDERGKLDELAEKL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*..
gi 492048676 166 piIIQQI--FEIVEQLRRDGVTVFLVE 190
Cdd:COG1245 245 --IYQRLnvARLIRELAEEGKYVLVVE 269
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
4.47e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRyMGEElVGLESSIIMRKSIA-- 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGET-VKLAYVDQSRDALDpn 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 80 -----VVPEGrrvfarltvEENLAMGGFFTEKADYQeqmdkvlqlfprlkERFNQRG-------GTMSGGEQQMLAIGRA 147
Cdd:PRK11819 403 ktvweEISGG---------LDIIKVGNREIPSRAYV--------------GRFNFKGgdqqkkvGVLSGGERNRLHLAKT 459
|
170
....*....|....
gi 492048676 148 LMSKPKLLLLDEPS 161
Cdd:PRK11819 460 LKQGGNVLLLDEPT 473
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
129-216 |
4.50e-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: 46.45 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 129 QRGGTMSGGEQQMLAIGRALmSKPK----LLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNANqALKVADraY 204
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCAD--W 240
|
90 100
....*....|....*....|
gi 492048676 205 VLE--------NGRVVMQGT 216
Cdd:cd03271 241 IIDlgpeggdgGGQVVASGT 260
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-159 |
4.55e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 20 VNVDVRQGEIVTLIGANGAGKSTLLMTLCG--SPRAHSGSIRYMGEELvGLESSIImrksiavvpegrrvfarltveENL 97
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF-GREASLI---------------------DAI 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492048676 98 AMGGFFTEKADYQEQM---DKVLqlfprLKERFNQrggtMSGGEQQMLAIGRALMSKPKLLLLDE 159
Cdd:COG2401 107 GRKGDFKDAVELLNAVglsDAVL-----WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDE 162
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-233 |
1.16e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 132 GTMSGGEQQ--MLA--IGRALMSKpkLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNAnQALKVADraYVLE 207
Cdd:COG0178 484 GTLSGGEAQriRLAtqIGSGLVGV--LYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDE-DTIRAAD--YIID 558
|
90 100 110
....*....|....*....|....*....|....*
gi 492048676 208 --------NGRVVMQGTGEELLVDPK-VRDAYLGG 233
Cdd:COG0178 559 igpgagehGGEVVAQGTPEEILKNPDsLTGQYLSG 593
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-180 |
1.52e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 13 KIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGspRAHSGSIrymgeelvglESSIimrkSIAVVPEGRRVFARL- 91
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI----------EGDI----RISGFPKKQETFARIs 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 92 -------------TVEENLAMGGF--FTEKADYQEQM---DKVLQL--FPRLKERFNQRGGT--MSGGEQQMLAIGRALM 149
Cdd:PLN03140 956 gyceqndihspqvTVRESLIYSAFlrLPKEVSKEEKMmfvDEVMELveLDNLKDAIVGLPGVtgLSTEQRKRLTIAVELV 1035
|
170 180 190
....*....|....*....|....*....|....*
gi 492048676 150 SKPKLLLLDEPSLGL----APIIIQQIFEIVEQLR 180
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLdaraAAIVMRTVRNTVDTGR 1070
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-191 |
2.21e-05 |
|
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: 44.74 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 1 MLQFENVS--TFYGKIqALHSVNVDVRQGEIVTLIGANGAGKSTLLmtlcgsprahsgsiRYMGE--ELVGLESSIIMRK 76
Cdd:TIGR00954 451 GIKFENIPlvTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLF--------------RILGElwPVYGGRLTKPAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 77 SIAVVPEgRRVFARLTVEENL--AMGGFFTEKADYQ----EQMDKVLQLfprlkERFNQRGG----------TMSGGEQQ 140
Cdd:TIGR00954 516 KLFYVPQ-RPYMTLGTLRDQIiyPDSSEDMKRRGLSdkdlEQILDNVQL-----THILEREGgwsavqdwmdVLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492048676 141 MLAIGRALMSKPKLLLLDEPSLGLAPIIIQQIFEIveqLRRDGVTVFLVEQ 191
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-161 |
2.24e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 17 LHSVNVDVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGE---ELVGLESSIIMRKSIAVVPEGRRVFARLTV 93
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 94 EENLAmggffTEKAD------------------YQEQMDKVLQLFPRLKERFNQRGGTMSGGEQQMLAIGRALMSKPKLL 155
Cdd:PRK10636 97 QLHDA-----NERNDghaiatihgkldaidawtIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
....*.
gi 492048676 156 LLDEPS 161
Cdd:PRK10636 172 LLDEPT 177
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
14-59 |
6.09e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.38 E-value: 6.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 492048676 14 IQALHSVnvdVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIR 59
Cdd:PRK01889 185 LDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-160 |
7.68e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 32 LIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVG-------LESSIIMRKSIAV-VPEGRRVFARLT-VEENLA---- 98
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGylpqepqLDPEKTVRENVEEgVAEVKAALDRFNeIYAAYAepda 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492048676 99 -MGGFFTEKADYQEQMDKV---------------LQLFPRlkerfNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEP 160
Cdd:PRK11819 118 dFDALAAEQGELQEIIDAAdawdldsqleiamdaLRCPPW-----DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-161 |
2.36e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKIQALHSVNVDVRQGEIVTLIGANGAGKSTLLMTLC-----GSPRahSGSIRYMGEELVGLESSII--- 73
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPK--NCQILHVEQEVVGDDTTALqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 74 ----MRKSIAVVPEGRRVFARLTVEENLAMG--GFFTEKADYQEQMDKVL-QLFPRLK---------------------- 124
Cdd:PLN03073 256 lntdIERTQLLEEEAQLVAQQRELEFETETGkgKGANKDGVDKDAVSQRLeEIYKRLElidaytaearaasilaglsftp 335
|
170 180 190
....*....|....*....|....*....|....*..
gi 492048676 125 ERFNQRGGTMSGGEQQMLAIGRALMSKPKLLLLDEPS 161
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-233 |
5.94e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 132 GTMSGGEQQM--LA--IGRALMSKpkLLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNaNQALKVADraYVLE 207
Cdd:PRK00349 488 GTLSGGEAQRirLAtqIGSGLTGV--LYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHD-EDTIRAAD--YIVD 562
|
90 100 110
....*....|....*....|....*....|....*
gi 492048676 208 --------NGRVVMQGTGEELLVDPK-VRDAYLGG 233
Cdd:PRK00349 563 igpgagvhGGEVVASGTPEEIMKNPNsLTGQYLSG 597
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-220 |
8.88e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 133 TMSGGEQQMLAIGRALmSKPK----LLLLDEPSLGLAPIIIQQIFEIVEQLRRDGVTVFLVEQNanqaL---KVADraYV 205
Cdd:COG0178 826 TLSGGEAQRVKLASEL-SKRStgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN----LdviKTAD--WI 898
|
90 100
....*....|....*....|...
gi 492048676 206 LE--------NGRVVMQGTGEEL 220
Cdd:COG0178 899 IDlgpeggdgGGEIVAEGTPEEV 921
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-180 |
9.74e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 2 LQFENVSTFYGKiqalhsVNVDVRQGeIVTLIGANGAGKSTLLMTLC--------GSPRAHSGSIRYMGEEL-VGLESSI 72
Cdd:COG0419 5 LRLENFRSYRDT------ETIDFDDG-LNLIVGPNGAGKSTILEAIRyalygkarSRSKLRSDLINVGSEEAsVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 73 IMRKSIAVVPEG-------------RRVFARLTVEENL--AMGGFFTEKADYQEQMDKVLQLFPRLKERFNQRGG----- 132
Cdd:COG0419 78 GGKRYRIERRQGefaefleakpserKEALKRLLGLEIYeeLKERLKELEEALESALEELAELQKLKQEILAQLSGldpie 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492048676 133 TMSGGEQQMLAIGRALMskpklLLLDEPSLGlaPIIIQQIFEIVEQLR 180
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILDFGSLD--EERLERLLDALEELA 198
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-184 |
1.08e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 30 VTLI-GANGAGKSTLL----MTLCGS------PRAHSGSIRYMGEEL--VGLESSiimrksiavVPEGRRVfarlTVEEN 96
Cdd:cd03240 24 LTLIvGQNGAGKTTIIealkYALTGElppnskGGAHDPKLIREGEVRaqVKLAFE---------NANGKKY----TITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 97 LAMggffTEKADY--QEQMDKVLQLFPrlkerfnqrgGTMSGGEQQM------LAIGRALMSKPKLLLLDEPSLGL-API 167
Cdd:cd03240 91 LAI----LENVIFchQGESNWPLLDMR----------GRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLdEEN 156
|
170
....*....|....*..
gi 492048676 168 IIQQIFEIVEQLRRDGV 184
Cdd:cd03240 157 IEESLAEIIEERKSQKN 173
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-207 |
1.19e-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: 38.71 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 23 DVRQGEIVTLIGANGAGKSTLLMTLCGSPRAHSGSIRYMGEELVglessiimrksiavvpegrrvfarltveenlamggf 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492048676 103 ftekadYQEQMDKvlqlfprlkerfnqrggtMSGGEQQMLAIGRALMSKPKLLLLDEPSlglAPIIIQQIFEIVEQLRR- 181
Cdd:cd03222 65 ------YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPS---AYLDIEQRLNAARAIRRl 117
|
170 180
....*....|....*....|....*....
gi 492048676 182 ---DGVTVFLVEQNANQALKVADRAYVLE 207
Cdd:cd03222 118 seeGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-164 |
1.65e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|.
gi 492048676 134 MSGGEQQMLAIGRALMSKPKLLLLDEPSLGL 164
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
210-233 |
5.77e-03 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 33.38 E-value: 5.77e-03
|
| |
